Find where to buy products from suppliers in the USA, including: distributors, industrial manufacturers in America, bulk supplies and wholesalers of raw ingredients & finished goods.
1-(2,3,4,6-Tetra-O-acetyl-b-D-glucopyranosyl)imidazole, a highly efficient glycosylation reagent, has shown remarkable utility in the synthesis of glycans and glycoconjugates. Its applications have expanded to the development of glycosidehydrolase inhibitors as well as in the preparation of oligosaccharides. The versatility and efficacy of this chemical compound make it a valuable tool in glycosylation research. Synonyms: 1-(2,3,4,6-tetra-O-acetyl-b-D-glucopyranosyl)imidazole; 38953-70-7; [(2R,3R,4S,5R,6R)-3,4,5-triacetyloxy-6-imidazol-1-yloxan-2-yl]methyl acetate; DTXSID60855871; 1-(2,3,4,6-Tetra-O-acetyl-beta-D-glucopyranosyl)-1H-imidazole; [(2R,3R,4S,5R,6R)-3,4,5-tris(acetyloxy)-6-(1H-imidazol-1-yl)oxan-2-yl]methyl acetate; (2R,3R,4S,5R,6R)-2-(acetoxymethyl)-6-(1H-imidazol-1-yl)tetrahydro-2H-pyran-3,4,5-triyl triacetate. CAS No. 38953-70-7. Molecular formula: C17H22N2O9. Mole weight: 398.4.
1,4-b-D-Cellotetraitol
1,4-b-D-Cellotetraitol is a saccharide that can acts as a chemical probe for studying GlycosideHydrolase Enzyme mechanisms, which are involved in research of various diseases including Gaucher's disease and Tay-Sachs disease. CAS No. 5548-55-0. Molecular formula: C24H44O21. Mole weight: 668.59.
1,4-b-D-Xylopentaose
1,4-b-D-Xylopentaose is a hemicellulose-derived pentasaccharide. It's instrumental for studying xylanases and glycosidehydrolases and their role in the degradation of complex carbohydrates within the human digestion system. CAS No. 49694-20-4. Molecular formula: C25H42O21. Mole weight: 678.59.
2,4-Dinitrophenyl α-D-Galactopyranoside
2,4-Dinitrophenyl α-D-Galactopyranoside is used in the synthesis of 2,4-Dinitrophenyl Glycoside and in the glycosidehydrolases anlaysis. CAS No. 25694-52-4. Molecular formula: C12H14N2O10. Mole weight: 346.25.
2,4-Dinitrophenyl α-D-Galactopyranoside
2,4-Dinitrophenyl α-D-Galactopyranoside is used in the synthesis of 2,4-Dinitrophenyl Glycoside. It is also used in the anlaysis of glycosidehydrolases. Group: Biochemicals. Grades: Highly Purified. CAS No. 25694-52-4. Pack Sizes: 10mg, 100mg. Molecular Formula: C12H14N2O10, Molecular Weight: 346.25. US Biological Life Sciences.
2-Azido-4,6-O-benzylidene-N-Boc-1,2,5-trideoxy-1,5-imino-D-glucitol, a chemical compound commonly employed in the biomedical industry to investigate the inhibitory properties of glycosidehydrolases, exhibits tremendous potential for treating ailments associated with carbohydrate metabolism, such as diabetes and obesity. Its integration in the pharmaceutical field has garnered significance, with researchers observing its dynamic properties and investigating how its unique molecular structure impacts the inhibition of glycosidehydrolases. Molecular formula: C14H24N4O5. Mole weight: 328.36.
2-Nitrophenyl a-D-glucopyranoside
2-Nitrophenyl α-D-glucopyranoside is a highly esteemed compound, serving as an impeccable tool for the meticulous investigation of enchanting enzymatic activities and the momentous impact of potent inhibitors. Its illustrious presence in the realm of scientific research is indubitably intertwined with the elucidation of the captivating complexities surrounding glycosidases and glycosidehydrolases. Boasting an incomparable reactivity as a substrate, this extraordinary compound facilitates the striking detection and meticulous quantification of these celestial enzymes. Synonyms: 2-Nitrophenyl a-D-glucopyranoside; 56193-44-3; SCHEMBL150631; r-nitrophenyl alpha-d-glucopyranoside; AKOS015919352; HY-148672; CS-0636848. CAS No. 56193-44-3. Molecular formula: C12H15NO8. Mole weight: 301.25.
2-Nitrophenyl b-D-cellobioside
2-Nitrophenyl b-D-cellobioside, a chemical compound utilized in the realm of enzymology and biochemistry, finds its purpose in the detection of different types of enzymes, especially glycosidehydrolases. Its functionalities are not limited to this, however, as it can also be employed to analyze carbohydrate-binding proteins. Widely renowned for its ability to influence the development of biosensors for detecting environmental contaminants, this product stands to revolutionize the approach to the pesticide problem that currently plagues our society. Synonyms: 2-Nitrophenyl β-D-cellobioside; ONP-cellobioside; o-Nitrophenyl β-D-Cellobioside; 2-Nitrophenyl 4-O-β-D-Glucopyranosyl-β-D-glucopyranoside. Grades: ≥95%. CAS No. 70867-33-3. Molecular formula: C18H25NO13. Mole weight: 463.39.
