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| Product | Description | |
|---|---|---|
| Bicine | To prepare stable substrate solution for the determination of guanine deaminase. The buffer is widely used with the working concentration of 3-100 mM. Synonyms: N,N-Bis(2-hydroxyethyl)glycine; Diethanolglycine; Dihydroxyethylglycine; Diethanol glycine; N,N-Di(2-hydroxyethyl)glycine; N,N-Dihydroxyethylglycine; Fe-3-Specific; DHEG; Glycine, N,N-bis(2-hydroxyethyl)-; (Bis(2-hydroxyethyl)amino)acetic acid; 2-[Bis(2-hydroxyethyl)azaniumyl]acetate; Bicin; Bis(2-Hydroxyethyl)glycine; Chelest GA; DHEG; Diethylolglycine; Fe-3-Specific; N,N-Bis(2-hydroxyethyl)aminoacetic acid; N,N-Bis(hydroxyethyl)glycine; N,N-Bis(β-hydroxyethyl)glycine; NSC 7342; NSC 7512. Grades: ≥95%. CAS No. 150-25-4. Molecular formula: C6H13NO4. Mole weight: 163.17. |  |
| Endoglycoceramidase II from Rhodococcus sp., Recombinant | In enzymology, an endoglycosylceramidase (EC 3.2.1.123) is an enzyme that catalyzes the chemical reaction: oligoglycosylglucosylceramide + H2O<-> ceramide + oligoglycosylglucose. Thus, the two substrates of this enzyme are oligoglycosylglucosylceramide and H2O, whereas its two products are ceramide and oligoglycosylglucose. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O-and S-glycosyl compounds. Applications: Endoglycoceramidase ii from rhod oc occus sp. has been used in a study to assess the differentiation of glycosphingolipid-derived glycan structural isomers by liquid chromatography and mass spectrometry. endoglycoceramidase ii from rhodococcus sp. has also been used in a study to investigate structural and mechanistic analyses of endoglycoceramidase ii. Group: Enzymes. Synonyms: EC 3.2.1.123, endoglycoceramidase; EGCase; glycosyl-. Enzyme Commission Number: EC 3.2.1.123. CAS No. 105503-61-5. EGCase. Storage: -20°C. Form: Solution in 20 mM sodium acetate buffer, pH 6.0, containing 0.2% BSA and 0.1% Lubrol PX. Source: E. coli. Species: Rhodococcus sp. EC 3.2.1.123, endoglycoceramidase; EGCase; glycosyl-N-acetyl-sphingosine 1,1-β-D-glucanohydrolase, oligoglycosylglucosylceramide glycohydrolase; oligoglycosylglucosyl (1<->1)ceramide glycohydrolase. Cat No: NATE-0210. |  |
| Endoglycosidase F3 from Elizabethkingia miricola, Recombinant | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: Endoglycosidase F3; Elizabethkingia miricola; Endo-β-N-. Enzyme Commission Number: EC 3.2.1.96. CAS No. 231-791-2. Endo-β-N-acetylglucosaminidase. Activity: 30 U/mg. Storage: 2-8°C. Form: Aseptically filled solution in 20 mM Tris-HCl, pH 7.5. Source: E. coli. Species: Elizabethkingia miricola. Endoglycosidase F3; Elizabethkingia miricola; Endo-β-N-acetylglucosaminidase F3; Endoglycosidase F3 from Elizabethkingia (Chryseobacterium/Flavobacterium) meningosepticum; EC 3.2.1.96; 231-791-2; Endo F3. Pack: Supplied with 5× Reaction Buffer, 250 mM sodium acetate, pH 4.5. Cat No: NATE-0216. | |
| Lacto-N-Biosidase, Recombinant | Lacto-N-Biosidase may be used during glycoprotein analysis to better study the structure and function of glycoprotein and glycolipid sugar chains. This product can be used for specific oligosaccharide hydrolysis of type-I chain oligosaccharides, producing lacto-N-biose (Gal β 1-3 GlcNAc) as a byproduct, but not oligosaccharide hydrolysis of type-II chain oligosaccharides. As a result, Lacto-N-Biosidase can be used to distinguish type-I versus type-II glycoprotein as well as glycolipid sugar chains. When used in conjunction with α -1,3/4-Fucosidase, Lacto-N-Biosidase can also help distinguish Sialyl-Lewis x and Sialyl-Lewis a structures. Applications: Specific hydrolysis of oligosaccharides with type-i sugar chains and production of byproduct lacto-n-biose (gal β 1-3 glcnac). Group: Enzymes. Synonyms: Oligosaccharide lacto-N-biosylhydrolase; Lacto-N-Biosidase. Lacto-N-Biosidase. Mole weight: 60 kDa (SDS-PAGE). Form: Solution in 50 mM sodium acetate buffer, pH 5.5, containing 0.05% Brij-58. Source: Streptomyces sp. 142. Oligosaccharide lacto-N-biosylhydrolase; Lacto-N-Biosidase. Cat No: NATE-0855. | |
