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| Product | Description | |
|---|---|---|
| Acetylcholinesterase Human, Recombinant | Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides. Group: Enzymes. Synonyms: true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl; β-methylcholinesterase; AcCholE; EC 3.1.1.7; 9000-81-1; Acetylcholinesterase; AChE; acetylhydrolase. Enzyme Commission Number: EC 3.1.1.7. CAS No. 9000-81-1. Acetylcholinesterase. Activity: > 1,000 units/mg protein (Lowry). Storage: -20°C. Form: Lyophilized powder containing phosphate buffer salt. Source: HEK 293 cells. Species: Human. Cat No: NATE-0020. |  |
| Acid phosphatase 1 from Human, recombinant | Acid phosphatase 1, also known as ACP1, belongs to the phosphotyrosine protein family. It functions as an acid phosphatase and a protein tyrosine phosphatase (PTPase) and is present in all human tissues, including adipocytes. This enzyme hydrolyzes protein tyrosine phosphate to protein tyrosine and orthophosphate, and also orthophosphoric monoesters to alcohol and orthophosphate. Group: Enzymes. Synonyms: Acid phosphatase 1; soluble isoform b; ACP1; HAAP; LMW-PTP; Red cell acid phosphatase 1; Adipocyte acid phosphatase. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Purity: > 95% by SDS-PAGE. Apase. Mole weight: 20.1 kDa (178 aa, 1-158 aa + NT His-Tag). Activity: > 60,000 unit/mg of protein. Storage: Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Human. Acid phosphatase 1; soluble isoform b; ACP1; HAAP; LMW-PTP; Red cell acid phosphatase 1; Adipocyte acid phosphatase; Acid Phosphatase. Cat No: NATE-1672. | |
| α-L-Iduronidase from Human, Recombinant | This enzyme catalyses the hydrolysis of unsulfated α-L-iduronosidic linkages in dermatan sulfate. In lysosomal degradation process α-L-Iduronidase plays a crucial role. It hydrolyzes the non-reducing terminal α-L-iduronic acid residues in GAGs, including dermatan sulfate and heparan sulfate. It is involved in the degeneration of glycosaminoglycans such as dermatan sulfate and heparan sulfate. It is found in the lysosomes of cells. Applications: Α-l-iduronidase may be used for leukocyte assay in the study of a-l-iduronidase deficiency in new born. Group: Enzymes. Synonyms: Iduronidase; EC 3.2.1.76; L-iduronidase; alpha-L-iduronidase); glycosaminoglycan alpha-L-iduronohydrolase; IDUA; α-L-Iduronidase. Enzyme Commission Number: EC 3.2.1.76. IDUA. Mole weight: 71 kDa. Activity: >7,500 units/μg protein. Storage: Store at -20°C. Form: Supplied as a solution in 40 mM sodium acetate , 400 mM NaCl and 20% (v/v) glycerol, pH 5.0. Source: Mouse NSO cells. Species: Human. Iduronidase; EC 3.2.1.76; L-iduronidase; alpha-L-iduronidase); glycosaminoglycan alpha-L-iduronohydrolase; IDUA; α-L-Iduronidase. Cat No: NATE-0930. | |
| Baker's yeast (S. cerevisiae) Carboxypeptidase Y, recombinant | Carboxypeptidase Y (CPY) catalyzes the following reaction: Peptidyl-L-amino acid + H2O ------> Peptide + L-amino acid.It is prepared according to the method of Moore & Stein (J. Biol Chem, 211, 907, 1954). It resembles Carboxypeptidase A in its substrate specificity, but it hydrolyzes C-terminal glycine and L-leuicine more rapidly and L-phenylalanine more slowly. Group: Enzymes. Synonyms: carboxypeptidase Y; serine carboxypeptidase I; cathepsin A; lysosomal protective protein; deamidase; lysosomal carboxypeptidase A; phaseolin; EC 3.4.16.5; 9046-67-7; Peptidyl-L-amino acid Hydrolase; Serine Carboxypeptidase; Carboxypeptidase C; Peptidyl-L. Enzyme Commission Number: EC 3.4.16.1. Purity: > 90 %. Carboxypeptidase Y. Activity: > 10u/mg. Appearance: Clear, colorless to lightly colored. Storage: Long term below -20°C, short term 2-8°C. Avoid multiple freeze-thaws. Form: 500 mM sodium chloride, 500 mM imidazole, 20 mM sodium phosphate monobasic, 20 mM sodium phosphate dibasic, pH 7.5. Species: S. cerevisiae. carboxypeptidase Y; serine carboxypeptidase I; cathepsin A; lysosomal protective protein; deamidase; lysosomal carboxypeptidase A; phaseolin; EC 3.4.16.5; 9046-67-7; Peptidyl-L-amino acid Hydrolase; Serine Carboxypeptidase; Carboxypeptidase C; Peptidyl-L-amino-acid (-L-proline ) hydrolase; EC 3.4.12.8. Cat No: NATE-0103. | |
| β-N-Acetylglucosaminidase from Streptococcus pneumoniae, Recombinant | Hexosaminidase, 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. Appli...Commission Number: 3.2.1.52. CAS No. 9012-33-3. β-N-Acetylhexosaminidase. Activity: > 80 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. Source: E. coli. Species: Streptococcus pneumoniae. EC 3.2.1.52; 9012-33-3; 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. Pack: vial of > 1.0 unit. Cat No: NATE-0782. | |
| Chymotrypsin from Human, Recombinant | Chymotrypsin is a recombinant serine endopeptidase expressed in E.coli, purified with HPLC, the gene sequence is the same as human chymotrypsin. Recombinant chymotrypsin hydrolyzes at the carboxyl side of aromatic amino acids residues: Tyr, Phe and Trp. Cleavage may also be observed, but at a lower rate, at Leu and Met. Chymotrypsin activity is optimal in pH 7.0-9.0. Applications: Hydrolysis of proteins by chymotrypsin alone or in combination with other proteases. suitable for peptide mapping, fingerprinting, and sequence analysis. Group: Enzymes. Synonyms: EC 3.4.21.1; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; &alpha. Enzyme Commission Number: EC 3.4.21.1. CAS No. 9004-7-3. Purity: > 95% by HPLC. Chymotrypsin. Mole weight: 26,950 Da. Activity: >1000 unit/mg protein. Storage: Recombinant Chymotrypsin lyophilized should be stored under 2°C-8°C in sealed container. It is stable within 24 months. After dissolved, it should be stored under -20°C. Form: White lyophilized. Source: E. coli. Species: Human. EC 3.4.21.1; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; α-Chymotrypsin. Cat No: NATE-1890. | |
| Endo-β-galactosidase from Bacteroides fragilis, Recombinant | Endo-β-Galactosidase is an enzyme that hydrolyzes internal β-galactosidic linkages of oligosaccharides in poly-N-acetyl-lactosamine structures. This enzyme resembles the Escherichia freundii enzyme due to its specificity towards bovine corneal keratan sulphate, milk oligosaccharides and the glycolipids lacto-N-neotetraosylceramide and lacto-N-tetraosylceramide. Group: Enzymes. Synonyms: β-Galactosidase bacterial; Keratanase; Endo-β-galactosidase; keratan sulfate endogalactosidase; keratan-sulfate 1,4-β-D-galactanohydrolase; EC 3.2.1.103. Enzyme Commission Number: EC 3.2.1.103. CAS No. 55072-01-0. Endo-β-galactosidase. Mole weight: ~32 kDa. Activity: >14 U/ml; Specific Activity: >140 U/mg protein. Storage: 2-8°C. Form: Sterile-filtered in 20 mM Tris-HCl, pH 7.5. Source: E. coli. Species: Bacteroides fragilis. β-Galactosidase bacterial; Keratanase; Endo-β-galactosidase; keratan sulfate endogalactosidase; keratan-sulfate 1,4-β-D-galactanohydrolase; EC 3.2.1.103. Cat No: NATE-1413. | |