3,5-Dinitrosalicylic acid 99+% (HPLC)
3,5-Dinitrosalicylic acid (DNS) is used in colorimetric determination of reducing sugars and to analyze glycosidase (glycosidehydrolase) activity by quantitation of enzymatically released reducing sugar. The dinitrosalicylic acid method has been compared to the Nelson-Somogi colorimetric method. 3,5-Dinitrosalicylic acid (DNS) has been used to stop the reaction in in vitro α-amylase inhibition study. It has also been used for the quantitation of enzymatically released reducing sugars. Group: Biochemicals. Alternative Names: 2-Hydroxy-3,5-dinitro-benzoic Acid; 2-Hydroxy-3,5-dinitrobenzoic Acid; 3,5-Dinitro-2-hydroxybenzoic Acid; NSC 181. Grades: Highly Purified. CAS No. 609-99-4. Pack Sizes: 25g, 100g, 250g, 1Kg. Molecular Formula: C7H4N2O7. US Biological Life Sciences.
Worldwide
4-Methylphenyl b-D-galactopyranoside
4-Methylphenyl b-D-galactopyranoside is a valuable compound exhibiting potential as a substrate for various enzymatic assays and commonly employed in the biochemical analysis of glycosidehydrolases. This compound plays a crucial role in understanding and discovering novel therapeutic drugs, particularly in research related to carbohydrate metabolism and galactoside-specific enzymes. Synonyms: p-Tolyl-b-D-galactopyranoside. CAS No. 3150-22-9. Molecular formula: C13H18O6. Mole weight: 270.28.
4-Nitrophenyl 2-acetamido-2-deoxy-4-O-(b-D-galactopyranosyl)-a-D-glucopyranoside, an indispensable compound in the realm of biomedicine, boasts a multitude of uses. Embraced widely in glycosylation research, it unravels the intricate tapestry of carbohydrates' biological phenomena. Employed as a substrate for enzyme assays, this compound delves into the realm of glycosidehydrolases, sugar transporters, and carbohydrate metabolism. Synonyms: Gal-b-1,4-GlcNAc-a-PNP PNP-N-Acetyl-a-D-lactosamine PNP-a-LacNAc. CAS No. 184377-56-8. Molecular formula: C20H28N2O13. Mole weight: 504.44.
4-Nitrophenyl 2-O-(a-D-glucopyranosyl)-a-D-glucopyranoside is a highly intricate biomedical compound, acting as an effectively stifling glycosidehydrolase that governs carbohydrate metabolism. This potent enzyme inhibitor has applicantion in research of ameliorating aberrant glucose processing. Synonyms: 4-Nitrophenyl a-kojibioside PNP-a-kojibioside. CAS No. 147103-31-9. Molecular formula: C18H25NO13. Mole weight: 463.39.
4-Nitrophenyl a-L-arabinofuranoside
4-Nitrophenyl α-L-arabinofuranoside, a remarkable biomedical product, emerges as a paramount asset for addressing specific afflictions. Serving as a substrate mimetic within enzymatic analyses and scientific investigations, this chemical compound unveils its potential. Its intricate configuration facilitates the in-depth scrutiny of diverse glycosidehydrolases and glycosyltransferases intricately entwined in carbohydrate metabolism. With its implications in drug discovery and precision medicine, this compound incessantly enlightens us about the pivotal role these enzymes play in maintaining sound health and combating diseases. Synonyms: 4-Nitrophenyl a-L-arabinofuranoside; 4-NITROPHENYL-ARA; 4-Nitrophenyl-alpha-L-arabinofuranoside; 4-nitrophenyl alpha-L-arabinofuranoside; 4-Nitrophenyl |A-L-arabinofuranoside; pNP-alpha-L-Arabinofuranoside; (2S,3R,4R,5S)-2-(hydroxymethyl)-5-(4-nitrophenoxy)oxolane-3,4-diol; p-Nitrophenyl alpha-L-arabinofuranoside; alpha-L-Arabinofuranoside, 4-nitrophenyl; (2S,3R,4R,5S)-2-(hydroxymethyl)-5-(4-nitrophenoxy)tetrahydrofuran-3,4-diol; pNPalphaAraf; 4-Nitrophenyla-L-arabinofuranoside; p-Nitrophenylalpha-L-arabinofuranoside. CAS No. 6892-58-6. Molecular formula: C11H13NO7. Mole weight: 271.22.
4-Nitrophenyl b-L-arabinopyranoside
4-Nitrophenyl b-L-arabinopyranoside is a valuable substrate for biomedical applications, specifically in the measurement of glycosidehydrolase activity, such as β-D-arabinofuranosidase, in drug discovery and enzymatic studies. Additionally, it is utilized in the study of L-arabinose and xylose metabolism in bacteria and fungi, and elucidates their relevance to pathways implicated in diseases including diabetes. Through utilization of this specialized substrate, significant advances can be made in the fields of biomedicine and microbiology research. Synonyms: PNP-arabinoside; (2R,3R,4S,5S)-2-(4-Nitrophenoxy)tetrahydro-2H-pyran-3,4,5-triol; P-nitrophenyl β-L-arabinopyranoside. Grades: ≥95%. CAS No. 72732-54-8. Molecular formula: C11H13NO7. Mole weight: 271.22.