| Native Almond α (1-3,4) Fucosidase | 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 ...buffer supplied with the enzyme, >85% of the original activity is observed after two months at 2-8°C. In the buffer solution at 37°C, the half-life is approximately 80 hours. Storage: Shipped on ice pack for next day delivery. Store at -20°C. Store lyophilized enzyme at-20°C. Enzyme reconstituted with the provided reaction buffer is stable at 2-8°C for at least two months and may be stored at-20°C for at least six months. Avoid repeated freeze/thaw cycles. Form: Lyophilized from 50 mM sodium acetate, 3 mg/ml bovine serum albumin (pH 5.0). Source: Almond meal. Species: Almond. α (1-3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA. Cat No: NATE-0260. | |
| Native α-lytic protease | Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications. This protease cleaves after T, A, S, and V residues. It geneRates peptides of similar average length as trypsin. aLP was first isolated from the myxobacterium Lysobacter enzymogenes. The pro-form of aLP is 397 amino acids long. In its mature form, aLP is 198 amino acids long. Its tertiary structural core resembles those of pancreatic serine proteases. Group: Enzymes. Synonyms: Alpha-lytic protease; myxobacter α-lytic proteinase; α-lytic proteinase; α-lytic protease; Mycobacterium sorangium α-lytic proteinase; Myxobacter 495 α-lytic proteinase; Alp. α-LP. Storage: -70°C. Form: Supplied as a solution in 10 mM sodium acetate buffer, pH 5.0. Alpha-lytic protease; myxobacter α-lytic proteinase; α-lytic proteinase; α-lytic protease; Mycobacterium sorangium α-lytic proteinase; Myxobacter 495 α-lytic proteinase; Alp. Cat No: NATE-0052. | |
| Native Bovine Pyruvate Carboxylase | Pyruvate carboxylase catalyzes the carboxylation of pyruvate to oxaloacetate. Pyruvate carboxylase is a mitochondrial protein that has a biotin prosthetic group that requiries magnesium or manganese and acetyl CoA. Applications: Pyruvate is critical for gluconeogenesis, lipogenesis, glyceroneogenesis, neurotransmitter biosynthesis and glucose-induced insulin, and is used to study these pr ocesses. the enzyme from creative enzymes has been used as a positive control during the assay of pyruvate carboxylase activity in cell-free extracts of corynebacterium glutamicum. Group: Enzymes. Synonyms: Pyruvate carboxylase; PC; EC 6.4.1.1; 9014-19-1; pyruvic carboxylase. Enzyme Commission Number: EC 6.4.1.1. CAS No. 9014-19-1. PC. Activity: 5-25 units/mg protein (BCA). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 0.05 M Tris-HCl, pH 7.4, 2 mM magnesium acetate and 1 mM EDTA. Source: Bovine liver. Species: Bovine. Pyruvate carboxylase; PC; EC 6.4.1.1; 9014-19-1; pyruvic carboxylase. Cat No: NATE-0508. | |
| Native Human Cathepsin B | 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; cathepsin B1; APPS; CPSB; EC 3.4.22.1; 9047-22-7; cathepsin II; CatB. Enzyme Commission Number: EC 3.4.22.1. CAS No. 9047-22-7. Cathepsin B. Activity: > 2 ,000 units/mg protein (E1%/280). Storage: -20°C. Form: buffered aqueous solution. Solution in 50 mM sodium acetate, pH 5.0, with 1 mM EDTA. Source: Human liver. Species: Human. CTSB; cathepsin B; cathepsin B1; APPS; CPSB; EC 3.4.22.1; 9047-22-7; cathepsin II; CatB. Cat No: NATE-0168. | |
| Native Vibrio cholerae Neuraminidase | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. At least four mammalian sialidase homologs have been described in the...say of neuraminidase. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Enzyme Commission Number: EC 3.2.1.18. CAS No. 9001-67-6. Neuraminidase. Activity: Type I, 1-5 units/mg protein (Lowry, using NAN-lactose); Type II, 8-24 units/mg protein (Lowry, using NAN-lactose); Type III, > 1.5 units/mg protein. Storage: 2-8°C. Form: Type I, buffered aqueous solution; Aqueous solution, pH 5.5, containing 0.15 M NaCl and 4 mM CaCl2; Type II, buffered aqueous solution, Solution in 50 mM sodium acetate, pH 5.5, containing 0.15 M sodium chloride and 4 mM calcium chloride; Type III, sterile filte | |