| Immobilized Endoproteinase Glu-C on F7m | Endoproteinase Glu-C hydrolyzes peptide and ester linkages specifically at the carboxyl end of glutamic acid (-Glu/-X; in ammonium carbonate pH 7. 8, or ammonium acetate pH 4. 0, buffer A) or of glutamic and aspartic acid (-Glu/-X and -Asp/-X; in phosphate buffer pH 7. 8, buffer B). F7m: 1. 0 mg endoproteinase Glu-C immobilized on matrix F7m per CR-column. 900 units immobilized per CR-column. Nr. 7 Storage buffer: 50 mM Tris/HCl at pH 7. 5, 5 mM EDTA. Nr. 31 Reaction buffer A: 25 mM ammonium acetate, pH 4. 0 (see above)Nr. 32 Washing buffer A: 25 mM ammonium acetate, pH 4. 0, 1 M NaClNr. 62 Reaction buffer B: 50 mM phosphate buffer, pH 7. 8 (see above)Nr. 63 Washing buffer B: 50 mM phosphate buffer, pH 7. 8, 1 M NaCl. Group: Enzymes. Synonyms: EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Enzyme Commission Number: EC 3. 4. 21. 19. Storage: 4 °C. Source: Staphylococcus aureus. EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase; Immobilized Endoproteinase Glu-C. Cat No: NATE-1763. | |
| Immobilized Endoproteinase Glu-C on G3m | Endoproteinase Glu-C hydrolyzes peptide and ester linkages specifically at the carboxyl end of glutamic acid (-Glu/-X; in ammonium carbonate pH 7. 8, or ammonium acetate pH 4. 0, buffer A) or of glutamic and aspartic acid (-Glu/-X and -Asp/-X; in phosphate buffer pH 7. 8, buffer B). G3m: 25 ug (22 units) endoproteinase Glu-C per CR-column immobilized on dextran. This CR-column cuts at least 12 ug tubulin or 5 ug BSA per application in phosphate buffer. Nr. 7 Storage buffer: 50 mM Tris/HCl at pH 7. 5, 5 mM EDTA. Nr. 31 Reaction buffer: 25 mM NH4-acetate, pH 4. 0 (see above)Nr. 32 Washing buffer: 25 mM NH4-acetate, pH 4. 0, 1 M NaClNr. 62 Reaction buffer: 50 mM phosphate buffer, pH 7. 8 (see above)Nr. 63 Washing buffer: 50 mM phosphate buffer, pH 7. 8, 1 M NaCl. Group: Enzymes. Synonyms: EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Enzyme Commission Number: EC 3. 4. 21. 19. Storage: 4 °C. Source: Staphylococcus aureus. EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase; Immobilized Endoproteinase Glu-C. Cat No: NATE-1764. | |
| Immobilized TPCK-Trypsin on F7m | Trypsin hydrolyzes proteins, peptides, amides and esters specifically at the carboxyl groups of the basic amino acids L-arginine or L-lysine. F7m: 1. 0 mg trypsin per CR-column, immobilized on polyvinyl10,200 ST-units immobilized per CR-column. Nr. 15 Storage buffer: 50 mM Tris/HCl at pH 8. 0 at 4°CNr. 67 Reaction buffer: 50 mM phosphate at pH 8. 0Nr. 68 Washing buffer: 50 mM phosphate at pH 8. 0, 1 M NaCl. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin. Enzyme Commission Number: EC 3. 4. 21. 4. Storage: 4 °C. Source: Bovine pancreas. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin; Immobilized TPCK-Trypsin; Immobilized Trypsin; TPCK-Trypsin. Cat No: NATE-1771. | |
| Immobilized TPCK-Trypsin on G3m | Trypsin hydrolyzes proteins, peptides, amides and esters specifically at the carboxyl groups of the basic amino acids L-arginine or L-lysine. G3m: 25 ug trypsin per CR-column, immobilized on dextran. 260 ST-units immobilized per CR-column. This CR-column cuts at least 50 ug tubulin per application. Nr. 15 Storage buffer: 50 mM Tris/HCl at pH 8. 0Nr. 67 Reaction buffer: 50 mM phosphate at pH 8. 0 (S?rensen)Nr. 68 Washing buffer: 50 mM phosphate at pH 8. 0, 1 M NaCl. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin. Enzyme Commission Number: EC 3. 4. 21. 4. Storage: 4 °C. Source: Bovine pancreas. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin; Immobilized TPCK-Trypsin; Immobilized Trypsin; TPCK-Trypsin. Cat No: NATE-1772. | |
| Keratanase II from Bacillus circulans, Recombinant | Keratansae II hydrolyzes 1, 3-beta-glucosaminidic linkages to galactose in keratan sulfate. On cleavage, the enzyme requires the sulfate at 6-0 position of the participating glucosamine, but acts independently of the sulfate at 6-0 position of the galactose linked to the glucosamine. Applications: Used in the screening and diagnosis of morquio a syndrome (mps iva). validation of an lc-ms/ms assay for detecting relevant disaccharides from keratan sulfate as a biomarker for morquio a syndrome. Group: Enzymes. Purity: >90%. Endo-β-galactosidase. Storage: Reconstituted protein can be stored at 4°C or in small aliquots at -20°C or below. Avoid repeated freeze-thaw cycles. Form: Powder. Source: E. coli. Species: Bacillus circulans. Endo-β-galactosidase; endo-β-galactosidase; keratan sulfate endogalactosidase; keratanase; keratan-sulfate 1,4-β-D-galactanohydrolase; Keratanase II. Cat No: NATE-1618. | |
| Matrix Metalloproteinase-13 (HisoTag) from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular pr..., a ca2+- and zn2+- binding catalytic domain, a hinge region, and a c-terminal hemopexin domain. hydrolyzes collagen type ii 5-6 times faster than collagens type i and iii. exhibits high activity towards gelatin and degrades α1-antichymotrypsin and plasminogen activator inhibitor-2. Group: Enzymes. Synonyms: Collagenase-3; Matrix metallopeptidase 13; MMP13; CLG3; MANDP1; MMP-13. Purity: >90% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 60 kDa. Activity: >50 mU/mg protein. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: S. frugiperda. Species: Human. Collagenase-3; Matrix metallopeptidase 13; MMP13; CLG3; MANDP1; MMP-13. Cat No: NATE-0859. | |
| Methylation modified Trypsin from Porcine, Recombinant | Trypsin specifically hydrolyzes peptide bonds at the carboxyl side of lysine and arginine residues. Recombinant trypsin is free of any other proteases activities, and TPCK is unnecessary and not contained. Unmodified trypsin is subject to auto-proteolysis, generating fragments that can interfere with protein sequencing or HPLC/MS peptides analysis. Sequencing grade modified trypsin is recombinant porcine trypsin modified by reductive methylation, rendering it resistant to proteolytic digestion. Applications: Protein digests for peptide mapping applications or protein identification by peptide mass fingerprinting or ms/ms spectral matching. it is suitable for digest...under -70°C, It is stable within 24 months.2. Above 95% activity is remained after 5 times repeated freezing and thawing.3. Above 90% activity is remained after kept under 4°C or 25°C for 24h.4. A 0.05 mg/ml solution of sequencing grade modified recombinant trypsin in 50mM NH4HCO3 is retained above 95% after a 3 hours incubation at 37 °C. For long-term such as 20hours incubation, 1mM CaCl2 is recommended to be contained. Form: Lyophilized. Source: E. coli. Species: Porcine. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Tryp | |