4-Nitrophenyl O-(N-acetyl-α-neuraminosyl)-(2-3)-β-D-galactopyranosyl-(1-4)-2-acetamido-2-deoxy-β-D-glucopyranoside, a compound of interest in biomedical research, presents a fascinating opportunity to explore cell recognition and immune response mechanisms. Leveraging its properties, scientists can delve into the involvement of glycosidases in lysosomal storage diseases and analyze the enzymatic activity of glycosidehydrolases. Notably, this compound holds promise in developing therapeutics that can effectively combat drug-resistant bacterial infections. Synonyms: Neu5Aca(2-3)Galb(1-4)GlcNAc-b-pNP. CAS No. 501427-92-5. Molecular formula: C31H45N3O21. Mole weight: 795.70.
4-O-(a-D-Glucopyranosyl) moranoline
4-O-(α-D-Glucopyranosyl) moranoline, a compound of significant value in the biomedical realm, possesses potential advantages for addressing certain medical conditions. Within drug development, it specifically targets enzymes associated with diverse metabolic processes, offering therapeutic prospects encompassing diabetes, cancer, and cardiovascular ailments. Uses: Glycosidehydrolase inhibitors. Synonyms: G1M 4-O-(a-D-Glucopyranosyl)-1-deoxynojirimycin. CAS No. 80312-32-9. Molecular formula: C12H23NO9. Mole weight: 325.32.
α(1-3,4,6) Galactosidase from Green coffee bean, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. GLA. Mole weight: 39700 daltons. Activity: 71,000 units/mg. Storage: 4°C. Form: 20 mM Tris-HCl (pH 7.5), 50 mM NaCl and 1 mM EDTA. Source: E. coli. Species: Green coffee bean. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α(1-3,4,6) Galactosidase. Cat No: NATE-1263.
α(1-3,6) Galactosidase from Xanthomonas manihotis, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Α1-3,6 galactosidase is a highly specific exoglycosidase that catalyzes the hydrolysis of α1-3 and α1-6 linked d-galactopyranosyl residues from oligosaccharides. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Purity: > 95% determined by SDS-PAGE. GLA. Mole weight: 70000 daltons. Activity: 137,000 units/mg. Storage: Recommended storage temperature is 4°C. Avoid repeated freeze/thaw cycles. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 1 mM Na2EDTA. Source: E. coli. Species: Xanthomonas manihotis. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α(1-3,6) Galactosidase. Cat No: NATE-1279.
α(2-3,6,8) Neuraminidase from Clostridium perfringens, Recombinant
Neuraminidase enzymes are glycosidehydrolase 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. Neuraminidase is the common name for acetyl-neuraminyl hydrolase (sialidase). this neuraminidase catalyzes the hydrolysis of α2-3, α2-6, and α2-8 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-ne. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 43 kDa. Activity: ~225,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 5 mM Na2EDTA. Source: E. coli. Species: Clostridium perfringens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3,6,8) Neuraminidase. Cat No: NATE-1277.
α(2-3) Neuraminidase from Salmonella typhimurium LT2, Recombinant
Neuraminidase enzymes are glycosidehydrolase 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. Α2-3 neuraminidase is a highly specific exogl... sialyl linkages and shows only trace activity against α2-8 sialyl linkages. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Neuraminidase. Mole weight: 41 kDa. Activity: ~11,300,000 units/mg. Storage: Store at 4°C or in small aliquots at -20°C. Avoid repeated freeze/thaw cycles. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C), and 5 mM Na2EDTA. Source: E. coli. Species: Salmonella typhimurium LT2. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3) Neuraminidase. Cat No: NATE-1276.
α(2-3) Neuraminidase S from Streptococcus pneumoniae, Recombinant
Neuraminidase enzymes are glycosidehydrolase 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. Neuraminidase is the common name for acetyl-neurami...;2-3 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 74000 daltons. Activity: 160,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 1 mM EDTA. Source: E. coli. Species: Streptococcus pneumoniae. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3) Neuraminidase S; α(2-3) Neuraminidase. Cat No: NATE-1275.
α-D-xyloside xylohydrolase
The enzyme catalyses hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide. Representative α-xylosidases from glycosidehydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product. Group: Enzymes. Synonyms: α-xylosidase. Enzyme Commission Number: EC 3.2.1.177. α-Xylosidase. 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-3860; α-D-xyloside xylohydrolase; EC 3.2.1.177; α-xylosidase. Cat No: EXWM-3860.
α-Galactosidase 110A from Bacteroides fragilis, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.-. CAS No. 9025-35-8. Purity: >90% by SDS-PAGE. GLA. Mole weight: 67.9 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides fragilis. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 110A. Cat No: NATE-1405.
α-Galactosidase 110A from Bacteroides thetaiotaomicron, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >50% by SDS-PAGE. GLA. Mole weight: 65.1 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides thetaiotaomicron. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 110A. Cat No: NATE-1403.
α-Galactosidase 27A from Clostridium cellulolyticum, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >90% by SDS-PAGE. GLA. Mole weight: 44.0 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Clostridium cellulolyticum. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 27A. Cat No: NATE-1400.
α-Galactosidase 4A from Bacillus halodurans, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >90% by SDS-PAGE. GLA. Mole weight: 51.8 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus halodurans. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 27A. Cat No: NATE-1404.