| Sodium acetate | Sodium acetate is used as part of a buffer system when combined with acetic acid. Sodium acetate can be used to reduce the bitter taste of oral drugs and enhance the antibacterial properties of the preparations. Sodium acetate is widely used as a preservative in the food industry and as a treatment for metabolic acidosis in premature infants and in hemodialysis solutions. Synonyms: Acetic acid, sodium salt; Sodium acetate anhydrous; Acetic acid sodium salt. Grades: 99%. CAS No. 127-09-3. Molecular formula: C2H3NaO2. Mole weight: 82.03. | |
| Zinc acetate | Zinc acetate. Synonyms: Acetic acid, zinc(II) salt; aceticacid, zinc(II)salt; ai3-04465; Dicarbomethoxyzinc; Zinc acetate, pure, 99%;zinc acetate solution;Zinkdi(acetat);zinc(+2) cation diacetate. CAS No. 557-34-6. Pack Sizes: 1 kg. Product ID: CDC10-0250. Molecular formula: C2H4O2Zn++. Category: Buffering Agents. Product Keywords: Cosmetic Ingredients; Buffering Agents; Zinc acetate; CDC10-0250; 557-34-6; C2H4O2Zn++; Acetic acid, zinc(II) salt; aceticacid,zinc(II)salt; ai3-04465; Dicarbomethoxyzinc; Zinc acetate, pure, 99%; zinc acetate solution; Zinkdi(acetat); zinc(+2) cation diacetate; 209-170-2; MFCD00012454; 557-34-6. Purity: 0.99. Color: Colourless or white efflorescent. EC Number: 209-170-2. Physical State: crystals. Storage: Inert atmosphere,Room Temperature. Boiling Point: 242-4°C. Melting Point: 83-86°C. Density: 1.84 g/cm3. |  |
| Alcohol Dehydrogenase (NADP+ dependent) from Entamoeba species, Recombinant | NADP-dependent isopropanol dehydrogenase belongs to the superfamily of alcohol dehydrogenases with a preference for medium chain secondary alcohols, such as 2- butanol and isopropanol, while it has low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. It is also active with acetaldehyde and propionaldehyde. Group: Enzymes. Synonyms: EC 1.1.1.2; Aromatic Alcohol Dehy. Purity: > 95% by SDS-PAGE. ALR. Mole weight: ~40.9 kDa (SDS-PAGE). Activity: > 60U/mg. Storage: Aliquot and store at -20°C. Avoid repeated freeze thaw cycles. Form: Liquid, 1 mg/mL solution in 50 mM Tris-HCl buffer (pH 8.0) containing 100 mM NaCl and 50% glycerol. Source: E. coli. Species: Entamoeba species. EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: NATE-1590. | |
| Amidase from Pseudomonas aeruginosa, Recombinant | The amidase from Pseudomonas aeruginosa catalyzes the hydrolysis of a small range of short aliphatic amides. Each amidase monomer is formed by a globular four-layer αββα sandwich domain with an additional 81-residue long C-terminal segment. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. Applications: The importance of these hydrolases in biotechnology is growing rapidly, because their potential applications span through chemical and pharmaceutical industries as well as in bioremediation. immobilized amidase can be used efficiently for production of ac...onyms: acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous); amidase; EC 3.5.1.4; acylamide amidohydrolase. Enzyme Commission Number: EC 3.5.1.4. CAS No. 9012-56-0. Amidase. Activity: >200 units/mg protein (biuret). Storage: Store at -20°C. Form: Solution in 50% glycerol containing 7 mM 2-mercaptoethanol and phosphate buffer salt. Source: E. coli. Species: Pseudomonas aeruginosa. acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous); amidase; EC 3.5.1.4; acylamide amidohydrolase. Cat No: NATE-0809. | |
| 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. | |
| Endoglycosidase F1 from Elizabethkingia miricola, Recombinant | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosida...ules. if an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. an endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: Endoglycosidase; Endo F1; Endo-β-N-acetylglucosaminidase F1; Endoglycosidase F1 from Chryseobacterium meningosepticum; Endoglycosidase F1 from Elizabethkingia meningoseptica; Endoglycosidase F1 from Flavobacterium meningosepticum; Endoglycosidase F1; EC 3.2.1.96; 231-791-2. Enzyme Commission Number: EC 3.2.1.96. CAS No. 231-791-2. Endo-β-N-acetylglucosaminidase. Activity: > 16 U/mg, buffered aqueous solution. Storage: 2-8°C. Form: buf | |
