Creative Enzymes - Products

Enzyme manufacturing for life science research and medicines, food, alcohol, fabric, paper etc. Uses include: drug discovery, cancer and infectious disease research, microbiology and personalized medicine.

Product	Description	Suppliers Website
Native Bacteria Achromopeptidase Quick inquiry Where to buy	Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus. Hemolysins are lipids and proteins that cause lysis of red blood cells by destroying their cell membrane. although the lytic activity of some microbe-derived hemolysins on red blood cells may be of great importance for nutrient acquisition, many hemolysins produced by pathogens do not cause significant destruction of red blood cells during infe...and the effect of ciprofloxacin on biofilm formation. Group: Enzymes. Synonyms: Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. Mole weight: ~27 kDa. Activity: > 1,000 units/mg solid; > 20,000 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Bacteria. Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Cat No: NATE-0022.
Native Bacterial Environmental DNA Glucan elongation enzyme Quick inquiry Where to buy	A thermostable 4-α-glucanotransferase that elongates linear alpha-glucan chains in starch and amylose by catalyzing the transfer of one glucose unit from the non-reducing end to a new position in an acceptor, which may be triose or larger. The enzyme can be used various applications, such as for modifications of alpha-polysaccharides and is ideal for making clear size ladders of oligosaccharides larger than maltose. The enzyme was developed from metagenome DNA obtained from environmental sample from a geothermal environment. The enzyme catalyzes the formation of the alpha-1,4-glucosidic linkages. the enzyme transfers a segment of a (1->4)-alpha-d-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-d-glucan. Group: Enzymes. Synonyms: Glucan elongation enzyme. Glucan elongation enzyme. Source: Bacterial Environmental DNA. Glucan elongation enzyme. Cat No: NATE-0302.
Native Bacteria Maltose phosphorylase Quick inquiry Where to buy	Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose. Group: Enzymes. Synonyms: maltose phosphorylase; maltose:phosphate 1-β-D-glucosyltransferase; EC 2.4.1.8; 9030-19-7; MP. Enzyme Commission Number: EC 2.4.1.8. CAS No. 9030-19-7. MP. Activity: > 5 units/mg protein (at 25°C and pH 7.5). Storage: 0 -5°C. Form: Ammonium sulfate suspension. Source: Bacteria. maltose phosphorylase; maltose:phosphate 1-β-D-glucosyltransferase; EC 2.4.1.8; 9030-19-7; MP. Cat No: NATE-1031.
Native Bacterium cadaveris L-Lysine Decarboxylase Quick inquiry Where to buy	Lysine decarboxylase is an enzyme that converts lysine to cadaverine. Group: Enzymes. Synonyms: Lysine decarboxylase; EC 4.1.1.18; 9024-76-4; L-lysine carboxy-lyase; L-Lysine Decarboxylase. Enzyme Commission Number: EC 4.1.1.18. CAS No. 9024-76-4. Lysine decarboxylase. Activity: ~0.01 unit/mg solid. Storage: -20°C. Source: Bacterium cadaveris. Lysine decarboxylase; EC 4.1.1.18; 9024-76-4; L-lysine carboxy-lyase; L-Lysine Decarboxylase. Cat No: NATE-0425.
Native Baker's yeast (S. cerevisiae) 3-Phosphoglyceric Phosphokinase Quick inquiry Where to buy	PhosphoglyceRate kinase (EC 2.7.2.3) (PGK) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglyceRate (1,3-BPG) to ADP producing 3-phosphoglyceRate (3-PG) and ATP. Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-geneRating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, geneRating ADP and 1,3-BPG. Applications: 3-phosphoglyceric phosphokinase generates atp by catalyzing the transfer of a phosphate group from 1,3-diphosphoglycerate to adp. 3-phosphoglycerate phosphokinase is used to study glycolysis ...phoglyceric kinase; phosphoglycerokinase; EC 2.7.2.3. Enzyme Commission Number: EC 2.7.2.3. CAS No. 9001-83-6. 3-PGK. Activity: > 1000 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Source: Baker's yeast (S. cerevisiae). PGK; 3-PGK; ATP-3-phospho-D-glyceRate-1-phosphotransferase; ATP:D-3-phosphoglyceRate 1-phosphotransferase; 3-phosphoglyceRate kinase; 3-phosphoglyceRate phosphokinase; 3-phosphoglyceric acid kinase; 3-phosphoglyceric acid phosphokinase; 3-phosphoglyceric kinase; glyceRate 3-phosphate kinase; glycerophosphate kinase; phosphoglyceric acid kinase; phosphoglyceric kinase; phosphoglycerokinase; EC 2.7.2.3. Cat No: NATE-0006.
Native Baker's yeast (S. cerevisiae) D-Ribulose-5-phosphate 3-Epimerase Quick inquiry Where to buy	RPE is a metalloenzyme and has been shown to use the divalent Zn2+ ion predominantly for catalysis. Human D-ribulose-5-phosphate 3-epimerase (hRPE) has been shown to use Fe2+ for catalysis. Applications: D-ribulose-5-phosphate 3-epimerase is an enzyme that converts the reversible conversion of d-ribulose 5-phosphate into d-xylulose 5-phosphate, which is important for the cellular response against oxidative stress. d-ribulose-5-phosphate 3-epimerase is involved in the pentose phosphate pathway, pentose and glucuronate interconversions and carbon fixation. this product is from bakers yeast and is provided as a lyophilized powder. it is useful in enzyme syste...EC 5.1.3.1. CAS No. 9024-20-8. RPE. Activity: 50-100 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: lyophilized powder. Lyophilized and essentially sulfate-free; contains approx. 35% Citrate buffer salts. Source: Baker's yeast (S. cerevisiae). EC 5.1.3.1; RPE; phosphoribulose epimerase; erythrose-4-phosphate isomerase; phosphoketopentose 3-epimerase; xylulose phosphate 3-epimerase; phosphoketopentose epimerase; ribulose 5-phosphate 3-epimerase; D-ribulose phosphate-3-epimerase; D-ribulose 5-phosphate epimerase; D-ribulose-5-P 3-epimerase; D-xylulose-5-phosphate 3-epimerase; pentose-5-phosphate 3-epimerase; 9024-20-8. Cat No: NATE-0659.
Native Baker's yeast (S. cerevisiae) Enolase Quick inquiry Where to buy	Enolase is a metalloenzyme that catalyzes the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Enolase is essential for both glycolysis and gluconeogenesis. Enolase from bakers yeast is a homodimer containing two bound Mg2+ ions. The molecular weight is 93.069 kDa.The peptide consists of 436 amino acids and contains a single cysteine residue. Two of the active site components include His191 and Arg414. The phosphorylated tyrosine residue present in yeast enolase forms a substrate for phosphorylation by tyrosine protein kinase. Apart from Mg2+, the enzyme can be activated by Zn2+, Mn2+, and Cd2+. Applications: Enolase from baker?s yeast has been used in a st...d spectroscopy. it has also been used along with other proteins to study gradient chromatof ocusing-mass spectrometry; a new technique for protein analysis. Group: Enzymes. Synonyms: EC 4.2.1.11; enolase; 2-phosphoglyceRate dehydRatase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydRatase; 2-phosphoglyceRate dehydRatase; 2-phosphoglyceric dehydRatase; 2-phosphoglyceRate enolase; γ-enolase; 2-phospho-D-glyceRate hydro-lyase; 9014-08-8. Enzyme Commission Number: EC 4.2.1.11. CAS No. 9014-8-8. Enolase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Baker's yeast (S. cerevisiae)
Native baker's yeast (S. cerevisiae) Glucose-6-phosphate Dehydrogenase Quick inquiry Where to buy	Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: Glucose-6-phosphate dehydrogenase is used to test ketose reductase activity in developing maize endosperm. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Storage: -20°C. Form: lyophilized powder. Source: Baker's yeast (S. cerevisiae). Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: DIA-219.