α-Galactosidase 95A from Bacteroides ovatus, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >90% by SDS-PAGE. GLA. Mole weight: 91 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides ovatus. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 95A. Cat No: NATE-1406.
α-Galactosidase 97A from Bacteroides thetaiotaomicron, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >50% by SDS-PAGE. GLA. Mole weight: 74.7 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides thetaiotaomicron. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 97A. Cat No: NATE-1402.
α-Galactosidase 97B from Bacteroides thetaiotaomicron, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >90% by SDS-PAGE. GLA. Mole weight: 74.9 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides thetaiotaomicron. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 97B. Cat No: NATE-1401.
α-Galactosidase, Aspergillus niger
α-Galactosidase, Aspergillus niger (EC 3.2.1.22), that is, α-galactosidase, is a glycosidehydrolase that widely exists in animals, plants and microorganisms, and is often used in biochemical research. α-Galactosidase catalyzes the hydrolysis of α-1,6-linked terminal galactose residues, including galactooligosaccharides, galactomannans, and galactolipids. Catalyzes many catabolic processes including cleavage of glycoproteins, glycolipids and polysaccharides [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: EC 3.2.1.22. CAS No. 9025-35-8. Pack Sizes: 5 g; 10 g. Product ID: HY-P2871.
α-Galactosidase from Cellvibrio mixtus, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: > 95 % as judged by SDS-PAGE. GLA. Mole weight: 44582.3 Da. Activity: 150 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Lyophilised powder. Source: Cellvibrio mixtus ATCC 12120. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-1175.
α-Galactosidase from Clostridium cellulolyticum, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: > 95 % as judged by SDS-PAGE. GLA. Mole weight: 64179.5 Da. Activity: 186.7 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Clostridium cellulolyticum H10. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-1176.
α-Galactosidase, positionally specific from Escherichia coli, Recombinant
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Activity using maltose as substrate at ph 6.0 at 25 deg c is ~2x > that obtained using p-nitrophenyl-α-d-glucoside as substrate at ph 6.8 at 37 oc. protein determined by biuret. Applications: Α-glucosidase is potential enzyme for the biosynthesis of complex carbohydrates. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. GLA. Activity: > 50 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: E. coli. Species: Escherichia coli. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0293.
α-Glucosidase from Escherichia coli, Recombinant
Glycosidehydrolases (also called glycosidases or glycosyl hydrolases) assist in the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose and hemicellulose, in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms (e.g., viral neuraminidases) and in normal cellular function (e.g., trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds. Group: Enzymes. Synonyms: Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucra. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. Purity: > 95 % as judged by SDS-PAGE. α-Glucosidase. Mole weight: 72992.3 Da. Activity: 34.1 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; alpha-glucopyranosidase; glucosidoinvertase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase; glycosidases; glycosyl hydrolases; α-Glucosidase. Cat No: NATE-1177.
α-N-Acetylgalactosaminidase from Chryseobacterium meningosepticum, Recombinant
α-N-acetylgalactosaminidase (EC 3.2.1.49) is a glycosidehydrolase from bacteria and animals, also known as nagalase. The human gene that codes for this enzyme is NAGA. Mutations in this gene and the deficiency in alpha-N-acetylgalactosaminidase activity have been identified as the cause of Schindler disease. Group: Enzymes. Synonyms: EC 3.2.1.49; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. α-NAGA. Mole weight: 47 kDa. Storage: at -20°C. Source: E. coli. Species: Chryseobacterium meningosepticum. EC 3.2.1.49; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. Cat No: NATE-1259.
α-Rhamnosidase 78A from Streptomyces avermitilis, Recombinant
A thermostable Alpha-L-Rhamnosidase (Naringinase, RhamA) that catalyzes the cleavage of the bond between terminal L (+)-rhamnose and the aglycone of rhamnose-containing glycosides. The enzyme is very active on naringin but has also substantial activity with hesperidin as substrate. Group: Enzymes. Synonyms: glycosidehydrolase; RhamA; naringinase; hesperidinase; α-L-rhamnosidase A; α-L-rhamnosidase N; α-L-rhamnoside rhamnohydrolase; EC 3.2.1.40. Enzyme Commission Number: EC 3.2.1.40. CAS No. 37288-35-0. Purity: >90% as judged by SDS-PAGE. RhamA. Mole weight: 115 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Streptomyces avermitilis. glycosidehydrolase; RhamA; naringinase; hesperidinase; α-L-rhamnosidase A; α-L-rhamnosidase N; α-L-rhamnoside rhamnohydrolase; EC 3.2.1.40; α-Rhamnosidase. Cat No: NATE-1510.
β-Acetylglucosaminidase 18A from Bacteroides thetaiotaomicron, Recombinant
β-acetylglucosaminidase 18A, is an enzyme from Bacteroides thetaiotaomicron that participates in the endohydrolysis of the diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the (Man(GlcNAc)(2))Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Recombinant BtAcp18A (GH18), purified from Escherichia coli, is a single domain family 18 GlycosideHydrolase (GH18). Group: Enzymes. Synonyms: beta-N-acetyl-D-hexosaminide; N-acetylhexosaminohydrolase; β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Purity: >50% by SDS-PAGE. β-N-Acetylhexosaminidase. Mole weight: 50.3 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides thetaiotaomicron. beta-N-acetyl-D-hexosaminide; N-acetylhexosaminohydrolase; β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Cat No: NATE-1291.