| Native Arachis hypogaea (peanut) Phospholipase D | Phospholipase D is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion. Hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid. Phospholipase D is involved in conferring drought susceptibility in peanuts, which increases the risk of aflatoxin contamination. Phospholipase d is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion. Applications: Research has shown adp-ribosylation factor regulation of phospholipase d is important in the release of nascent secretory vesicles from the trans-golgi network. it has also been used in a study to investigate stimulation of na+-ca2+ exchange activity in canine cardiac sarcolemmal vesicals. Group: Enzymes. Synonyms: Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Enzyme Commission Number: EC 3.1.4.4. CAS No. 9001-87-0. PLD. Activity: > 60 units/mg protein. Storage: -20°C. Form: Partially purified, lyophilized powder containing buffer salts. Source: Arachis hypogaea (peanut). Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Cat No: NATE-0594. | |
| Native Arthrobacter luteus Lyticase | Lyticase hydrolyzes poly-β (1?3)-glucose such as yeast cell wall glucan. Applications: Yeast cells are difficult to disrupt because the cell walls may form capsules or resistant spores. dna can be extracted from yeast by using lysing enzymes such as lyticase, chitinase, zymolase, and gluculase to induce partial spheroplast formation; spheroplasts are subsequently lysed to release dna. lyticase is preferred to digest cell walls of yeast and generate spheroplasts from fungi for transformation. reported to be useful for lysis of ashbya, candida, debaryomyces, eremothecium, endomyces, hansenula, hanseniaspora, kloeckera, kluyveromyces, lipomyces, metschikowia, pichia, pullularia, torulopsis, saccharomyces, saccharomycopsis, saccharomycodes, and schwanniomyces species. Group: Enzymes. Synonyms: Lyticase; 37340-57-1. CAS No. 37340-57-1. Lyticase. Activity: > 200 units/mg solid; > 1,500 units/mg protein; > 2,000 units/mg protein, Protein > 20 % by biuret. Storage: 2-8°C. Form: lyophilized powder. Source: Arthrobacter luteus. Lyticase; 37340-57-1. Cat No: NATE-0431. | |
| Native Aspergillus oryzae Ribonuclease T1 | Ribonuclease T1 (RNase T1) from Aspergillus oryzae is an endoribonuclease that hydrolyzes after G residues. Cleavage occurs between the 3-phosphate group of a guanidine ribonucleotide and 5-hydroxyl of the adjacent nucleotide. The initial product is a 2:3 cyclic phosphate nucleoside that is hydrolyzed to the corresponding 3-nucleoside phosphate. It differs from Pancreatic RNase in that it attacks the guanine sites specifically to yield 3'-GMP and oligonucleotides with a 3'-GMP terminal group. Applications: Ribonuclease t1 (rnase t1) from aspergillus oryzae is used to digest denatured rna prior to sequencing and is used for protein folding studies. Group: Enzymes. Synonyms: Ribonuclease T1; EC 3.1.27.3; g. Enzyme Commission Number: EC 3.1.27.3. CAS No. 9026-12-4. Rnase. Activity: 300,000-600,000 units/mg protein. Storage: -20°C. Form: ammonium sulfate suspension; Suspension in 2.8 M (NH4)2SO4 solution. Source: Aspergillus oryzae. Ribonuclease T1; EC 3.1.27.3; guanyloribonuclease; Aspergillus oryzae ribonuclease; RNase N1; RNase N2; ribonuclease N3; ribonuclease U1; ribonuclease F1; ribonuclease Ch; ribonuclease PP1; ribonuclease SA; RNase F1; ribonuclease C2; binase; RNase Sa; guanyl-specific RNase; RNase G; RNase T1; ribonuclease guaninenucleotido-2'-transferase (cyclizing); ribonuclease N3; ribonuclease N1; 9026-12-4. Cat No: NATE-0658. | |
| Native Bacillus licheniformis Alkaline Protease | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin a is a member of the serine s8 endoproteinase family. it has broad specificity with a preference for a large uncharged residue in the p1 position. it hydrolyzes native and denatured proteins, and is active under alkaline conditions. Applications: The enzyme has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart.1 it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax...ex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. Mole weight: 27 Kda. Activity: 7.0-14.0 units/mg. Form: lyophilized powder. Source: Bacillus licheniformis. ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Cat No: NATE-0444. | |
| Native Bacillus polymyxa Dispase I | Dispase I is a rapid, effective, gentle and neutral protease that can separate intact epidermis from the dermis. It can also separate intact epithelial sheets in culture from the substratum. The enzyme preserves the viability of the epithelial cells while cleaving the basement membrane zone region. It can also be used to prevent clumping in suspension cultures. This protease cleaves fibronectin and type IV collagen, but not laminin, type V collagen, serum albumin, or transferrin. It hydrolyzes N-terminal peptide bonds of non-polar amino acid residues. It preferentially attacks denatured and intercellular proteins with exposed hydrophobic amino acid residues. Ca2+, Mg2+, Mn2+...e i has also been used in a study to investigate a dityrosine-based substrate for a protease assay. dispase i has been used in lung digestion and processing for flow staining, as well as for cd4 cell isolation in mice. the enzyme has also been used to digest excised wounds and a small amount of surrounding skin for the detection of gfp+ (green fluorescence protein) cells. this study to investigated the effect of differentiation and angiogenesis of bone marrow-derived mesenchymal stem cells on wound healing. it has also been used to remove the epidermis during the isolation of dermal fibroblasts from mice. Group: Enzymes. Synonyms: Dispase I; Dispase; 42613-33-2; Protease fro | |
| Native Barley β-Amylase | 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 Bovine α-Chymotrypsin | 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 β-N-Acetylglucosaminidase | 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 Cholesterol Esterase | 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 Deoxyribonuclease II | 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 Lipoprotein Lipase | 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 Phosphodiesterase, 3',5'-cyclic-nucleotide-specific | Hydrolyzes the 3',5'-phosphodiester bond in cyclic nucleotide monophosphates, such as cAMP and cGMP, to the corresponding nucleotide 5'-monophosphate. Applications: May be used to assay the protein activator, calmodulin. Group: Enzymes. Synonyms: cyclic 3',5'-mononucleotide phosphodiesterase; PDE. Enzyme Commission Number: EC 3.1.4.17. CAS No. 9040-59-9. PDE. Mole weight: mol wt ~60 kDa. Activity: 15-30 units/mg protein (in the presence of 0.03 mM Ca2+ and a saturating level (10 units per ml) of calmodulin (P2277)). Storage: -20°C. Form: Lyophilized powder containing Tris-HCl buffer salts and lactose. Source: Bovine brain. Species: Bovine. cyclic 3',5'-mononucleotide phosphodiesterase; PDE; cyclic 3',5'-nucleotide phosphodiesterase; cyclic 3',5'-phosphodiesterase; 3',5'-nucleotide phosphodiesterase; 3':5'-cyclic nucleotide 5'-nucleotidohydrolase; 3',5'-cyclonucleotide phosphodiesterase; cyclic nucleotide phosphodiesterase; 3', 5'-cyclic nucleoside monophosphate phosphodiesterase; 3':5'-monophosphate phosphodiesterase (cyclic CMP); cytidine 3':5'-monophosphate phosphodiesterase (cyclic CMP); cyclic 3',5-nucleotide monophosphate phosphodiesterase; nucleoside 3',5'-cyclic phosphate diesterase; nucleoside-3',5-monophosphate phosphodiesterase; EC 3.1.4.17. Pack: Package size based on activated units. Cat No: NATE-0515. | |