Native Baker's yeast (S. cerevisiae) Glutathione Reductase Quick inquiry Where to buy	Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl ...reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.6.4.2. CAS No. 9001-48-3. GR. Mole weight: mol wt 118 kDa. Activity: 100-300 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol. Source: Baker's yeast (S. cerevisiae). EC 1.6.4.2; 9001-48-3; Glutathione Reductase; GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-0317.
Native Baker's yeast (S. cerevisiae) Glyceraldehyde-3-phosphate Dehydrogenase Quick inquiry Where to buy	Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles. Group: Enzymes. Synonyms: EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde . Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: 70-140 units/mg protein. Storage: -20°C. Form: Lyophilized, sulfate-free powder stabilized with trehalose, Citrate, and DTT. Useful for systems requiring low sulfate. Source: Baker's yeast (S. cerevisiae). EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Cat No: NATE-0278.
Native Baker's yeast (S. cerevisiae) Inorganic Pyrophosphatase Quick inquiry Where to buy	Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. This ubiquitous enzyme serves to drive metabolic reactions that produce pyrophosphate, since these reactions typically have...phohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.1. CAS No. 9024-82-2. Inorganic pyrophosphatase. Mole weight: 71 kDa (homodimer consisting of two equal subunits of molecular weight 32-35 kDa). Activity: Type I, > 1,000 units/mg protein (BCA); Type II, > 500 units/mg protein (E1%/280). Storage: -20°C. Form: Type I, lyophilized powder containing 90% buffer salts; Type II, Lyophilized powder containing 85% buffer salts. Source: Baker's yeast (S. cerevisiae). Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0354.
Native Baker's yeast (S. cerevisiae) Invertase Quick inquiry Where to buy	Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar). The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertases cleave the O-C (fructose) bond, whereas the sucrases cleave the O-C (glucose) bond. Typically used in manufacturing confectionaries, dietary supplements, and other food grade applications. Applications: Used in the production of confectionary foods and artificial honey. Group: Enzymes. Synonyms: EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; β-fructofuranosidase; β-D-fructofuranoside fructohydrolase; 9001-57. Enzyme Commission Number: EC 3.2.1.26. CAS No. 9001-57-4. Invertase. Activity: Type I, 200-300 units/mg solid; Type II, > 300 units/mg solid. Storage: -20°C. Source: Baker's yeast (S. cerevisiae). EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; β-fructofuranosidase; β-D-fructofuranoside fructohydrolase; 9001-57-4. Cat No: NATE-0357.
Native Baker's yeast (S. cerevisiae) Nucleoside 5'-Diphosphate Kinase Quick inquiry Where to buy	Nucleoside 5'-diphosphate kinase is a cytosolic enzyme. Nucleoside 5'-diphosphate kinase from Saccharomyces cerevisiae is found highly expressed in the cytoplasm. It affects DNA synthesis, in part, by binding to Cdc8p. Nucleoside 5?-diphosphate kinase is a cytosolic enzyme. Applications: Nucleoside 5?-diphosphate kinase has been used in a study to examine a possible intracellular activity of the drug disodium cromoglycate in mast cells. it has also been used in a study to investigate protein synthesis in rabbit reticul ocytes. Group: Enzymes. Synonyms: nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; nucleoside-diphosphate kinase; EC 2.7.4.6; 9026-51-1; NDPK. Enzyme Commission Number: EC 2.7.4.6. CAS No. 9026-51-1. NDPK. Storage: -20°C. Form: lyophilized powder; essentially sulfate-free powder. Contains sodium Citrate with a trace of magnesium and EDTA salts. Source: Baker's yeast (S. cerevisiae). nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; nucleoside-diphosphate kinase; EC 2.7.4.6; 9026-51-1; NDPK. Cat No: NATE-0476.
Native Baker's yeast (S. cerevisiae) Phosphoglucose Isomerase Quick inquiry Where to buy	Phosphoglucose Isomerase (PGI) is an enzyme crucial for the interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate. PGI is responsible for the second step of glycolysis and is involved in glucogenesis. It is highly conserved in bacteria and eukaryotes. Applications: Isomerization of ketoses to aldoses. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Mole weight: 145 kDa. Activity: 350 U/mg at +25°C with F6P as substrate. Storage: Stable at +2 to +8°C. Source: Baker's yeast (S. cerevisiae). Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Cat No: NATE-0554.
Native baker's yeast (S. cerevisiae) Proteinase A Quick inquiry Where to buy	Saccharopepsin is an enzyme. This enzyme catalyses the following chemical reaction:Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves-Leu-Leu-Val-Tyr bond in a synthetic substrate. This enzyme is present in baker's yeast (Saccharomyces cerevisiae). Applications: Possibly useful for producing overlap peptides in sequence studies. Group: Enzymes. Synonyms: Endopeptidase; Proteinase A; EC 3.4.23.25; yeast endopeptidase A; Saccharomyces aspartic proteinase; aspartic proteinase yscA; proteinase yscA; yeast proteinase A; Saccharomyces cerevisiae aspartic proteinase A. Enzyme Commission Number: EC 3.4.23.25. Proteinase A. Activity: 15-50 units/mg protein. Storage: -20°C. Form: Lyophilized solids containing sodium Citrate, pH 5.0. Source: S. cerevisiae. Species: baker's yeast. Endopeptidase; Proteinase A; EC 3.4.23.25; yeast endopeptidase A; Saccharomyces aspartic proteinase; aspartic proteinase yscA; proteinase yscA; yeast proteinase A; Saccharomyces cerevisiae aspartic proteinase A. Pack: Package size based on protein content. Cat No: NATE-0636.
Native Baker's yeast (S. cerevisiae) Pyruvate Decarboxylase Quick inquiry Where to buy	Pyruvate decarboxylase (PDC) is a homotetrameric enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. PDC contains a β-α-β structure, yielding parallel β-sheets. Applications: Pyruvate decarboxylase (pdc) is used to study residues involved in thiamine pyrophosphate (tpp) binding. it is used to study the regulation of fermentation pathways in plant species. Group: Enzymes. Synonyms: Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Enzyme Commission Number: EC 4.1.1.1. CAS No. 9001-4-1. PDC. Activity: 5.0-20.0 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4 pH 6.5, stabilized with 5% glycerol, 5 mM potassium phosphate, 1 mM magnesium acetate, 0.5 mM EDTA, and 25 μM c ocarboxylase. Source: Baker's yeast (S. cerevisiae). Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Cat No: NATE-0510.
Native Baker's yeast (S. cerevisiae) S-Acetyl-coenzyme A synthetase Quick inquiry Where to buy	Acetyl-coenzyme A synthetase catalyzes the production of acetyl-CoA. It is involved in histone acetylation in the nucleus. It may be involved in the growth of nonfermentable carbon sources such as glycerol. Acetyl-coenzyme A synthetase is induced by acetate, acetaldehyde and ethanol. Applications: S-acetyl-coenzyme a synthetase may be used to study various metabolic pathways, such as glycolysis, gluconeogenesis, pyruvate metabolism and co fixation. it may also be used in gene expression studies. Group: Enzymes. Synonyms: acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl C. Enzyme Commission Number: EC 6.2.1.1. CAS No. 9012-31-1. ACS. Activity: > 3 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing stabilizers as potassium phosphate, sucrose, and reduced glutathione. Source: Baker's yeast (S. cerevisiae). acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl CoA synthase; acetyl-coenzyme A synthase; short chain fatty acyl-CoA synthetase; short-chain acyl-coenzyme A synthetase; ACS; EC 6.2.1.1; 9012-31-1. Pack: Package size based on protein content. Cat No: NATE-0026.