β-Galactosidase, E. coli
β-Galactosidase (EC 3.2.1.23) is a glycosidehydrolase that hydrolyzes the β-glycosidic bonds formed between galactose and its organic moieties. In E.coli , the lacZ gene is the structural gene of β-galactosidase, which can be used as part of the induction system lac operon. β-Galactosidase can hydrolyze lactose to form glucose and galactose, and enter glycolysis; it can also catalyze the transgalactosylation of lactose into allolactose; allolactose can be cracked into monosaccharides [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: EC 3.2.1.23; GAL. CAS No. 9031-11-2. Pack Sizes: 1 KU; 5 KU. Product ID: HY-P2869.
β-Glucosidase, almond
β-Glucosidase, almond is the rate-limiting enzyme of degradation of cellulose. β-Glucosidase is a major group among glycosidehydrolases. β-Glucosidase is involved in the degradation of cellulose in soils and has potential for monitoring biological soil quality [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9001-22-3. Pack Sizes: 50 mg; 100 mg. Product ID: HY-P2775.
Cellobiohydrolase I
Cellobiohydrolase I (Cbh1) belongs to glycosidehydrolase family 7 (GH7) that catalyzes the processive hydrolysis of cellulose into cellobiose [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Cbh1. CAS No. 37329-65-0. Pack Sizes: 5 U. Product ID: HY-E70107.
cellodextrin phosphorylase
This enzyme belongs to GH (glycosidehydrolases) family 94. The systematic name of this enzyme class is 1,4-beta-D-oligo-D-glucan:phosphate alpha-D-glucosyltransferase. This enzyme is also called beta-1,4-oligoglucan:orthophosphate glucosyltransferase. Group: Enzymes. Synonyms: β-1,4-oligoglucan:orthophosphate glucosyltransferase; 1,4-β-D-oligo-D-glucan:phosphate α-D-glucosyltransferase. Enzyme Commission Number: EC 2.4.1.49. CAS No. 37277-58-0. 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-2595; cellodextrin phosphorylase; EC 2.4.1.49; 37277-58-0; β-1,4-oligoglucan:orthophosphate glucosyltransferase; 1,4-β-D-oligo-D-glucan:phosphate α-D-glucosyltransferase. Cat No: EXWM-2595.
cellulose 1,4-β-cellobiosidase (reducing end)
Some exocellulases, most of which belong to the glycosidehydrolase family 48 (GH48, formerly known as cellulase family L), act at the reducing ends of cellulose and similar substrates. The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism. It liberates cellobiose units from the reducing end by hydrolysis of the glycosidic bond, employing an inverting reaction mechanism. Different from EC 3.2.1.91, which attacks cellulose from the non-reducing end. Group: Enzymes. Synonyms: CelS; CelSS; endoglucanase SS; cellulase SS; cellobiohydrolase CelS; Cel48A. Enzyme Commission Number: EC 3.2.1.176. Cellulose 1,4-beta-cellobiosidase. 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-3859; cellulose 1,4-β-cellobiosidase (reducing end); EC 3.2.1.176; CelS; CelSS; endoglucanase SS; cellulase SS; cellobiohydrolase CelS; Cel48A. Cat No: EXWM-3859.
DEXTRANASE
DEXTRANASE. Synonyms: dextranase from paecilomyces lilacinus;Dextranase Paecilomyces lilacinus;dextranase partially purified. CAS No. 9025-70-1. Product ID: CDF4-0042. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; DEXTRANASE; CDF4-0042; 9025-70-1; 232-803-9; 9025-70-1. Purity: 0.99. Color: Brown. EC Number: 232-803-9. Physical State: Solution. Storage: 2-8°C. Product Description: Dextranase from fungi belong to the glycosidehydrolase families (GH) 49. Dextranase from Penicillium sp. are stable at varying temperature and pH.
(D-Galactopyranosyl)-b-D-thiogalactopyranoside
(D-Galactopyranosyl)-b-D-thiogalactopyranoside is a crucial compound widely used in the biomedical industry. It acts as a substrate analogue for enzymes involved in carbohydrate metabolism and is utilized in the study of glycosidehydrolases. It aids in the exploration of enzyme activity and glycosylation pathways, facilitating research on carbohydrate-related diseases and drug development. Synonyms: Thiodigalactoside TDG. CAS No. 51555-87-4. Molecular formula: C12H22O10S. Mole weight: 358.36.
Endo-1,4-β-xylanase
Endo-1,4-β-xylanase (Xylanase) is an arabinoxylan (AX) degrading enzyme and a glycosidehydrolase, is often used in biochemical studies. Endo-1,4-β-xylanase cleaves the β-xylosidic bond between two d-xylopyranosyl residues linked in β-(1,4) [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: CtXyn11A; EC 3.2.1.8. CAS No. 9025-57-4. Pack Sizes: 1 g; 5 g; 10 g. Product ID: HY-P3017.