| Native Bovine Phosphodiesterase II | Phosphodiesterase (PDE) is any enzyme that is used to breaks phosphodiester bonds. The enzyme acts on poly (A), poly (U), and poly (I). Native DNA and poly (C) are quite resistant to the action of this enzyme. Hydrolyzes RNA, RNA-Core, 3'-alkyl-and 3'-aryl-nucleoside phosphates, and polydeoxyribonucleotides with 3'-phosphate end groups to 3'-mononucleotides. Polynucleotides having 5'-phosphomonoester end groups are not attacked. Applications: Phosphodiesterase (pde) is any enzyme that is used to breaks phosphodiester bonds. it is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. phosphodiesterase ii has been used in t...yloxobutyl (pob) base adducts from dna. furthermore, it has been used along with micr oc occal endonuclease to hydrolyze purified dna to 3-nucleoside monophosphates. Group: Enzymes. Synonyms: 3'-exonuclease; spleen phosphodiesterase; 3'-nucleotide phosphodiesterase; phosphodiesterase II; spleen exonuclease; EC 3.1.16.1; 9068-54-6; PDE2. Enzyme Commission Number: EC 3.1.16.1. CAS No. 9068-54-6. PDE. Activity: > 5.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Bovine spleen. Species: Bovine. 3'-exonuclease; spleen phosphodiesterase; 3'-nucleotide phosphodiesterase; phosphodiesterase II; spleen exonuclease; EC 3.1.16.1; 9068-54-6; PDE2. Cat No: NATE-0518. | |
| Native Bovine Phospholipase A2 | Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. It aggressively attacks phospholipids in membranes of intact cells. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Group: Enzymes. Synonyms: Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-84-7. PLA2. Activity: > 20 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains Tris buffer salts. Source: Bovine pancreas. Species: Bovine. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0583. | |
| Native Burkholderia sp. Lipoprotein Lipase | 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 (GPI...rin in rats. Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 3.1.1.34. CAS No. 9004-2-8. LPL. Activity: > 50,000 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Burkholderia sp. 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-0417. | |
| Native Canavalia ensiformis β-N-Acetylglucosaminidase | 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. At ph 4.0, p-nit...ta;-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; EC 3.2.1.52; 9012-33-3. Enzyme Commission Number: EC 3.2.1.52. CAS No. 9012-33-3. β-N-Acetylhexosaminidase. Activity: > 15 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 2.5 M (NH4)2SO4, pH 7.0. Source: Canavalia ensiformis. hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-ac | |
| Native Clostridium perfringens (C. welchII) Phospholipase C | Phospholipase C is induced by thrombin and platelet-activating factor, forming 1,2-diacylglycerol and phosphatidic acid. PLC hydrolyzes the phosphate bond on phosphatidylcholine and other glycerophospholipids yielding diacylglycerol; this enzyme will also hydrolyze the phosphate bonds of sphingomyelin, cardiolipin, choline plasmalogen and ceramide phospholipids. Group: Enzymes. Synonyms: Phospholipase C; PLC; 9001-86-9; lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oede. Enzyme Commission Number: EC 3.1.4.3. CAS No. 9001-86-9. Phospholipase C. Activity: Type I, > 150 units/mg protein; Type II, 10-50 units/mg protein; Type III, Type IV, > 1,000 units/mg protein (Lowry). Storage: -20°C. Form: Type I, Lyophilized powder in buffered salts; Type II, lyophilized powder; Type III, buffered aqueous glycerol solution; Solution in 60% (v/v) glycerol containing 10 mM Tris-HCl, pH 8.0 and 10 mM EDTA; Type IV, lyophilized powder, Contains phosphate buffer salts, EDTA and stabilizer. Source: Clostridium perfringens (C. welchII). Phospholipase C; PLC; 9001-86-9; lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oedematiens β-and γ-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; α-toxin; EC 3.1.4.3. Cat No: NATE-0593. | |
| Native Crotalus durissus terrificus venom Phospholipase A2 | Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. It aggressively attacks phospholipids in membranes of intact cells. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Group: Enzymes. Synonyms: Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-84-7. PLA2. Activity: ~200 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Crotalus durissus terrificus venom. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0584. | |
| Native Electrophorus electricus (electric eel) Acetylcholinesterase | Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides. Type vi-s, lyophilized powder, 200-1000 units/mg protein; type v-s, lyophilized powder, > 1000 units/mg protein. Applications: The enzyme has been used as a reference to to evaluate the effect of aspartame metabolites on hippocampal acetylcholinesterase activity. the enzyme has also been used in immobilization studies for the rapid detection of acetylthiocholine chloride. Group: Enzymes. Synonyms: true c. Enzyme Commission Number: EC 3.1.1.7. CAS No. 9000-81-1. Acetylcholinesterase. Mole weight: 280 kDa. Activity: > 1 ,000 units/mg protein; 200-1 ,000 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Electrophorus electricus (electric eel). true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl; β-methylcholinesterase; AcCholE; EC 3.1.1.7; 9000-81-1; Acetylcholinesterase; AChE; acetylhydrolase. Cat No: NATE-0018. | |
| Native Honey bee venom (Apis mellifera) Phospholipase A2 | Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. It aggressively attacks phospholipids in membranes of intact cells. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Group: Enzymes. Synonyms: Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-84-7. PLA2. Activity: 600-2400 units/mg protein. Storage: -20°C. Form: salt-free, lyophilized powder. Source: Honey bee venom (Apis mellifera). Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0585. | |
| Native Human β-N-Acetylglucosaminidase | 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: Β-n-...etylhexosaminidase; 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: 6-20 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 2.4 M (NH4)2SO4 containing 0.15 M NaCl and 0.1 M sodium phosphate, pH 6.0. Source: Human placenta. Species: Human. 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 | |
| Native Human erythrocytes Acetylcholinesterase | Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides. The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel. Applications: Acetylcholinesterase (ache) from creative enzymes has been used in the structure-activity study of phosphoramido acid esters as inhibitors of ache. Group: Enzymes. Synonyms: true cholinesterase; choline esterase I; cholines. Enzyme Commission Number: EC 3.1.1.7. CAS No. 9000-81-1. Acetylcholinesterase. Mole weight: ~80 kDa. Activity: > 500 units/mg protein (BCA). Storage: 2-8°C. Form: buffered aqueous solution. Solution in 20 mM HEPES, pH 8.0, containing 0.1% TRITON X-100. Source: Human erythrocytes. Species: Human. true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl; β-methylcholinesterase; AcCholE; EC 3.1.1.7; 9000-81-1; Acetylcholinesterase; AChE; acetylhydrolase. Cat No: NATE-0019. | |