Native Baker's yeast (S. cerevisiae) Transaldolase Quick inquiry Where to buy	Transaldolase is an enzyme (EC 2.2.1.2) of the non-oxidative phase of the pentose phosphate pathway. In humans, transaldolase is encoded by the TALDO1 gene. The following chemical reaction is catalyzed by transaldolase:sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate<-> erythrose 4-phosphate + fructose 6-phosphate. Applications: Useful in systems requiring low sulfate concentrations. Group: Enzymes. Synonyms: Transaldolase; EC 2.2.1.2; 9014-46-4; dihydroxyacetonetransferase; dihydroxyacetone synthase; formaldehyde transketolase; D-Sedoheptulose-7-phosphate:D-Glyceraldehyde-3-phosphate dihydroxyacetonetransferase. Enzyme Commission Number: EC 2.2.1.2. CAS No. 9014-46-4. Transaldolase. Activity: 10-30 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized, essentially sulfate-free; contains approx. 5% Citrate buffer salts. Source: Baker's yeast (S. cerevisiae). Transaldolase; EC 2.2.1.2; 9014-46-4; dihydroxyacetonetransferase; dihydroxyacetone synthase; formaldehyde transketolase; D-Sedoheptulose-7-phosphate:D-Glyceraldehyde-3-phosphate dihydroxyacetonetransferase. Cat No: NATE-0714.
Native Baker's yeast (S. cerevisiae) Triosephosphate Isomerase Quick inquiry Where to buy	Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess differential expression of fourteen proteins of uveal melanoma. triosephosphate isomerase has also been used in a study to investigate the use of sigmoid ph gradients in free-flow isoelectric f ocusing of human endothelial cell proteins. Group: Enzymes. Synonyms: Triose-. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: ~10,000 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Crystalline suspension in 2.7 M (NH4)2SO4, 0.5 mM EDTA, pH 6.5. Source: Baker's yeast (S. cerevisiae). Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0711.
Native Baker's yeast Uridine-5'-diphosphoglucose pyrophosphorylase Quick inquiry Where to buy	UTP-glucose-1-phosphate uridylyltransferase is an enzyme associated with glycogenesis. It synthesizes UDP-glucose from glucose-1-phosphate and UTP; i.e., glucose-1-phosphate + UTP<-> UDP-glucose + pyrophosphate. Applications: Uridine-5?-diphosphoglucose pyrophosphorylase has been used in assays to determine the concentration of pyrophosphate in human urine samples. Group: Enzymes. Synonyms: UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase; EC 2.7.7.9; 9026-22-6. Enzyme Commission Number: EC 2.7.7.9. CAS No. 9026-22-6. UDPG pyrophosphorylase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized, sulfate-free powder containing Citrate buffer salt. Source: Baker's yeast. UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase; EC 2.7.7.9; 9026-22-6. Cat No: NATE-0728.
Native Barley β-Amylase Quick inquiry Where to buy	β-Amylase hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units. Natural substrates such as starch and glycogen are broken down into glucose and maltose. Pure, crystalline β-amylase preparation consists of four isoenzymes with different isoelectric points. The enzyme polymerizes very rapidly through the sulfhydryl groups in the absence of reducing agents. p-Chloromercuribenzoate inhibits the polymerization and the enzymatic activity. The reducing agents mercaptoethanol or dithiothreitol can completely restore the activity. Applications: Β-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. β-amylase, has been used in various plant studies, such as carbon starvation studies in populus tremuloides. β-amylase, from barley, has been used to study how pressure and temperature affect catalytic activity. Group: Enzymes. Synonyms: saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrola. Enzyme Commission Number: EC 3.2.1.2. CAS No. 9000-91-3. β-Amylase. Activity: 20-80 units/mg protein (biuret). Storage: 2-8°C. Source: Barley. saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3. Cat No: NATE-0761.
Native Basidiomycetes sp. Driselase Quick inquiry Where to buy	Driselase is a cell wall degrading enzyme that contains cellulase, hemicellulase, pectinase etc. Therefore, it is very effective in removing plant cell walls to make protoplasts. Applications: Driselase from basidiomycetes has been used in a study to assess the digestion by fungal glycanases of arabinoxylans with different feruloylated side-chains. driselase from basidiomycetes has also been used in a study to investigate the purification, characterization, and mode of action of a rhamnogalacturonan hydrolase. the enzyme from creative enzymes has been used as a control while testing the ability of p-coumaroyl esterase to release p-coumaroyl and feruloyl groups from intact cell walls. it has also been used in the protoplast preparation from mycelia during a study to investigate the pathogenicity of cochliobolus carbonum on maize. Group: Enzymes. Synonyms: Driselase; 85186-71-6. CAS No. 85186-71-6. Driselase. Storage: 2-8°C. Source: Basidiomycetes sp. Driselase; 85186-71-6. Cat No: NATE-0207.
Native β-hemolytic Streptococcus Streptokinase Quick inquiry Where to buy	Streptokinase (SK) is an enzyme secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack) and pulmonary embolism. Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin. There are three domains to Streptokinase, denoted α (residues 1-150), β (residues 151-287), and γ (residues 288-414). Each domain binds plasminogen, altho...bral hemorrhage. streptokinase is also used in the treatment of complicated parapneumonic effusions and empyema where adverse reactions, allergic type, are rare. streptokinase has been used in a study to compare primary coronary intervention and thrombolytic therapy in my ocardial infarction patients. Group: Enzymes. Synonyms: Streptokinase; SK; EC 3.4.99.0; 9002-01-1. Enzyme Commission Number: EC 3.4.99.0. CAS No. 9002-1-1. SK. Activity: > 3,500 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing ~50% total protein by biuret and sodium glutamate. Total protein composed of enzyme protein and human serum albumin. Source: β-hemolytic Streptococcus
Native Bjerkandera adusta Peroxidase Quick inquiry Where to buy	The transformation of industrial dyes by manganese peroxidases from Bjerkandera adusta is a manganese-independent reaction. Applications: Peroxidase is isolated from bjerkandera adusta. peroxidases from b. adusta, a white rot fungus, is used to degrade synthetic dyes. peroxidase is used in bi ochemistry applications such as western blots, elisa and immunohist ochemistry. peroxidases are used to amplify a weak signal and increase detectability of a target molecule, such as a protein2. peroxidase is commonly used to determine amounts of glucose and peroxides in solution. Group: Enzymes. Synonyms: Peroxidases; lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxi. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Peroxidase. Activity: > 2.8 units/mg. Storage: -20°C. Source: Bjerkandera adusta. Peroxidases; lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase; EC 1.11.1.7; 9003-99-0. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0549.
Native Bothrops atrox Phosphodiesterase I Quick inquiry Where to buy	Phosphodiesterase I breaks phosphodiester bonds and catalyzes the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is released from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C. Group: Enzymes. Synonyms: Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodiesterase; oligonucleate 5'-nucleotidohydrolase; 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5'-NPDase; 5'-PDase; 5'-PDE; 5'NPDE; alkaline phosphodiesterase; nucleotide pyrophosphatase/phosphodiesterase I; orthophosphoric diester phosphohydrolase; PDE I; phosphodiesterase; exonuclease I. Enzyme Commission Number: EC 3.1.4.1. CAS No. 9025-82-5. PDE. Activity: > 0.01 unit/mg solid. Storage: -20°C. Form: crude dried venom. Source: Bothrops atrox. Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodiesterase; oligonucleate 5'-nucleotidohydrolase; 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5'-NPDase; 5'-PDase; 5'-PDE; 5'NPDE; alkaline phosphodiesterase; nucleotide pyrophosphatase/phosphodiesterase I; orthophosphoric diester phosphohydrolase; PDE I; phosphodiesterase; exonuclease I. Cat No: NATE-0511.