exo-1,4-β-D-glucosaminidase
Chitosan is a partially or totally N-deacetylated chitin derivative that is found in the cell walls of some phytopathogenic fungi and comprises D-glucosamine residues with a variable content of GlcNAc residues. Acts specifically on chitooligosaccharides and chitosan, having maximal activity on chitotetraose, chitopentaose and their corresponding alcohols. The enzyme can degrade GlcN-GlcNAc but not GlcNAc-GlcNAc. A member of the glycosidehydrolase family 2 (GH-2). Group: Enzymes. Synonyms: CsxA; GlcNase; exochitosanase; GlmA; exo-β-D-glucosaminidase; chitosan exo-1,4-β-D-glucosaminidase. Enzyme Commission Number: EC 3.2.1.165. 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-3847; exo-1,4-β-D-glucosaminidase; EC 3.2.1.165; CsxA; GlcNase; exochitosanase; GlmA; exo-β-D-glucosaminidase; chitosan exo-1,4-β-D-glucosaminidase. Cat No: EXWM-3847.
glycyrrhizin hydrolase
The enzyme from Aspergillus niger is specific for the hydrolysis of the triterpenoid glycoside glycyrrhizin from roots of Glycyrrhiza sp. Group: Enzymes. Synonyms: glycyrrhizinate β-glucuronidase; glycyrrhizin β-hydrolase; glycyrrhizinic acid hydrolase. Enzyme Commission Number: EC 3.2.1.128. CAS No. 102484-56-0. 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-3811; glycyrrhizin hydrolase; EC 3.2.1.128; 102484-56-0; glycyrrhizinate β-glucuronidase; glycyrrhizin β-hydrolase; glycyrrhizinic acid hydrolase. Cat No: EXWM-3811.
Hemicellulase
Hemicellulase is a hemicellulose-targeting hydrolase that breaks down the binding of glucose and polymers to water molecules present in plant fibers. Hemicellulase specifically degrades hemicellulose (such as xylan and mannan) in plant cell walls by hydrolyzing β-1,4-xylosidic bonds and ester bonds (such as acetyl and ferulic acid ester bonds). Hemicellulase relies on the synergistic action of the glycosidehydrolase (GH) and carbohydrate esterase (CE) families to achieve efficient hydrolysis through acid-base catalysis (such as Glu/Asp residues) and substrate binding pockets. Hemicellulase can be used in the food industry (such as improving bread texture), biofuel production (lignocellulose pretreatment) and paper industry (biobleaching) [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9025-56-3. Pack Sizes: 5 g; 10 g; 25 g. Product ID: HY-P2875.
Ikarisoside F
Ikarisoside F, a flavonol glycoside from Vancouveria hexandra, could bind to AdoHcy hydrolase. Synonyms: Ikarisoside F. Grades: >98%. CAS No. 113558-14-8. Molecular formula: C31H36O14. Mole weight: 632.61.
Keratan sulfate Endo-N-acetylglucosaminidase 111A from Bacillus circulans
BcKsh111A (GH111), E.C. number 3.2.1.-, is an endo-β -N-acetylglucosaminidase from Bacillus circulans. Recombinant BcKsh111A (GH111), purified from Escherichia coli, is a single domain family 111 GlycosideHydrolase (GH111). Group: Enzymes. Synonyms: endo-β -N-acetylglucosaminidase; single domain family 111 GlycosideHydrolase; Keratan sulfate Endo-N-acetylglucosaminidase 111A; Keratan sulfate Endo-N-acetylglucosaminidase; GH111. Enzyme Commission Number: EC 3.2.1.-. Purity: >90% as judged by SDS-PAGE. α-L-Arabinofuranosidase. Mole weight: 69,07 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus circulans. endo-β -N-acetylglucosaminidase; single domain family 111 GlycosideHydrolase; Keratan sulfate Endo-N-acetylglucosaminidase 111A; Keratan sulfate Endo-N-acetylglucosaminidase; GH111. Cat No: NATE-1940.
Lysozyme 23A from Bacillus subtilis, Recombinant
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycosidehydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequ... lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Purity: >90% by SDS-PAGE. Lysozyme. Mole weight: 20.5 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus subtilis. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2; Lysozyme 23A. Cat No: NATE-1455.
Lysozyme 25A from Streptococcus pneumoniae, Recombinant
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycosidehydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in ... LYZ; LZM; EC 3.2.1.17; 9001-63-2. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Purity: >90% by SDS-PAGE. Lysozyme. Mole weight: 26.3 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Streptococcus pneumoniae. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2; Lysozyme 25A. Cat No: NATE-1456.
Lysozyme from Human, Recombinant
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycosidehydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence and structure, making them part of the same family. In humans, the lysozyme enzyme is encoded by the LYZ gene. Group: Enzymes. Synonyms: muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Lysozyme. Activity: > 100 ,000 units/mg protein (E1%/280). Storage: -70°C. Form: lyophilized powder. Source: Rice. Species: Human. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Pack: Package size based on protein content. Cat No: NATE-0434.
Maltose phosphorylase
Maltose phosphorylase is a dimerase which catalyzes the transformation of maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose. Maltose phosphorylases have been classified in family 65 of the glycosidehydrolases [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: E.C. 2.4.1.8. CAS No. 9030-19-7. Pack Sizes: 50 U; 250 U. Product ID: HY-P2741.