| Native Naja mossambica mossambica Phospholipase A2 | Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. It aggressively attacks phospholipids in membranes of intact cells. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Group: Enzymes. Synonyms: Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-84-7. PLA2. Activity: ~1,500 units/mg protein. Storage: -20°C. Source: Naja mossambica mossambica. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0586. | |
| Native Porcine Deoxyribonuclease II | 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 to treat transformed cells during the purification of β-lactamase. it has also been used for the preparation of adenoma tissue in a study that investigated the effect of somatoprim on growth hormone secretion in human adenoma cell cultures (hsa). deoxyribonuclease ii from porcine spleen has been used in an immunohistological study of the immune system cells in paraffin-embedded tissues. deoxyribonuclease ii from porcine spleen has also been used in a study to investigate its reassociation with the lysosomal membrane. Group: Enzymes. Synony. Enzyme Commission Number: EC 3.1.22.1. CAS No. 9025-64-3. DNASE2. Activity: 2,000-6,000 Kunitz units/mg protein (biuret). Storage: -20°C. Form: lyophilized powder. Contains sodium chloride. Source: Porcine spleen. Species: Porcine. 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-0202. | |
| Native Porcine Leucine Aminopeptidase | Leucine aminopeptidase (LAP) is a proteolytic enzyme which hydrolyzes the peptide bond adjacent to a free amino group. It is called leucine aminopeptidase because it rapidly catalyzes the hydrolysis of leucine containing peptides. However, it also catalyzes the hydrolytic release of other amino acids located at the N-terminal end of various peptides and proteins. The enzyme from porcine kidney has been extensively studied. It has a molecular weight of 255,000 and it consists of four subunits each having one atom of zinc. Group: Enzymes. Synonyms: Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidas. Enzyme Commission Number: EC 3.4.11.1. Purity: 90% (biuret). LAP. Activity: >100 U/mg protein. Storage: Stable when stored at 4°C. Do not freeze. Form: Ammonium Sulfate. Source: Porcine Kidney. Species: Porcine. Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I; EC 3.4.11.1; leucyl aminopeptidase; LAP. Cat No: NATE-1879. | |
| Native Porcine Phospholipase A2 | Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. It aggressively attacks phospholipids in membranes of intact cells. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Group: Enzymes. Synonyms: Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-84-7. PLA2. Activity: Type I, > 600 units/mg protein. Storage: -20°C. Form: Type I, ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4 solution, pH 5.5; Type II, suspension, off-white. Source: Porcine pancreas. Species: Porcine. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0587. | |
| Native Porcine Prolidase | Prolidase is an enzyme that catalyzes the hydrolysis of the imide bond between an α-carboxyl group and proline or hydroxyproline. The protein forms a homodimer that hydrolyzes dipeptides or tripeptides with C-terminal proline or hydroxyproline residues. Applications: Prolidase is has an important role recycling of proline and collagen production. it is used to study mutations in the pepd gene that cause prolidase deficiency. it is used to hydrolyze proteins with c-terminal proline or hydroxyproline residues. prolidase from porcine kidney, has been used to hydrolyze peptide bonds from the amino terminus when studying enzymatic methylation of membrane proteins. Group: Enzymes. Synonyms: Xaa-Pro dipeptidase; prolidase; imidodipeptidase; proline dipeptidase; peptidase D; gamma-peptidase; X-Pro dipeptidase; EC 3.4.13.9; 9025-32-5. Enzyme Commission Number: EC 3.4.13.9. CAS No. 9025-32-5. Prolidase. Activity: > 100 units/mg protein. Storage: -20°C. Form: Supplied as a lyophilized powder containing Tris buffer salt and MnCl2. Source: Porcine kidney. Species: Porcine. Xaa-Pro dipeptidase; prolidase; imidodipeptidase; proline dipeptidase; peptidase D; gamma-peptidase; X-Pro dipeptidase; EC 3.4.13.9; 9025-32-5. Cat No: NATE-0627. | |
| Native Pseudomonas fluorescens Cholesterol Esterase | 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 from pseudomonas fluorescens has...iterpenol esterase; cholesteryl esterase; 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: > 10,000 units/g protein. Storage: -20°C. Form: lyophilized powder. Source: Pseudomonas fluorescens. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Cat No: NATE-0116. | |
| Native Rabbit Glucose-6-Phosphatase | Glucose 6-phosphatase (EC 3.1.3.9, G6Pase) is an enzyme that hydrolyzes glucose-6-phosphate, resulting in the creation of a phosphate group and free glucose. Glucose is then exported from the cell via glucose transporter membrane proteins. This catalysis completes the final step in gluconeogenesis and glycogenolysis and therefore plays a key role in the homeostatic regulation of blood glucose levels. Applications: Glucose-6-phosphatase was used to study the effects of clausena anisata (wild hook leaf) extracts on selected diabetes-related metabolizing enzymes. Group: Enzymes. Synonyms: EC 3.1.3.9; glucose 6-phosphate phosphatase; G6Pase; 9001-39-2; glucose-6-phosphatase. Enzyme Commission Number: EC 3.1.3.9. CAS No. 9001-39-2. Purity: Protein ~30 % (balance mostly sucrose). G6Pase. Activity: > 0.05 units/mg protein. Storage: -20°C. Form: powder with sucrose. Source: Rabbit liver. Species: Rabbit. EC 3.1.3.9; glucose 6-phosphate phosphatase; G6Pase; 9001-39-2; glucose-6-phosphatase. Cat No: NATE-0269. | |
| Native Sweet potato β-Amylase | 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-linke...ng and removing staphylococcus aureus biofilms. the enzyme has also been used to prepare β-limit dextrin from waxy maize starch. Group: Enzymes. Synonyms: saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3. Enzyme Commission Number: EC 3.2.1.2. CAS No. 9000-91-3. β-Amylase. Mole weight: 127.5. Activity: > 750 units/mg protein (E1%/280). Storage: 2-8°C. Form: ammonium sulfate suspension. Crystalline suspension in 2.3 M (NH4)2SO4. Source: Sweet potato. saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3. Cat No: NATE-0762. | |
| Trypsin | Trypsin is a serine protease enzyme, and hydrolyzes proteins at the carboxyl side of the Lysine or Arginine. Trypsin activates PAR2 and PAR4. Trypsin induces cell-to-cell membrane fusion in PDCoV infection by the interaction of S glycoprotein of PDCoV and pAPN. Trypsin also promotes cell proliferation and differentiation. Trypsin can be used in the research of wound healing and neurogenic inflammation [1] [2] [3] [4] [6]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9002-7-7. Pack Sizes: 100 mg; 500 mg; 1 g. Product ID: HY-129047. |  |