Native Bothrops atrox snake Defibrase Quick inquiry Where to buy	The medicine Defibrase is the trade name given to batroxobin and is isolated from the venom of Bothrops moojeni. It functions as an defibrinogenating agent and is used for patients with thrombosis. The batroxobin from the snake Bothrops atrox is patented as Reptilase and used as a hemostatic drug. Group: Enzymes. Synonyms: Defibrase; batroxobin; reptilase. Purity: Purity (SDS-PAGE): No band other than 31000-41000 Purity (HPLC): > 90.0%. Defibrase. Activity: pecific activity(CP): > 1,200 units / mg protein. Appearance: White lyophilized powder. Storage: Store in an airtight container, protect from light, at a temperature of < 10°C. Form: Freeze dried powder. Source: Bothrops atrox snake. Defibrase; batroxobin; reptilase. Cat No: PHAM-176.
Native Bovine Acid Phosphatase, Prostatic Quick inquiry Where to buy	Acid phosphatases (APase) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7. Acid phosphatase from potatoes is a 111 kDa diner consisting of two subunits at 41 and 35 kDa. This phosphatase has also been shown to cleave DNA. Group: Enzymes. Synonyms: acid phosphatase; 9001-77-8; acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum); EC 3.1.3.2; APase. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Apase. Activity: ~10 units/g solid. Storage: -20°C. Form: Partially purified, lyophilized powder. Source: Bovine prostate. Species: Bovine. acid phosphatase; 9001-77-8; acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum); EC 3.1.3.2; APase. Cat No: NATE-0081.
Native Bovine Alkaline Phosphatase Quick inquiry Where to buy	Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Bovine intestinal alkaline phosphatase is a dimeric, membrane-derived glycoprotein. at least three isoforms exist, which typically possess two n-linked and one or more o-linked glycans per monomer.2 the enzyme requires zinc, and magnesium or calcium divalen...r proteins for elisa, western blotting, and hist ochemical detection. it is routinely used to dephosphorylate proteins and nucleic acids. it may be used for protein labeling when high sensitivity is required. alkaline phosphatase may be also be used to dephosphorylate the 5?-termini of dna or rna to prevent self-ligation. dna or rna can also be tagged with radiolabeled phosphate (via t4 polynucleotide kinase) after dephosphorylation with alkaline phosphatase. this product has been used to study the mon oclonal alkaline phosphatase-anti-alkaline phosphatase (apaap) complex. high specific activity grade recommended for antibody and protein conjugation. Group: Enzymes. Synonyms
Native Bovine α (1-2,3,4,6) Fucosidase Quick inquiry Where to buy	Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. Group: Enzymes. Synonyms: α (1-2,3,4,6) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA. FUCA. Source: Bovine kidney. Species: Bovine. α (1-2,3,4,6) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA. Cat No: NATE-0261.
Native Bovine α-Chymotrypsin Quick inquiry Where to buy	Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. It is activated in the presence of trypsin. Applications: Chymotrypsin (ec 3.4.21.1, chymotrypsins a and b, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chym...ate p1 sidechain and the enzyme s1 binding cavity accounts for the substrate specificity of this enzyme. chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine and methionine at the p1 position. structurally, it is the archetypal structure for its superfamily, the pa clan of proteases. Group: Enzymes. Synonyms: EC 3.4.21.1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin. Enzyme Commission Number: EC 3.4.21.1. CAS No. 9004-7-3. Chymotrypsin. Activity: > 40 units/mg protein. Sto
Native Bovine α-Chymotrypsinogen A Quick inquiry Where to buy	Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Applications: The enzyme has been used in the non-invasive determination of solid-state protein conformation using near infrared (nir) spectroscopy. it has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. the enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. in this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution. Group: Zymogens. Synonyms: 9035-75-0; Chymotrypsinogen; α-Chymotrypsino. CAS No. 9035-75-0. Chymotrypsinogen A. Activity: > 40 units/mg solid. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine Pancreas. Species: Bovine. 9035-75-0; Chymotrypsinogen; α-Chymotrypsinogen A; Chymotrypsinogen A; Chymotrypsin. Cat No: NATE-0748.
Native Bovine α-L-Fucosidase Quick inquiry Where to buy	In enzymology, an alpha-L-fucosidase (EC 3.2.1.51) is an enzyme that catalyzes the chemical reaction:an alpha-L-fucoside + H2O<-> L-fucose + an alcohol. Thus, the two substrates of this enzyme are alpha-L-fucoside and H2O, whereas its two products are L-fucose and alcohol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O-and S-glycosyl compounds. This enzyme participates in n-glycan degradation and glycan structures-degradation. Group: Enzymes. Synonyms: α-L-Fucosidase; EC 3.2.1.51; α-fucosidase. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 2.0 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, 10 mM NaH2PO4 10 mM Citrate, pH 6.0. Source: Bovine kidney. Species: Bovine. α-L-Fucosidase; EC 3.2.1.51; α-fucosidase. Cat No: NATE-0266.
Native Bovine Angiotensin Converting Enzyme Quick inquiry Where to buy	Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels. Applications: Positive control. Group: Enzymes. Synonyms: ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipept...te buffer-300 mM NaCl, pH 8.3 at 37°C. Storage: Maintain at -20°C in undiluted aliquots for up to 12 months. Maintain at 4°C for up to one month. A decrease in activity may occur within prolonged storage at 4°C. Source: Bovine lung. Species: Bovine. ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase, peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; "hypertensin converting enzyme" peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidyl dipeptidase; peptidyl dipept
Native Bovine Auto-Activated Protein Kinase Quick inquiry Where to buy	Auto-Activated Protein Kinase phosphorylates and inactivates protein phosphatase 2A. The funtion appears to be related to the catalytic domain of p21-activated p65 (PAK) protein kinase which is produced in apoptotic cells. AK is also involved in cytoskeleton organization and other signal transduction processes. Group: Enzymes. Synonyms: AK; Auto-Activated Protein Kinase. AK. Activity: ~17,000 units/mg protein. Stability: -70°C. Form: aqueous solution. Source: bovine kidney. Species: Bovine. AK; Auto-Activated Protein Kinase. Cat No: NATE-0042.
Native Bovine β(1-3,4)-Galactosidase Quick inquiry Where to buy	Hydrolyzes non-reducing terminal galactose β(1-3) and β(1-4) linkages. Can be used in conjunction with other β-galactosidases for exoglycosidase sequencing. Applications: The enzyme has applications in the analysis of a wide variety of glycoconjugates. it is particularly useful for ensuring the complete removal of β(1-3) and β(1-4)-linked non-reducing terminal galactose residues of oligosaccharides. gal β(1-6) glcnac is hydrolyzed more slowly, however this linkage is not normally encountered in native complex glycans. this activity towards β(1-3) and β(1-4)-linked galactose contrasts with that of our other β-galactosidases whi...tose residues. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. β-gal. Mole weight: ~68 kD. Form: 20 mM sodium Citrate phosphate, 150 mM NaCl (pH 4.0). Source: Bovine testis. Species: Bovine. β(1-3,4)-Galactosidase; β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Cat No: NATE-0973.
Native Bovine β-1,4-Galactosyl Transferase Quick inquiry Where to buy	β-1,4-Galactosyl Transferase catalyzes the transfer of galactose from UDP-galactose to the terminal N-acetylglucosamine residues on elongating oligosaccharide chains. It is also considered to be a biosynthetic enzyme of the Golgi apparatus. β-1,4-Galactosyl Transferase can also be found on the cell surface functioning as a cell-adhesion molecule during various cellular interactions by binding to N-acetylglucosamine containing oligosaccharide substrates or ligands in the extracellular matrix. Group: Enzymes. Synonyms: lactose synthase; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; EC . Enzyme Commission Number: EC 2.4.1.22. CAS No. 9030-11-9. Galactosyltransferase. Mole weight: Mr ~44000. Activity: > 0.6 units/mg. Storage: -20°C. Source: Bovine milk. Species: Bovine. lactose synthase; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; EC 2.4.1.22; 9030-11-9. Cat No: NATE-0760.