Miglitol
Miglitol (BAY-m1099) is an orally active antidiabetic compound that inhibits the breakdown of glycoconjugates into glucose. Miglitol inhibits glycosidehydrolase enzymes called α-glucosidases. Miglitol inhibits oxidative stress-induced apoptosis and mitochondrial ROS over-production in endothelial cells by enhancement of AMP-activated protein kinase. Dietary supplementation with Miglitol from pre-onset stage in OLETF rats delays the onset and development of diabetes and preserves the insulin secretory function of pancreatic islets [1] [2] [3] [4]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: BAY1099; BAY-m1099. CAS No. 72432-03-2. Pack Sizes: 10 mM * 1 mL; 500 mg; 1 g; 5 g. Product ID: HY-B0481.
Neuraminidase enzymes are glycosidehydrolase 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. Applications: Neuraminidase is an important deglycosyl... resulting in partial or complete o-deglycosylation. sds-page and maldi-tof ms are typically utilized in purification, structural analysis, and sequencing process. these techniques also remove heterogeneity and charge from the glycoprotein. 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: Lyophilized powder. Source: Arthrobacter ureafaciens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Cat No: NATE-0756.
Native Chicken α-N-Acetylgalactosaminidase
α-N-acetylgalactosaminidase (EC 3.2.1.49) is a glycosidehydrolase from bacteria and animals, also known as nagalase. The human gene that codes for this enzyme is NAGA. Mutations in this gene and the deficiency in alpha-N-acetylgalactosaminidase activity have been identified as the cause of Schindler disease. Group: Enzymes. Synonyms: EC 3.2.1.49; 9075-63-2; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. Enzyme Commission Number: EC 3.2.1.49. CAS No. 9075-63-2. α-NAGA. Source: Chicken Liver. Species: Chicken. EC 3.2.1.49; 9075-63-2; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. Cat No: NATE-0755.
Native Chicken Lysozyme chloride form
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycosidehydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence ...lmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Lysozyme. Mole weight: mol wt ~14.3 kDa. Activity: > 100,000 units/mg protein (E1%/280). Storage: -20°C. Form: Lyophilized powder containing sodium chloride and sodium acetate. Source: Chicken egg white. Species: Chicken. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Cat No: NATE-0432.
Neuraminidase enzymes are glycosidehydrolase 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.
Neuraminidase enzymes are glycosidehydrolase 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. Neuraminidase enzymes are hydrolase enzymes that promo...cells. 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, 6-10 units/mg protein (using 4MU-NANA), 2-5 units/mg protein (mucin); Type II, 10-20 units/mg protein (using 4MU-NANA), 3.5-8.0 units/mg protein (mucin); Type III, > 50 units/mg protein (using 4MU-NANA). Storage: -20°C. Form: lyophilized powder. Source: Clostridium perfringens (C. welchII). neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Cat No: NATE-0479.
Native Cucumis melo α-Galactosidase I, Alkaline
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Applications: Alkaline α-galactosidase i was used to assay enzyme activity with 2 mmp-nitrophenyl-α-d-galactoside as substrate at ph 6.5 to compare with the enzyme activity of α-gal a isolated and purified from sf-9 insect cells infected with a recombinant baculovirus encoding normal α-gal a gene. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. GLA. Mole weight: apparent mol wt ~84 kDa by SDS-PAGE. Storage: -20°C. Form: The product is supplied as a lyophilized powder containing Tris-HCl buffer salts, DTT, EDTA, and NaCl. Source: Cucumis melo. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0291.
Native Environmental DNA Pustulanase (β-glucanase)
A thermostable β-1,6-endoglucanase or pustulanase (E.C. 3.2.1.75) which catalyses the cleavage of β-1,6 bonds in pustulan and other beta-glucans containing 1,6 linked glucose units. The enzyme is now a component in a standard assay for beta-glucan from Bakers yeast as documented in US Pharmacopeia Food and Chemicals Index. Group: Enzymes. Synonyms: EC 3.2.1.75; glycosidehydrolase; pustulanase; glucan endo-1,6-β-glucosidase; 6-β-D-glucan glucanohydrolase; endo-1,6-β-glucanase; β-1?6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase. Enzyme Commission Number: EC 3.2.1.75. CAS No. 37278-39-0. Pustulanase. Source: Proprietary metagenome environmental DNA. Species: Environmental DNA. EC 3.2.1.75; glycosidehydrolase; pustulanase; glucan endo-1,6-β-glucosidase; 6-β-D-glucan glucanohydrolase; endo-1,6-β-glucanase; β-1?6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase. Cat No: NATE-0645.
Native Green coffee beans α-Galactosidase
Alpha-galactosidase is a glycosidehydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. GLA. Activity: > 9 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4 solution, pH 6.0, containing BSA. Source: Green coffee beans. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0292.
Native Human Lysozyme
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycosidehydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence and structure, making them part of the same family. In humans, the lysozyme enzyme is encoded by the LYZ gene. Group: Enzymes. Synonyms: muramidase; globulin G; mucopeptide gl. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Purity: > 95% (SDS-PAGE). Lysozyme. Activity: > 100 ,000 units/mg protein (E1%/280). Storage: -20°C. Form: Lyophilized from 50 mM sodium acetate, pH 6.0, with 100 mM NaCl. Source: Human neutrophils. Species: Human. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Cat No: NATE-0433.