| Trypsin (MS grade) | Trypsin MS grade is a serine protease enzyme, and hydrolyzes proteins at the carboxyl side of the Lysine or Arginine. Trypsin MS grade activates PAR2 and PAR4. Trypsin MS grade induces cell-to-cell membrane fusion in PDCoV infection by the interaction of S glycoprotein of PDCoV and pAPN. Trypsin MS grade also promotes cell proliferation and differentiation. Trypsin MS grade can be used in the research of wound healing and neurogenic inflammation [1] [2] [3] [4] [6]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9002-7-7. Pack Sizes: 100 μg. Product ID: HY-129047A. | |
| 6-Chloro-3-indolyl b-D-galactopyranoside | 6-Chloro-3-indolyl b-D-galactopyranoside is a colorless substrate used to detect β-galactosidase activity, which is an extensively studied enzyme in molecular biology. This compound can be hydrolyzed by β-galactosidase to form an insoluble blue precipitate, commonly used in reporter assays to monitor gene expression or analyze protein interactions. Synonyms: Salmon Gal 6-Chloro-3-(b-D-galactopyranosyloxy)indole Rose Gal Red-Gal. CAS No. 138182-21-5. Molecular formula: C14H16ClNO6. Mole weight: 329.73. |  |
| Acid Protease for beer | Acid protease abstracts from fermentation of Aspergillus niger. Under low PH value, it can effectively hydrolyze protein. Acid protease be widely used in ethanol, wine, beer, brewage, food processing, feedstuff and etc. Applications: Ethanol, wine, beer, brewage, food processing, feedstuff and etc. Group: Enzymes. Synonyms: Acid Protease; for beer; Acid Protease; ethanol; baijiu Enzyme; beer Enzyme; brewage Enzyme; Acid Protease for beer; BER-1512. Protease. Appearance: powder or liquid. Source: Aspergillus niger. Acid Protease; for beer; Acid Protease; ethanol; baijiu Enzyme; beer Enzyme; brewage Enzyme; Acid Protease for beer; BER-1512. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: BER-1512. | |
| Alkaline Protease for detergent | Protease is a kind of enzyme preparation produced by one microbes submerged fermentation. It is also a kind of modified enzyme preparation after DNA recombination. As a common used enzyme preparation in detergent industry, the main activated composition alkaline protease can rapidly decompose protein. Protease can hydrolyze the hardly soluble protein on fabric into soluble peptide chain and amino acid in detergent solution. smoothness. Therefore, after the washing with cellulase, white clothes will be whiter and color clothes will be brighter and softer. At the same time, it can get off the granular dirt in the fiber. Applications: Protease can effectively remove sweat stain, blood stains, food protein dirt, cream stain and etc, the detergent contains protease will make fabric get perfect effect after washing. Group: Enzymes. Synonyms: Alkaline Protease; for detergent; Protease; decompose protein; Detergent Enzymes; Detergents; Alkaline Protease for detergent; DETE-2623. CAS No. 37259-58-8. Alkaline Protease. Appearance: powder or liquid. Alkaline Protease; for detergent; Protease; decompose protein; Detergent Enzymes; Detergents; Alkaline Protease for detergent; DETE-2623. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DETE-2623. | |
| α amylase | α-Amylase isolated from porcine pancreas is a glycoprotein.2 It is a single polypeptide chain of approximately 475 residues containing 2 SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability.3,4 Chloride ions are necessary for activity and stability5 The pH range for activity is 5.5 to 8.0, with the pH optimum at 7.6. Α-amylase from porcine pancreas. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. product is from porcine pancreas and is type i-a. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. S...mission Number: EC 3.2.1.1. CAS No. 9000-90-2. α-Amylase. Mole weight: 51-54 kDa. Activity: 700-1400 units/mg protein (E1%/280). Stability: α-Amylase is stable in 25 mM Tris-HCl, pH 7.5, with 100 mM KCl, at 0 °C or at -20 °C for at least 9 days.8 Another recommended storage condition is in 1 mM phosphate, pH 7.3, with 30 mM CaCl2 at -15 °C. Appearance: Appearance (Color): White to Light Yellow Appearance (Form): Suspension. Form: PMSF treated, saline suspension. Alpha amylase enzyme; for flour; fungal alpha amylase enzyme; enhance quality of flour enzyme; enhance quality; alpha amylase enzyme; flour; alpha amylase; Alpha amylase enzyme for flour; FLO-1301. Cat No: BAK-250. | |
| Aspartic Acid | Aspartic Acid. Synonyms: L- aminosuccinic acid; L-Aspartic Acid. CAS No. 56-84-8. Product ID: PE-0423. Molecular formula: C4H7NO4. Mole weight: 133.1. Category: Flavoring agent; Carrier Excipients. Product Keywords: Pharmaceutical Excipients; Other Materials; Aspartic Acid; Carrier Excipients; Flavoring agent; Carrier Excipients; C4H7NO4; 56-84-8; 56-84-8. UNII: 30KYC7MIAI. Grade: Pharmceutical Excipients. Administration route: Intravenous injection. Dosage Form: Intravenous injection. Stability and Storage Conditions: Store in a cool and dry place in an airtight container. Source and Preparation: This product is naturally found in various animal and plant proteins, especially in beet molasses. Commercially available products are usually made by hydrolyzing various proteins rich in the product with acid, neutralizing them with calcium hydroxide to form calcium salts, and then separating them. It can also be prepared by enzyme addition of ammonia to fumaric acid. Safety: This product is a natural nutrient, non-toxic and generally recognized as safe. |  |
| β-N-Acetylhexosaminidase from Xanthomonas manihotis, Recombinant | This enzyme releases non-reducing terminal β1-2, β1-3, β1-4 and β1-6 linked N-acetylglucosamine from complex carbohydrates. When incubated with oligosaccharides at low concentrations (<50 mU/ml) the enzyme can differentiate between GlcNAcβ1-2Man, GlcNAcβ1-4Man and GlcNAcβ1-6Man linkages. Under such conditions, the enzyme cleaves essentially only β1-2 linked GlcNAc, with two provisos. Firstly, β1-2 GlcNAc is not hydrolyzed if the mannose to which it is substituted has a substitution at C-6. Thus, the enzyme is useful for the analysis of tri-antennary oligosaccharides. Secondly, if the β-linked mannose of the ...cing β-n-acetylglucosamine residues from oligosaccharides. Applications: Biosynthesis of glycans in eukaryotes, glycoprotein production in various expression systems, protein digestion, removal of n-linked & o-linked glycans from glycoproteins, sequencing glycans. Group: Enzymes. Synonyms: β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. β-N-Acetylhexosaminidase. Mole weight: 71000 daltons. Storage: 4°C, Avoid repeated freeze/thaw cycles. Source: E.coli. Species: Xanthomonas manihotis. β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Cat No: NATE-0934. | |