Native Bovine β-Galactosidase Quick inquiry Where to buy	β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Applications: Β-galactosidase was used in the production of a stabilized, single reagent for alcohol analysis. Group: Enzymes. Synonyms: β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Activity: > 0.15 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Bovine liver. Species: Bovine. β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Cat No: NATE-0294.
Native Bovine β-Glucuronidase Quick inquiry Where to buy	β-glucuronidase catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption. Applications: Β-glucuronidase is used as a reporter gene in gus assays to monitor gene expression. Group: Enzymes. Synonyms: β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Enzyme Commission Number: EC 3.2.1.31. CAS No. 9001-45-0. GUSB. Activity: Type B-10, ~10,000 units/mg solid; Type B-1, > 1,000,000 units/g solid; Type B-3, > 2,000,000 units/g solid. Source: Bovine liver. Species: Bovine. β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Cat No: NATE-0329.
Native Bovine β-N-Acetylglucosaminidase Quick inquiry Where to buy	This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates. The activity of β-N-actylglucosaminidase may be determined with the chromogenic substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. β-N-actylglucosaminidase hydrolyzes the terminal nonreducing N-acetyl-D-hexosamine residues. This enzyme contains two predominant isozymes, Hex A, a heterodimer, and Hex B, a homodimer. N-acetylglucosamine, acetamide, N-2-acetamido-2-deoyglucosylamine, N-acetylnojirimycin, and N-acetyldeoxynojirmycin are known inhibitors. Applications: Bovine ki...idase A; N-acetylhexosaminidase; β-D-hexosaminidase; 9012-33-3; EC 3.2.1.52. Enzyme Commission Number: EC 3.2.1.52. CAS No. 9012-33-3. β-N-Acetylhexosaminidase. Activity: 10-50 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, pH approx. 6.0. Source: Bovine kidney. Species: Bovine. hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-beta-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; β-D-hexosaminidase;
Native Bovine Carbonic Anhydrase Quick inquiry Where to buy	The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs relatively slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion; they are therefore classified as metalloenzymes. It was from bovine erythrocytes. a dialyzed, lyophilized powder. Applications: Co2 determination in blood; elimination of co2 in reagents for acidity testing; carboxy group transfers; reduction reactions. Group: Enzymes. Synonyms: carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Carbonic Anhydrase. Mole weight: 29.0 kDa (Theoretical) 30 kDa (Lindskog et al. 1971). Activity: > 3,000 units per mg dry weight. Storage: 2-8°C. Form: lyophilized powder. Source: Bovine Erythrocytes. Species: Bovine. carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Cat No: NATE-0101.
Native Bovine Carboxypeptidase A Quick inquiry Where to buy	Carboxypeptidase as isolated from Bovine pancreas glands is a metalloenzyme that contains 1 g atom of zinc per mole of protein. It catalyzes the hydrolysis of the carboxyl-terminal peptide bond in peptides and proteins. It is primarily specific to aromatic and hydrophobic side chains such as phenylalanine, tryptophan or leucine. The enzyme also exhibits esterase activity. It is inhibited by beta-phenylpropionate and indole acetate. Protein determined by e1%/278. Applications: Carboxypeptidase a from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase a in escherichia coli. carboxypeptidase a fr...dase A1; pancreatic procarboxypeptidase A; 11075-17-5; Carboxypolypeptidase; Peptidyl-L-amino-acid hydrolase; carboxypeptidase A; carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A. Enzyme Commission Number: EC 3.4.17.1. CAS No. 11075-17-5. CPA1. Mole weight: mol wt ~35 kDa. Activity: > 50 units/mg protein. Storage: 2-8°C. Form: aqueous suspension. Source: Bovine pancreas. Species: Bovine. EC 3.4.17.1; CPA1; CPA; carboxypeptidase A1; pancreatic procarboxypeptidase A; 11075-17-5; Carboxypolypeptidase; Peptidyl-L-amino-acid hydrolase; carboxypeptidase A; carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A. Cat No: NATE-0150
Native Bovine Catalase Quick inquiry Where to buy	Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis. Group: Enzymes. Synonyms: EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Activity: Type 1 (Suspension) > 20,000 units per mg; Type 2 (Filtered) > 40,000 units per mg; Type 3 (Lyophilized) > 3,000 units per mg. Storage: All preparations are stable for 12 months at 2-8°C. Lyophilized preparations should be protected from moisture. Form: A partially purified, lyophilized powder. Source: Bovine Liver. Species: Bovine. EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Cat No: NATE-0105.
Native Bovine Cathepsin B Quick inquiry Where to buy	Cathepsin B has been found to cleave procaspase 1 and procaspase 11 and to induce apoptosis in digitonin-permeabilized cells. Translocation of cathepsin B from the cytoplasm to the nucleus contributes to bile salt induced apoptosis of Rat hepatocytes. Levels of cathepsin B in PC12 cells significantly decrease 12 to 24 hours after apoptosis is induced. Group: Enzymes. Synonyms: CTSB; cathepsin B; 9047-22-7; APPS; CPSB; cathepsin B1 (obsolete); cathepsin II. CAS No. 9047-22-7. Cathepsin B. Activity: > 10 units/mg protein. Form: Lyophilized powder containing sodium phosphate, sodium chloride and ~6% EDTA as stabilizer. Source: Bovine spleen. Species: Bovine. CTSB; cathepsin B; 9047-22-7; APPS; CPSB; cathepsin B1 (obsolete); cathepsin II. Cat No: NATE-0167.
Native Bovine Cathepsin C Quick inquiry Where to buy	Cathespin C is a dipeptidyl aminopeptidase that can sequentially remove dipeptides from a peptide chain with an unsubstituted N-terminus. The enzyme exhibits a preference for glycine and proline as N-terminal aminoacids. Substrates that have an N-terminal lysyl or arginyl residue, or a penultimate proryl residue are not targeted by this enzyme. The endopeptidase activity requires the presence of halide ions and sulfydryl activators. Applications: Cathepsin c has been used in a study that demonstrated the potential of a proteomics approach to identify novel proteins expressed by extravillous trophoblast and to uncover the mechanisms leading to disease states in pregnancy. catheps...s. Synonyms: CTSC; cathepsin C; 9032-68-2; EC 3.4.14.1; dipeptidyl aminopeptidase I; dipeptidyl transferase; dipeptidyl transferase; dipeptide arylamidase I; DAP I; dipeptidyl-peptidase I; DPP-I; CPPI; DPP1; DPPI; HMS; JP; JPD; PALS; PDON1; PLS. Enzyme Commission Number: EC 3.4.14.1. CAS No. 9032-68-2. CTSC. Activity: > 5 units/mg protein. Form: Lyophilized from a 1 M sodium chloride solution. Source: Bovine spleen. Species: Bovine. CTSC; cathepsin C; 9032-68-2; EC 3.4.14.1; dipeptidyl aminopeptidase I; dipeptidyl transferase; dipeptidyl transferase; dipeptide arylamidase I; DAP I; dipeptidyl-peptidase I; DPP-I; CPPI; DPP1; DPPI; HMS; JP; JPD; PALS; PDON1; PLS. Cat No: NATE-0170.