| Endoglycosidase H from Streptomyces plicatus, Recombinant | The enzyme Endoglycosidase H is an enzyme with system name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-beta-glucosaminohydrolase. It is a highly specific endoglycosidase which cleaves asparagine-linked mannose rich oligosaccharides, but not highly processed complex oligosaccharides from glycoproteins. It is used for research purposes to deglycosylate glycoproteins. Group: Enzymes. Synonyms: EC 3.2.1.96;. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Endo-β-N-acetylglucosaminidase. Storage: 2-8°C. Form: Type I, buffered aqueous solution, Solution in 0.05 M sodium phosphate, pH 7, containing 25 mM EDTA and preservative; Type II, buffered aqueous solution, Solution in 20 mM Tris HCl, pH 7.5, containing 50 mM NaCl, 1 mM EDTA. Source: E. coli. Species: Streptomyces plicatus. EC 3.2.1.96; Endo H; β-N-Acetylglucosaminidase H; N,N'-diacetylchitobiosyl β-N-acetylglucosaminidase; endo-β-N-acetylglucosaminidase; mannosyl-glycoprotein endo-β-N-acetylglucosamidase; di-N-acetylchitobiosyl β-N-acetylglucosaminidase; endo-β-acetylglucosaminidase; endo-β-(14)-N-acetylglucosaminidase; mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase; endoglycosidase S; endo-N-acetyl-β-D-glucosaminidase; endo-N-acetyl-β-glucosaminidase; endo-&b | |
| Endoglycosidase S (Low Endotoxin) from Streptococcus pyogenes, Recombinant | EndoS LE is an endoglycosidase for deglycosylation of IgG Fc-glycan moieties. IgGZERO(R) LE hydrolyzes Fcglycans on IgG of all human IgG subclasses and IgG from the following species: mouse, rat, monkey, sheep, goat, cow and horse. The enzyme has limited activity on high-mannose and hybrid- type glycans. EndoS LE hydrolyzes the β1,4 linkage between the core GlcNAc residues in the Fc-glycan, leaving the innermost GlcNAc on the Fc. EndoS LE is a low endotoxin product,use endotoxin free material and solutions. Physiological reaction conditions at pH 7. 4 and 37°C yields optimal enzyme activity. Other buffers and pH (6-8) are compatible with enzyme activ.... EndoS LE is for R&D use only. Group: Enzymes. Synonyms: Endoglycosidase S; IgGZERO. Purity: > 95% homogeneity as determined by SDS-PAGE analysis. Endo-β-N-acetylglucosaminidase. Mole weight: 110 kDa. Storage: It is shipped at ambient temperature. It should be stored at -20°C upon arrival. After reconstitution EndoS LE is stable for 1 month at +4-8°C. Form: Lyophilized in 10 mM sodium phosphate, 150 mM NaCl, pH 7. 4, with no preservatives added. Source: E. coli. Species: Streptocoocus pyogenes. Endoglycosidase S; IgGZERO Enzyme; IgGZERO; Endoglycosidase; EndoS; EndoS LE; EndoS Low Endotoxin; IgGZERO LE (Low Endotoxin); IgGZERO LE. Cat No: NATE-1780. | |
| Native Almonds Glycopeptidase A | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Group: Enzymes. Synonyms: EC 3.5.1.52; glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; 83534-39-8; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Activity: > 0.05 unit/mL. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 50 mM Citrate-phosphate buffer, pH 5.0, and BSA. Source: Almonds. EC 3.5.1.52; glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; 83534-39-8; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. Cat No: NATE-0600. | |
| Native Clostridium perfringens (C. welchII) Neuraminidase | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. At least four mammalian sialidase homologs have been descr...ic mesenchymal stem cells in the treatment of f ocal cerebral ischemia. it has also been used in a study to investigate sinonasal terat ocarcinosarcoma with rhabdoid features. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18. Enzyme Commission Number: EC 3.2.1.18. Purity: > 95% (SDS-PAGE). Neuraminidase. Storage: -20°C. Form: buffered aqueous solution; Solution in 100 mM Tris-HCl, 5 mM MgSO4, 250 mM KCl, pH 5.0-5.2. Source: Clostridium perfringens (C. welchII). neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18. Cat No: NATE-0480. | |