| Biotinylated Luciferase from E. coli, Recombinant | Luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging. Group: Enzymes. Synonyms: Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Enzyme Commission Number: EC 1.13.12.7. Luciferase. Mole weight: ca. 70 kDa. Activity: > 1.0 x 10^10 relative light units (RLU)/ml Specific activity: 1.9 x 10^11 RLU/mg purified protein. Stability: stable at 25°C for at least one week (liquid form). Appearance: Liquid form. Storage: at -20°C. Source: E. coli. Species: E. coli. Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Cat No: NATE-1254. | |
| Bromelain | Bromelain is a protein-digesting enzyme extracted from the stem, fruit, and juice of the pineapple plant (Ananas comosus). It belongs to a group of enzymes called proteases or proteinases. Bromelain is a complex mixture of enzymes that can hydrolyze (break down) various types of proteins, including collagen, elastin, and fibrin. Uses: 1. anti-inflammatory: bromelain has been found to possess anti-inflammatory properties, which makes it useful in the treatment of arthritis, asthma, allergies, and other conditions characterized by inflammation. 2. digestive aid: bromelain is often used as a digestive aid because it helps break down proteins in the digestive tract, aiding digestion and reducing bloating. 3. wound healing: bromelai. Group: Heterocyclic organic compound. Alternative Names: STEM BROMELAIN; 3.4.22.32; BROMELAIN; BROMELAIN PINEAPPLE;BROMELIN;EC 3.4.22.1;EC 3.4.22.32;EC 3.4.22.4. CAS No. 9001-00-7. Molecular formula: N/A. Mole weight: N/A. Appearance: yellow to beige crystalline powder. Catalog: ACM9001007. |  |
| Carboxylesterase 1 isoform b from Human, Recombinant | Carboxylesterase 1 is a member of a large multigene carboxylesterase family. These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. This enzyme is known to hydrolyze aromatic and aliphatic esters and is necessary for cellular cholesterol esterification. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. Applications: Delivers high catalytic activity, ideal for robust high-throughput screening assays including drug-drug interaction studies, and pharmacokinetic...er: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ≥500 units/mg protein. Storage: at -70°C. Form: Liquid. Source: Baculovirus infected BTI insect cells. Species: Human. EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxyl | |
| Carboxylesterase 1 isoform c from Human, Recombinant | Carboxylesterase 1 is a member of a large multigene carboxylesterase family. These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. This enzyme is known to hydrolyze aromatic and aliphatic esters and is necessary for cellular cholesterol esterification. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. Applications: Delivers high catalytic activity, ideal for robust high-throughput screening assays including drug-drug interaction studies, and pharmacokinetic...er: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ≥1000 units/mg protein. Storage: at -70°C. Form: Liquid. Source: Baculovirus infected BTI insect cells. Species: Human. EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxy | |
| Endoglycosidase S from Streptococcus pyogenes, Recombinant | Endoglycosidase S is specific for N-glycans attached on the Fc domain of IgGs. The N-glycan is cleaved after the first Glc-Nac. Reaction is mild and runs fast under physiological conditions without the need for co-factors or detergent. The enzyme only hydrolyze glycans from the Fc-domain of IgGs even if other glycosylated proteins are present in solution. Group: Enzymes. Synonyms: Endoglycosidase S; IgGZERO. Purity: > 95% homogeneity as determined by SDS-PAGE analysis. Endo-β-N-acetylglucosaminidase. Mole weight: 110 kDa. Stability: The enzyme is reconstituted by addition of water and after reconstitution it is stable for 1 month at +4-8°C. The enzyme can be aliquoted and stored at -20°C for at least 6 months. The product is shipped at ambient temperature but should be stored at -20°C upon arrival. Appearance: White to light yellow powder. Storage: at -20°C. Form: Lyophilized powder with no preservatives added. Source: E.coli. Species: Streptocoocus pyogenes. Endoglycosidase S; IgGZERO Enzyme; IgGZERO; Endoglycosidase. Cat No: NATE-1603. | |
| Endo-protease | A protease enzyme used to hydrolyze protein to produce free-form amino acids for use as Free-Amino-Nitrogen (FAN).To increase the free amino-nitrogen content when brewing with high levels of raw wheat. Applications: Adding in the beginning of the mash, increasingremarkably the wort extract yield and the free amino-nitrogen content. Group: Enzymes. Synonyms: Endo-protease;protease enzyme; hydrolyze protein enzyme; as Free-Amino-Nitrogen; as FAN; Brewing; Endo-protease; BRE-1615. Endo-protease. Appearance: powder or liquid. Endo-protease;protease enzyme; hydrolyze protein enzyme; as Free-Amino-Nitrogen; as FAN; Brewing; Endo-protease; BRE-1615. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form) or subject to client requirement. Cat No: BRE-1615. | |
| Enzyme as soil nutrient | It is Aspergillus oryzae fermentation extract that is rich in protein, free-form amino acids, minerals, enzymes, vitamins, fiber and other nutrients. It is suitable as a stand-alone soil nutrient or as an additive mixed with other fertilizers such as hydrolyzed fish. Applications: As a stand-alone soil nutrient or as an additive mixed with other fertilizers. Group: Enzymes. Synonyms: Enzyme as soil nutrient; stand-alone soil nutrien; soil nutrien; soil. Soil nutrient. Appearance: inquire. Source: Aspergillus. Enzyme as soil nutrient; stand-alone soil nutrien; soil nutrien; soil. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: AGT-2911. | |
| Enzyme blend for flour proteins | This food-grade , non-synthetic, and organic-certifiable enzyme blend is used to hydrolyze soya, pea, yeast, maize and wheat flour proteins, producing high-quality functional protein hydrolysates. Applications: Vegetable proteins. Group: Enzymes. Enzyme for flour proteins. Appearance: powder or liquid. for flour proteins; Vegetable Proteins enzyme; hydrolyze soya enzyme;hydrolyze pea enzyme; hydrolyze yeast enzyme; maize and wheat flour proteins; pea; maize; wheat; hydrolyze soya; hydrolyze; Enzyme blend for flour proteins; PRO-1825. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: PRO-1825. | |
| Enzyme blend for hydrolyzing animal source proteins | This food-grade, non-synthetic, and organic-certifiable enzyme blend is used to hydrolyze fish, poultry, milk, gelatin, and other animal source proteins, producing high-quality functional protein hydrolysates. Applications: Meat & fish proteins. Group: Enzymes. Enzymes of animimal source proteins. Appearance: powder or liquid. hydrolyzing; animal source proteins; Meatand Fish Proteins enzyme; organic-certifiable; producing high-quality functional protein; hydrolysates enzyme; Enzyme blend for hydrolyzing animal source proteins; PRO-1822. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: PRO-1822. | |