Native Bovine Cathepsin D Quick inquiry Where to buy	Cathepsin D is an endosomal-lysosomal aspartic protease implicated in breast cancer metastasis and Alzheimers disease. Lysosomal release of cathepsin D has been found to precede cytochrome c release and loss of membrane potential in apoptotic Human foreskin fibroblasts. Cathepsin D levels in PC12 cells increase 12 to 24 hours after apoptosis is induced. Group: Enzymes. Synonyms: CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. CTSD. Mole weight: 45 kDa. Activity: > 2.0 units/mg protein. Form: Lyophilized powder containing Citrate buffer salts. Source: Bovine spleen. Species: Bovine. CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P. Cat No: NATE-0171.
Native Bovine Cholesterol Esterase Quick inquiry Where to buy	Cholesterol esterase (CE) is a reversible enzyme that can hydrolyze or synthesize fatty acid esters of cholesterol and other sterols. Hydrolysis of water insoluble long chain fatty acid esters requires bile salt activation. Hydrolysis of water soluble esters of short chain fatty acids and lysophospholipids does not require activation by bile salts. It also hydrolyzes tri-, di-, and mono-acylglycerols, phospholipids, lysophospholipids, and ceramide. This monomeric glycoprotein may have multiple functions in lipid and lipoprotein metabolism, as well as in atherosclerosis. Protein determined by biuret. Applications: Cholesterol esterase bound to membrane-associated heparin on b...terase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Activity: > 200 units/g protein. Storage: -20°C. Form: Lyophilized powder. This product is partially purified from bovine pancreas and is supplied as an off-white to tan lyophilized powder containing 30-65% protein (biuret), potassium phosphate. Source: Bovine pancreas. Species: Bovine. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrol
Native Bovine Chymotrypsinogen A Quick inquiry Where to buy	Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Group: Zymogens. Synonyms: chymotrypsinogen A; Chymotrypsinogen; Chymotrypsin. CAS No. 9035-75-0. Purity: Purified, Five times crystallized, electrophoretically homogeneous. Chymotrypsinogen A. Activity: Activates to at least 45 units per mg protein. Stability: The enzyme is stable for days in solution at pH 3.0 and for years as a dry powder when stored refrigerated. Storage: Store at 2-8°C. Form: lyophilized powder. Source: Bovine Pancreas. Species: Bovine. chymotrypsinogen A; Chymotrypsinogen; Chymotrypsin. Cat No: NATE-0134.
Native Bovine Creatine Phosphokinase Quick inquiry Where to buy	Creatine kinase plays a key role in the energy metabolism of cells with intermittently high and fluctuating energy requirements. Examples of such cells include cardiac or skeletal muscle cells and neural tissues of brain and retina. The enzyme catalyzes the reversible transfer of the phosphoryl group from phosphorylcreatine to ADP, in order to generate ATP.1 The molecular mass of the protein is found to be approximately 80 kDa Da. It is made up of 2 subunits, each having a molecular weight of 40 kDa ± 2000. The lighter subunit is present in larger amounts. Protein determined by biuret. Applications: Creatine phosphokinase from bovine heart has been used to investigate wheth...osphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. Activity: > 100 U/mg. Storage: -20°C. Form: salt-free, lyophilized powder. Source: Bovine heart. Species: Bovine. EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Cat No: NATE-0136.
Native Bovine Deoxyribonuclease I Quick inquiry Where to buy	Deoxyribonuclease I (usually called DNase I), is an endonuclease coded by the human gene DNASE1. DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides. It acts on single-stranded DNA, double-stranded DNA, and chromatin. In addition to its role as a waste-management endonuclease, it has been suggested to be one of the deoxyribonucleases responsible for DNA fragmentation during apoptosis. Protein determined by biuret. Applications: Used for the removal of dna from protein samples. dnase...rom bovine pancreas has also been used in a study to investigate the effects of minor and major groove-binding drugs and intercalators on the dna association of minor groove-binding proteins reca and deoxyribonuclease i. Group: Enzymes. Synonyms: DNASE1; deoxyribonuclease I; deoxyribonuclease-1; DNase I; 9003-98-9; EC 3.1.21.1; pancreatic DNase; DNase; thymonuclease, dornase; dornava; dornavac; pancreatic deoxyribonuclease; pancreatic dornase; deoxyribonuclease (pancreatic); pancreatic DNase; DNAase; deoxyribonucleic phosphatase; alkaline deoxyribonuclease; alkaline DNase; endodeoxyribonuclease I; DNA depolymerase; Escherichia coli endonuclease I; deoxyribonuclease A; DNA end
Native Bovine Deoxyribonuclease II Quick inquiry Where to buy	Deoxyribonuclease II, also called as acid DNAse, hydrolyzes deoxyribonucleotide linkages in native and denatured DNA yielding products with 3'-phosphates. In vitro, its optimum pH range is 4.5-5.0. It also acts upon p-nitrophenyl-phosphodiesters at pH 5.6-5.9. The molecular weight is approximately 38 kDa Da. Applications: Dnase ii from creative enzymes has been used in the dissociation medium during the preparation of embryonic cardiac myocytes from rat heart. deoxyribonuclease ii from bovine spleen has been used in a study that conducted a partial purification of deoxyribonucleases from eggs and liver of xenopus laevis. deoxyribonuclease ii from bovine spleen has also been used in a study to investigate nucleic acid and protein synthesis of splenic lymphocytes. Group: Enzymes. Synonyms: DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreati. Enzyme Commission Number: EC 3.1.22.1. CAS No. 9025-64-3. DNASE2. Activity: > 1,000 units/mg protein. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine spleen. Species: Bovine. DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreatic DNase II; acid deoxyribonuclease; acid Dnase. Cat No: NATE-0201.
Native Bovine Deoxyribonuclease I RNase-free solution Quick inquiry Where to buy	Deoxyribonuclease I (usually called DNase I), is an endonuclease coded by the human gene DNASE1. DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides. It acts on single-stranded DNA, double-stranded DNA, and chromatin. In addition to its role as a waste-management endonuclease, it has been suggested to be one of the deoxyribonucleases responsible for DNA fragmentation during apoptosis. Applications: Used in molecular biology applications for removing dna during rna purifica...zyme Commission Number: EC 3.1.21.1. CAS No. 9003-98-9. DNASE1. Mole weight: mol wt 29.1 kDa. Storage: -20°C. Form: buffered aqueous glycerol solution. Source: Bovine pancreas. Species: Bovine. DNASE1; deoxyribonuclease I; deoxyribonuclease-1; DNase I; 9003-98-9; EC 3.1.21.1; pancreatic DNase; DNase; thymonuclease, dornase; dornava; dornavac; pancreatic deoxyribonuclease; pancreatic dornase; deoxyribonuclease (pancreatic); pancreatic DNase; DNAase; deoxyribonucleic phosphatase; alkaline deoxyribonuclease; alkaline DNase; endodeoxyribonuclease I; DNA depolymerase; Escherichia coli endonuclease I; deoxyribonuclease A; DNA endonuclease; DNA nuclease. Cat No: NATE-0199.
Native Bovine Enterokinase Quick inquiry Where to buy	Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Enterokinase is a highly specific serine protease that is used for the removal of the flag peptide from n-terminal and met-n-terminal fusion proteins. it does not remove the c-terminal flag. Applications...ytic activation of trypsin from trypsinogen. enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags. removes flag peptide from n-terminal and met-n-terminal fusion proteins. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 150 kDa (consisting of 115kDa and 35kDa subunits.). Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: powder. Source: Bovine intestine. Species: Bovine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0224.