| Native Escherichia coli Chloramphenicol Acetyltransferase | Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. Applications: Chloramphenicol acetyltransferase from escherichia coli has been used in a study to assess the construction of a novel expression system in klebsiella pneumoniae and its application for 1,3-propanediol produ...etyl-CoA:chloramphenicol 3-O-acetyltransferase; CAT; 9040-07-7; chloramphenicol acetyltransferase; chloramphenicol acetylase; chloramphenicol transacetylase; CAT I; CAT II; CAT III. CAS No. 9040-7-7. Chloramphenicol Acetyltransferase. Mole weight: mol wt 75 kDa (three identical subunits). Activity: 50,000-150,000 units/mg protein (Lowry). Storage: -20°C. Form: Type I, lyophilized powder. Partially purified; contains Tris buffer salts; Type II, buffered aqueous glycerol solution. Clear, colorless solution in 50% glycerol containing 5 mM Tris-HCl, pH 7.8, and 0.5 mM 2-mercaptoethanol. Source: Escherichia coli. Acetyl-CoA:chloramphenicol 3-O-acetyltransferase; CAT; 9 | |
| 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 Streptococcus pneumoniae α (2?3) Neuraminidase | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Enzyme Commission Number: EC 3.2.1.18. CAS No. 9001-67-6. Neuraminidase. Storage: 2-8°C. Form: buffered aqueous solution. Solution in 50 mM sodium phosphate, pH 7.5. Source: Streptococcus pneumoniae. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Cat No: NATE-0757. | |
| O-Glycosidase from Streptococcus pneumoniae, Recombinant | O-Glycosidase releases unsubstituted Ser-and Thr-linked β-Gal-(1?3)-α-GalNAc (Core 1 type O-glycan) from glycoproteins. Substitutions of the disaccharide core with sialic acid, lactosamine (galactose-N-acetyl glucosamine), or fucose will block hydrolysis and prevent the liberation of the oligosaccharide from the protein. Pretreament with glycolytic enzymes to remove substituent saccharides from the O-glycan may be needed prior to cleavage using O-glycosidase. Group: Enzymes. Synonyms: endo-α-acetylgalactosaminidase; endo-α-N-acetyl-D-galactosaminidase; mucinaminylserine mucinaminidase; D-galactosyl-3-(N-acetyl-α-D-galacto. Enzyme Commission Number: EC 3.2.1.97. CAS No. 9032-92-2. O-Glycosidase. Storage: 2-8°C. Form: buffered aqueous solution; Solution in 50 mM sodium phosphate, pH 7.5. Source: E. coli. Species: Streptococcus pneumoniae. endo-α-acetylgalactosaminidase; endo-α-N-acetyl-D-galactosaminidase; mucinaminylserine mucinaminidase; D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase; endo-α-GalNAc-ase; glycopeptide α-N-acetylgalactosaminidase; D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase; 9032-92-2; EC 3.2.1.97. Pack: Supplied with 5× Reaction Buffer, 250 mM NaH2PO4 pH 5.0. Cat No: NATE-0497. | |
| PNGase F from Elizabethkingia meningoseptica, Recombinant | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Highly purified material can be used for preparative deglycosylation or for analytical applications in gel, in solution, or on blot membranes. ...n 50% (v/v) glycerol and 50% (v/v) 20 mM Potassium Phosphate, pH 7.5. Type III, buffered aqueous solution, Supplied as a solution in 20 mM Tris HCl, pH 7.5, 50 mM NaCl and 1 mM EDTA. Source: E. coli. Species: Elizabethkingia meningoseptica. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Pack: PNGase F was used for deglycosylation of P-glycoprotein in a study to investigate the dual impact of statins on p-glycoprotein and its effect on dox | |
| Ponceau Solution 0.1 % (w/v) in 5% (w/v) acetic acid | 5lt Pack Size. Group: Analytical Reagents, Biochemicals, Buffers, Diagnostic Raw Materials, Organics, Stains & Indicators. Formula: C22H12N4Na4O13S4. CAS No. 6226-79-5. Prepack ID 90029153-5lt. Molecular Weight 760.57. See USA prepack pricing. |  |
| Sodium Acetate Hydrous | Colorless crystals. Uses: buffer solution, textile dyeing. Group: organic salt. CAS No. 6131-90-4. |  |
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