| Fungal Acid Protease | An enzyme capable of hydrolyzing protein to peptides and amino acids in lower pH applications. Typically used in dietary supplements and flavor manufacture. Applications: Dietary supplements. Group: Enzymes. Synonyms: Fungal Acid Protease. CAS No. 9001-92-7. Acid Protease. Appearance: powder or liquid. Source: Aspergillus oryzae. Acid Protease; for beer; Acid Protease; ethanol; baijiu Enzyme; beer Enzyme; brewage Enzyme; Acid Protease for beer; BER-1512. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DIS-1019. | |
| Fungal Protease | An enzyme capable of hydrolyzing proteins to peptides and amino acids. Typically used in baking, flavor development (cheeses), and other food grade applications. Applications: Dietary supplements. Group: Enzymes. Synonyms: Fungal Protease. CAS No. 78990-62-2. Protease. Appearance: powder or liquid. Source: Aspergillus oryzae. Acid Protease; for beer; Acid Protease; ethanol; baijiu Enzyme; beer Enzyme; brewage Enzyme; Acid Protease for beer; BER-1512. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DIS-1022. | |
| glycosylphosphatidylinositol diacylglycerol-lyase | This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It therefore cleaves proteins from the lipid part of the glycosylphostphatidylinositol (GPI) anchors. In some cases, the long-chain acyl group at the sn-1 position of glycerol is replaced by an alkyl or alk-1-enyl group. In other cases, the diacylglycerol is replaced by ceramide (see Lip-1.4 and Lip-1.5 for definition). The only characterized enzyme with this specificity is from Trypanosoma brucei, where the acyl groups are myristoyl, but the function of the trypanosome enzyme is unknown. Substitution on O-2 of the inositol b...No. 129070-68-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5351; glycosylphosphatidylinositol diacylglycerol-lyase; EC 4.6.1.14; 129070-68-4; (glycosyl)phosphatidylinositol-specific phospholipase C; GPI-PLC; GPI-specific phospholipase C; VSG-lipase; glycosyl inositol phospholipid anchor-hydrolyzing enzyme; glycosylphosphatidylinositol-phospholipase C; glycosylphosphatidylinositol-specific phospholipase C; variant-surface-glycoprotein phospholipase C; 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming). Cat No: EXWM-5351. | |
| G/U Mismatch-Specific DNA Glycosylase from E.coli, Recombinant | G/U mismatch-specific DNA glycosylase (mug) is a part of the TDG/mug DNA glycosylase family. Mug is necessary for DNA damage lesion repair in stationary-phase cells. Mug protein removes three N4-ethenocytosine and takes away s the uracil base from mismatches in the order of U:G>U:A. The enzyme Uracil-N-Glycosylase removes uracil from the DNA leaving an AP position. Mug is also able to hydrolyzing the carbon-nitrogen bond among the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine plays a role in substrate recognition. Group: Enzymes. Synonyms: Xanthine DNA glycosylase; dug; ECK3058; JW3040; ygjF; G/U mismatch-specific DNA glycosylase; Double-strand-specific uracil glycosylase; Mismatch-specific uracil DNA-glycosylase; mug. Enzyme Commission Number: EC 3.2.2.28. Purity: Greater than 90% as determined by SDS-PAGE. MUG. Mole weight: 21.1 kDa. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. Form: Sterile Filtered colorless solution. Source: E.coli. Species: E.coli. Cat No: NATE-1911. | |
| Jojoba Protein HP, Hydrolyzed | Hydrolyzed (fragmented) proteins enzymatically extracted from the jojoba plant, 100% natural, MW 1800-2400 kD. Precipitations of proteins in the bottom of the container is normal. Uses: Lotions, creams, sun care products & after sun products, hair shampoos, leave-in-conditioners, hair mousse, shower gels, makeup products (mascara, foundations). Group: Skin actives. CAS No. 100684-35-3 / 7732-18-5 / 122-99-6 / 24634-61-5. Appearance: Dark brown, cloudy, faint odor. Catalog: CI-SC-0582. | |
| KT182 | KT182 is a potent inhibitor of α/β-hydrolase domain-containing protein 6 (ABHD6). ABHD6 is a transmembrane serine hydrolase hydrolyzing transmembrane serine hydrolase in nernous system. ABHD6 inhibition was shown to decrease seizure incidence in several mouse models of epilepsy, suggesting its potential for Dravet Syndrome treatment. Uses: Enzyme inhibitors. Synonyms: [4-[4-[3-(hydroxymethyl)phenyl]phenyl]triazol-1-yl]-(2-phenylpiperidin-1-yl)methanone. Grades: ≥98%. CAS No. 1402612-62-7. Molecular formula: C27H26N4O2. Mole weight: 438.5. | |
| L-377202 | L-377202 is a prodrug in which a peptide is covalently conjugated with the anthracycline antineoplastic antibiotic doxorubicin. This complex is hydrolyzed by the enzyme prostate-specific antigen (PSA), resulting in the formation of doxorubicin and leucine-doxorubicin. Selective targeting of these drugs to prostate tumor cells occurs because the hydrolyzing PSA enzyme is localized to the prostate gland. Doxorubicin and leucine-doxorubicin intercalate into DNA and interacts with topoisomerase II, thereby inhibiting DNA replication and repair and RNA and protein synthesis. These agents also produce toxic free-radical intermediates and interact with cell membrane lipids causing lipid peroxidation. Synonyms: L 377202; L377202; L-377,202; L 377,202; L377,202; (8S,10S)-10-[[3-[[1-(4-Carboxybutyryl)-t4Hyp-Ala-Ser-[(S)-2-cyclohexyl-Gly-]Gln-Ser-Leu-]amino]-2,3,6-trideoxy-alpha-L-lyxo-hexopyranosyl]oxy]-8-glycoloyl-7,8,9,10-tetrahydro-6,8,11-trihydroxy-1-methoxy-5,12-naphthacenedione. CAS No. 207395-85-5. Molecular formula: C65H89N9O25. Mole weight: 1396.46. | |
| L-iduronidase | Iduronidase (EC 3.2.1.76, L-iduronidase, alpha-L-iduronidase, laronidase) is an enzyme with the systematic name glycosaminoglycan alpha-L-iduronohydrolase. This enzyme catalyses the hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate.It is a glycoprotein enzyme found in the lysosomes of cells. It is involved in the degeneration of glycosaminoglycans such as dermatan sulfate and heparan sulfate. The enzyme acts by hydrolyzing the terminal alpha-L-induronic acid residues of these molecules, degrading them. The protein is reported as having a mass of approximately 83 kilodaltons. Group: Enzymes. Synonyms: α-L-iduronidase. Enzyme Commission Number: EC 3.2.1.76. CAS No. 9073-56-7. IDUA. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3940; L-iduronidase; EC 3.2.1.76; 9073-56-7; α-L-iduronidase. Cat No: EXWM-3940. | |
| Luciferase from E. coli, Recombinant | Luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging. Group: Enzymes. Synonyms: Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Enzyme Commission Number: EC 1.13.12.7. Luciferase. Mole weight: ca. 60 kDa. Activity: > 1.0 x 10^9 relative light units (RLU)/mg lyophilizate Specific activity: 1.4 x 10^11 RLU/mg purified protein. Stability: stable at 25°C for at least 5 days (liquid form). Appearance: White lyophilizate. Storage: at -20°C. Source: E. coli. Species: E. coli. Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Cat No: NATE-1253. | |
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