Native Bovine Factor IXa β Quick inquiry Where to buy	Prepared from Bovine Factor IX by activation with Bovine Factor Xla, this Bovine Factor Xla is removed after activation. Complete activation is observed by SDS-PAGE. The Factor Xla activates FIX in a two-step reaction. In the first step, an internal Arg-Ala bond is cleaved, and in the second step, an Arg-Val bond is cleaved. The second cleavage leads to the liberation of an activation peptide from the NH2-terminal portion of the heavy chain to produce factor IXa&beta. Group: Enzymes. Synonyms: Bovine Factor IXa Beta; Factor IXa Beta; Factor Ixa. Factor IXa Beta. Mole weight: 43.9 kDa. Activity: 3096.00 PEU/mg. Storage: < -60°C. Source: Bovine. Species: Bovine. Bovine Factor IXa Beta; Factor IXa Beta; Factor Ixa. Cat No: NATE-0867.
Native Bovine Factor Xa Quick inquiry Where to buy	Bovine Factor Xa is prepared from Bovine Factor X by activation with Russell's Viper Venom. This RVV-X is removed after activation. Complete activation is observed by SDS-PAGE. Factor Xa, as part of the prothrombinase complex along with the cofactor Va, phospholipids and calcium ions, catalyzes the rapid conversion of prothrombin to thrombin. Group: Enzymes. Synonyms: Bovine Factor Xa; Factor Xa. Factor Xa. Mole weight: 45.3 kDa. Activity: 210.00 IU/mg. Storage: < -60°C. Source: Bovine. Species: Bovine. Bovine Factor Xa; Factor Xa. Cat No: NATE-0868.
Native Bovine Factor X Activated (Xa) Quick inquiry Where to buy	Factor Xa catalyzes the hydrolysis of the Arg-Thr and then Arg-Ile bonds in prothrombin to yield active thrombin. The fairly strict recognition sequence is Ile-Glu (or Asp)-Gly-Arg-↓-X. It may sometimes cleave at other basic residues, depending on the conformation of the target protein. Factor Xa will not cleave if a proline residue follows the arginine of the recognition sequence. Factor xa is a serine endoproteinase and a member of the s1 peptidase family. factor xa plays a critical role in the coagulation cascade by catalyzing the proteolytic conversion of prothrombin to active thrombin. factor xa?s prothrombin conversion activity is greatly enhanced in vivo when c...d with 10 μg of factor xa for 2.5 hours at 37 oc. Group: Enzymes. Synonyms: EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Prower factor; activated factor X; coagulation factor Xa. Enzyme Commission Number: EC 3.4.21.6. CAS No. 9002-5-5. Factor Xa. Storage: -20°C. Form: aqueous glycerol solution. Source: Bovine plasma. Species: Bovine. EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Pr
Native Bovine Factor XIa Quick inquiry Where to buy	Bovine Factor Xla is purified from freshly collected Bovine Plasma using a combination of salt precipitations and activation on a negative surface. This Factor Xla is a potent activator of both Human and Bovine Factor IX. Bovine Factor XIa purity is determined by SDS-PAGE and shows complete reduction upon incubation with 2-mercaptoethanol. Group: Enzymes. Synonyms: Bovine Factor XIa; Factor XIa. Factor XIa. Storage: < -60°C. Source: Bovine. Species: Bovine. Bovine Factor XIa; Factor XIa. Cat No: NATE-0869.
Native Bovine Galactosyltransferase Quick inquiry Where to buy	Galactosyltransferase catalyzes the transfer of galactosyl molecules in the synthesis of oligosaccharides. Applications: Galactosyltransferase is the catalytic component of the lactose synthetase system; it synthesizes lactose slowly in the absence of the regulatory protein α-lactalbumin. galactosyltransferase will also transfer galactose from udp-galactose to n-acetylglucosamine. this preparation is useful in the determination of α-lactalbumin, udp-galactose, and n-acetylglucosamine. Group: Enzymes. Synonyms: EC 2.4.1.22; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; 9031-68-9. Enzyme Commission Number: EC 2.4.1.22. CAS No. 9031-68-9. Galactosyltransferase. Storage: -20°C. Form: Lyophilized powder containing Tris, EDTA, and (NH4)2SO4. Source: Bovine milk. Species: Bovine. EC 2.4.1.22; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; 9031-68-9. Cat No: NATE-0274.
Native Bovine Gamma-Glutamyl Transferase Quick inquiry Where to buy	γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular ...transferase; 9046-27-9; GGTP. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. Purity: Purified. γ-GT. Activity: > 30 U/mg (Dimension Clinical Chemistry System). Appearance: Tan Powder. Storage: -20°C. Form: Lyophilized. Source: Bovine Kidney. Species: Bovine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0790.
Native Bovine Glutamate Dehydrogenase Quick inquiry Where to buy	Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Group: Enzymes. Synonyms: glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase. Enzyme Commission Number: EC 1.4.1.3. CAS No. 9001-46-1. GLDH. Mole weight: 260 kDa (gel). Activity: > 500U /mg protein. Appearance: White/off white powder. Storage: -20°C. Form: Freeze dried powder. Source: Bovine liver. Species: Bovine. glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase. Cat No: DIA-146.
Native Bovine Glutathione Peroxidase Quick inquiry Where to buy	Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown. Applications: Glutathione peroxidase from bovine erythr ocytes was used as a positive control in cloning and characterization of full-length cdnas encoding two glutathione peroxidases (gpxs) from globodera rost ochiensis. it was used for the determination of glutathione peroxidase activity in human milk. Group: Enzymes. Synonyms: EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Enzyme Commission Number: EC 1.11.1.9. CAS No. 9013-66-5. Mole weight: mol wt 84.5 kDa. Activity: > 300 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing 25% sucrose and 2.5% dithiothreitol with sodium phosphate buffer salts. Source: Bovine erythr ocytes. Species: Bovine. EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Cat No: NATE-0322.
Native Bovine Guanylate Kinase Quick inquiry Where to buy	In enzymology, a guanylate kinase (EC 2.7.4.8) is an enzyme that catalyzes the chemical reaction:ATP + GMP<-> ADP + GDP. Thus, the two substrates of this enzyme are ATP and GMP, whereas its two products are ADP and GDP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in purine metabolism. Group: Enzymes. Synonyms: guanylate kinase; deoxyguanylate kinase; 5'-GMP kinase; GMP kinase; guanosine monophosphate kinase; ATP:GMP phosphotransferase; EC 2.7.4.8; 9026-59-9. Enzyme Commission Number: EC 2.7.4.8. CAS No. 9026-59-9. GMP kinase. Activity: 10-40 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Bovine brain. Species: Bovine. guanylate kinase; deoxyguanylate kinase; 5'-GMP kinase; GMP kinase; guanosine monophosphate kinase; ATP:GMP phosphotransferase; EC 2.7.4.8; 9026-59-9. Cat No: NATE-0309.
Native Bovine Hemoglobin Quick inquiry Where to buy	Hemoglobin is found in the erythrocytes of all vertebrates. It is a conjugated protein with the prosthetic group heme which contains iron. The heme group is involved with the transport of oxygen from the lungs to tissues, while the globin portion of hemoglobin plays a major role in transporting carbon dioxide from the tissues to the lungs. The iron in heme is in the ferrous state. In oxyhemoglobin, it is apparently still in the ferrous state, but the oxygen is loosely bound to it. The structure of the hemoglobin molecule has been extensively studied. Most of the mammalian hemoglobins are composed of four subunits, consisting of four peptide chains to each of which is attached a heme group. But, among the mammalian hemoglobins, there are structural differences in terms of the amino acid residues and their sequences in the polypeptide chains. The molecular weight of hemoglobin is about 66,000 and the iron content is about 0.34%. The principal applications for hemoglobin are as a substrate for proteases, in anemia diagnosis and as a marker during molecular weight determination. Group: Others. Synonyms: Hemoglobin; Bovine Hemoglobin. Purity: Approx. 100%. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Bovine Erythrocytes. Species: Bovine. Hemoglobin; Bovine Hemoglobin. Cat No: NATE-1878.