Native Jack bean α (1-2,3,6)-Mannosidase
α-Mannosidase is an acid hydrolase which is located in plant vacuoles and is thought to be involved with the turnover of N-linked glycoproteins. α-Mannosidase has been shown to inhibit the proliferation of B-lymphocytes. α-Mannosidase from Canavalia ensiformis is a tretamer composed of two subunits that each contain two components at 44 and 66 kDa. Group: Enzymes. Synonyms: α-mannosidase; α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranos. Purity: Contaminating glycosidase activities are determined using p-nitrophenyl glycoside substrates and are reported when they are > 0.001% of the enzyme activity. Mannosidase. Mole weight: ~190 kDa daltons. Activity: > 150 U/mL. Stability: The enzyme is stable at 2-8°C and-20°C. The enzyme is unstable below pH 5.5 unless Zn2+ ions are present. It is stable between 6.0-8.5 for 17 hours at 37°C. Ag+ and Hg2+ are potent inhibitors of enzyme activity. Storage: Store at 2-8°C Shipped with cold pack for next day delivery. Form: A sterile-filtered solution in 20 mM Tris-HCl, 20 mM NaCl, pH 7.5. Source: Jack bean. α-mannosidase; α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranosidase; 1,2-α-mannosidase; 1,2-α-D-mannosidase; exo-α-mannosidase; EC 3.2.1.24; 9025-42-7; Mannosidase. Cat No: NATE-0438.
Sucrose phosphorylase (EC. 2.4.1.7) is an important enzyme in the metabolism of sucrose and regulation of other metabolic intermediates. Sucrose phosphorylase is in the class of hexosyltransferases. More specifically it has been placed in the retaining glycosidehydrolases family although it catalyzes a transglycosidation rather than hydrolysis. Sucrose phosphorylase catalyzes the conversion of sucrose to D-fructose and α-D-glucose-1-phosphate. It has been shown in multiple experiments that the enzyme catalyzes this conversion by a double displacement mechanism. Group: Enzymes. Synonyms: Sucrose Phosphorylase; EC 2.4.1.7; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Enzyme Commission Number: EC. 2.4.1.7. CAS No. 9074-06-0. Sucrose Phosphorylase. Activity: > 100 units/mg protein. Storage: Store at -20°C. Form: Lyophilized powder. Source: Leuconostoc Mesenteroides. Sucrose Phosphorylase; EC 2.4.1.7; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Cat No: NATE-0890.
Native Microorganism α-Glucosidase (MALTASE)
Glycosidehydrolases (also called glycosidases or glycosyl hydrolases) assist in the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose and hemicellulose, in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms (e.g., viral neuraminidases) and in normal cellular function (e.g., trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds. Applications: This enzyme is useful for structural investi...tase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase; glycosidases; glycosyl hydrolases; α-Glucosidase. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. Activity: 20U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; alpha-glucopyranosidase; glucosidoinvertase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase; glycosidases; glycosyl hydrolases; α-Glucosidase. Cat No: DIA-194.
Native Penicillium sp. α-Rhamnosidase
A thermostable Alpha-L-Rhamnosidase (Naringinase, RhamA) that catalyzes the cleavage of the bond between terminal L (+)-rhamnose and the aglycone of rhamnose-containing glycosides. The enzyme is very active on naringin but has also substantial activity with hesperidin as substrate. Group: Enzymes. Synonyms: glycosidehydrolase; RhamA; naringinase; hesperidinase; α-L-rhamnosidase A; α-L-rhamnosidase N; α-L-rhamnoside rhamnohydrolase; EC 3.2.1.40. Enzyme Commission Number: EC 3.2.1.40. CAS No. 37288-35-0. RhamA. Activity: >0.2 u/mg. Appearance: Tan Powder. Storage: 4°C. Source: Penicillium sp. glycosidehydrolase; RhamA; naringinase; hesperidinase; α-L-rhamnosidase A; α-L-rhamnosidase N; α-L-rhamnoside rhamnohydrolase; EC 3.2.1.40. Cat No: NATE-1164.
Native Porcine Trehalase
Trehalase is a glycosidehydrolase enzyme located in on the brush border of the small intestine that catalyzes the conversion of trehalose to glucose. It is found in most animals. The non-reducing disaccharide trehalose (α-D-glucopyranosyl-1,1-α-D-glucopyranoside) is one of the most important storage carbohydRates, which is present in almost all forms of life except mammals. The disaccharide is hydrolyzed into two molecules of glucose by the enzyme trehalase. There are two types of trehalases found in Saccharomyces cerevisiae, viz. neutral trehalase (NT) and acid trehalase (AT) classified according to their pH optima. NT has an optimum pH of 7.0, while that of AT is 4...mopara viticola-infected grapevine leaves. trehalase has also been used in a study to investigate growth arrest by trehalose-6-phosphate. Group: Enzymes. Synonyms: α,α-Trehalose glucohydrolase; Trehalase; EC 3.2.1.28; 9025-52-9; α,α-trehalase. Enzyme Commission Number: EC 3.2.1.28. CAS No. 9025-52-9. Trehalase. Activity: > 1.0 units/mg protein. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 1% Triton(TM) X-100 and 25 mM potassium phosphate, pH 6.5. Source: Porcine kidney. Species: Porcine. α,α-Trehalose glucohydrolase; Trehalase; EC 3.2.1.28; 9025-52-9; α,α-trehalase. Cat No: NATE-0717.
Neuraminidase enzymes are glycosidehydrolase 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.
Would you like to list your products on USA Chemical Suppliers?
Our database is helping our users find suppliers everyday.