Native Bovine Hyaluronidase Quick inquiry Where to buy	Hyaluronidase degrades hyaluronan and has been found to be inappropriately regulated during cancer progression. These enzymes randomly cleave β-N-acetylhexosamine-[1?4] glycosidic bonds in hyaluronic acid, chondroitin, and chondroitin sulfates. Group: Enzymes. Synonyms: hyaluronoglucosaminidase; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I; hyaluronate 4-glycanohydrolase; EC 3.2.1.35; 37326-33-3. Enzyme Commission Number: EC 3.2.1.35. CAS No. 37326-33-3. Hyaluronidase. Mole weight: mol wt ~55 kDa (four subunits of 14 kDa each). Activity: Type I, 750-3000 units/mg solid; Type II, 300-1,000 units/mg; Type III, 3,000-15,000 units/mg solid; Type IV, 400-1000 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Bovine testes. Species: Bovine. hyaluronoglucosaminidase; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I; hyaluronate 4-glycanohydrolase; EC 3.2.1.35; 37326-33-3. Cat No: NATE-0347.
Native Bovine intestinal mucosa Alkaline Phosphatase Quick inquiry Where to buy	Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Bovine intestinal alkaline phosphatase is a dimeric, membrane-derived glycoprotein. at least three isoforms exist, which typically possess two n-linked and one or more o-linked glycans per monomer.2 the enzyme requires zinc, and magnesium or calciu...s for elisa, western blotting, and hist ochemical detection. it is routinely used to dephosphorylate proteins and nucleic acids. it may be used for protein labeling when high sensitivity is required. alkaline phosphatase may be also be used to dephosphorylate the 5?-termini of dna or rna to prevent self-ligation. dna or rna can also be tagged with radiolabeled phosphate (via t4 polynucleotide kinase) after dephosphorylation with alkaline phosphatase. this product has been used to study the mon oclonal alkaline phosphatase-anti-alkaline phosphatase (apaap) complex. high specific activity grade recommended for antibody and protein conjugation. Group: Enzymes. Synonyms
Native Bovine Kidney Alkaline Phosphatase Quick inquiry Where to buy	Alkaline Phosphatase is a hydrolase enzyme responsible for removing phosphate groups in the 5- and 3- positions from many types of molecules, including nucleotides, proteins, and alkaloids. In humans, alkaline phosphatase is present in all tissues throughout the entire body, but is particularly concentrated in liver, bile duct, kidney, bone, and the placenta. The optimal pH for the enzyme activity is 10.0 in standard conditions. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. Activity: > 750 U/mg solid. Storage: Store at -20°C. Form: Freeze dried powder. Source: Bovine Kidney. Species: Bovine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0946.
Native Bovine Lactoperoxidase Quick inquiry Where to buy	Lactoperoxidase catalyzes the oxidation of iodide to iodine by hydrogen peroxide. This activity provides a gentle, specific alternative to chloramine T for the radioiodination of proteins and DNA. Group: Enzymes. Synonyms: lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase; EC 1.11. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Peroxidase. Activity: Type I, > 50 units/mg protein; Type II, > 150 units/mg; Type III, > 200 units/mg protein; Type IV, > 80 units/mg protein. Storage: -20°C. Form: Type I, ammonium sulfate suspension, Suspension in 3.2 M (NH4)2SO4 pH approx. 7.0; Type II, Type IV, lyophilized powder; Type III, lyophilized powder (essentially salt-free). Source: Bovine milk. Species: Bovine. lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase; EC 1.11.1.7; 9003-99-0; LPO; SPO. Cat No: NATE-0418.
Native Bovine L-Arginase Quick inquiry Where to buy	Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is:arginine + H2O ? ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. Group: Enzymes. Synonyms: Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Enzyme Commission Number: EC 3.5.3.1. CAS No. 9000-96-8. Purity: Protein > 70 % by biuret. Arginase. Storage: -20°C. Form: powder. Source: Bovine liver. Species: Bovine. Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Cat No: NATE-0379.
Native Bovine L-Glutamic Dehydrogenase Quick inquiry Where to buy	L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Mammalian forms of this enzyme, including this bovine form, can use either NADP (H) or NAD (H) as coenzymes. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway by which ammonia can become bound to the α-carbon atom of an α-carboxylic acid and thus, is the only source of de novo amino acid synthesis in mammalian species. Group: Enzymes. Synonyms: glutamic dehydrogenase; glutamate dehydrogenase [NAD (P)]; 9029-12-3; glutamate dehydrogenase [NAD (P)+]; EC 1.4.1.3; L-GLDH; L-Glutamate:NAD[P]+ Oxidoreductase (deaminating). Enzyme Commission Number: EC 1.4.1.3. CAS No. 9029-12-3. GLDH. Activity: Type I, > 40 units/mg protein; Type II, > 20 units/mg protein; Type III, > 35 units/mg protein. Storage: 2-8°C. Form: Type I, ammonium sulfate suspension, Suspension in 2.0 M (NH4)2SO4 solution; Type II, lyophilized powder, Contains primarily Citrate buffer salt; Type III, aqueous glycerol solution, Solution in 50% glycerol, pH 7.3. Source: Bovine liver. Species: Bovine. glutamic dehydrogenase; glutamate dehydrogenase [NAD (P)]; 9029-12-3; glutamate dehydrogenase [NAD (P)+]; EC 1.4.1.3; L-GLDH; L-Glutamate:NAD[P]+ Oxidoreductase (deaminating). Cat No: NATE-0392.
Native Bovine Lipoprotein Lipase Quick inquiry Where to buy	Lipoprotein lipase (LPL) (EC 3.1.1.34) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. It is a water-soluble enzyme that hydrolyzes triglycerides in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL), into two free fatty acids and one monoacylglycerol molecule. It is also involved in promoting the cellular uptake of chylomicron remnants, cholesterol-rich lipoproteins, and free fatty acids. LPL requires ApoC-II as a cofactor. LPL is attached to the luminal surface of endothelial cells in capillaries by the protein glycosylphosphatidylinositol HDL-binding protein 1 (GPIHBP1) and by heparin sulfated proteoglycans. It is most widely distributed in adipose, heart, and skeletal muscle tissue, as well as in lactating mammary glands. Group: Enzymes. Synony. Enzyme Commission Number: EC 3.1.1.34. CAS No. 9004-2-8. LPL. Activity: > 2,000 units/mg protein (BCA). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.8 M ammonium sulfate, 0.02 M Tris HCl, pH 8.0. Source: Bovine milk. Species: Bovine. lipoprotein lipase; clearing factor lipase; diglyceride lipase; diacylglycerol lipase; postheparin esterase; diglyceride lipase; postheparin lipase; diacylglycerol hydrolase; lipemia-clearing factor; EC 3.1.1.34; 9004-02-8; LPL. Cat No: NATE-0416.
Native Bovine Liver Alkaline Phosphatase Quick inquiry Where to buy	Alkaline phosphatases (APs) are highly ubiquitous enzymes, present in all species from bacteria to man. In humans, APs are encoded by a multi-gene family composed of four loci; i.e., tissue-nonspecific AP, also called bone/liver/kidney AP, intestinal. The sequence and complexity of the AP genes from other vertebrates and lower species are now being elucidated. The biological function of AP isozymes is still unknown. In vitro, the enzymes behave as phosphotransferases at neutral pH. The use of phosphate acceptor molecules (diethanolamine, tris, 2-amino-2-methyl-1-propanol) in the buffered substrate solutions increases the reaction rates and, thus, the sensitivity of assays based on AP determinations. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. Activity: 100 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Bovine Liver. Species: Bovine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase; AP. Cat No: NATE-1871.

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