2. 酵素
  3. Glycobiology Enzymes

Glycobiology Enzymes

Glycobiology is a science that studies the structure, function, and biological properties of sugars. It can combine enzymology and analytical technology to explore the structure-activity relationship of sugars. Categories include common Endo S, LgtB etc.

Glycobiology enzymes are mainly used for:

• Sugar chain synthesis

• Glycose chain structure research

• Glycoconjugate research

• Cell surface glycosylation modification

• Disease diagnosis

Glycobiology Enzymes (518):

製品番号 製品名 CAS 番号  
  • HY-E70289
    Bovin beta-1,4-galactosyltransferase 1 (Y289L)  
    Bovin beta-1,4-galactosyltransferase 1 (Y289L) (Bovin B4GALT1 (Y289L)) is a mutated form of bovine-derived galactosyltransferase with a mutation at the Y289L genetic site. Bovin beta-1,4-galactosyltransferase 1 can label O-GlcNAcylated proteins with an N-azidoacetylgalactosamine (GalNAz) group. This labeling method allows for the specific, unbiased, and global labeling of O-GlcNAcylated proteins. After labeling, the appended azide group can react with a wide variety of alkyne-modified chemical probes, facilitating multiple downstream analyses.
  • HY-P2902
    Glucose oxidase 9001-37-0  
    Glucose oxidase is used in the food and beverage industry as a preservative and stabilizer and is commonly derived from the fungus Aspergillus niger. Glucose oxidase can react with intracellular glucose and oxygen (O2) to produce hydrogen peroxide (H2O2) and gluconic acid, which can cut off the nutrition source of cancer cells and consequently inhibit their proliferation.
  • HY-P2929
    PNGase F 83534-39-8  
    PNGase F, a glycosidase, catalyzes the cleavage of an internal glycoside bond in an oligosaccharide. PNGase F removes nearly all N-linked oligosaccharides from glycoproteins. PNGase F can release N-glycans from glycoproteins in glycoanalytical workflows.
  • HY-P2802
    α-Glucosidase, Yeast 9001-42-7  
    α-Glucosidase, Yeast (α-D-Glucosidase, Yeast), a carbohydrate hydrolyzing enzyme, catalyzes the liberation of α-glucose from the non-reducing end of the substrate. α-Glucosidase can facilitate the absorption of glucose by the small intestine. Inhibition of α-Glucosidase is an effective management of non-insulin-dependent diabetes mellitus (NIDDM).
  • HY-E70131
    Endo H, Streptomyces picatus 37278-88-9  
    Endo H, Streptomyces picatus (Endo-β-N-acetylglucosaminidase H), isolated from Streptomyces plicatus, hydrolyzes the central glycosidic bond of the β1, 4-di-N-acetylchitobiose core in asparagine-linked oligosaccharides.
  • HY-P2802H
    α-Glucosidase, Saccharomyces cerevisiae  
    α-Glucosidase, Saccharomyces cerevisiae (EC 3.2.1.20), is a glucosidase located at the brush border of the small intestine, acting on 1,4-α-glycosidic bonds. α-Glucosidase breaks down starch and disaccharides into glucose.
  • HY-E71360
    O-GlcNAcase, Clostridium perfringens  
    O-GlcNAcase, Clostridium perfringens is a glycosidase derived from Clostridium perfringens, which functions in bacterial nutrient metabolism, host interaction and virulence regulation. O-GlcNAcase is a core enzyme in the cellular signal regulatory network and serves as a key target for various major and chronic diseases. O-GlcNAcase, Clostridium perfringens can be used for basic research and drug development of O-GlcNAcase due to its high conservation in catalytic mechanism and structure with human-derived enzymes.
  • HY-E70069
    Endo S2, Streptococcus pyogenes 37278-88-9  
    Endo-β-N-acetylglucosaminidase (Endo S2) is a key enzyme involved in the processing of free oligosaccharides in the cytosol. Endo-β-N-acetylglucosaminidase catalyzes hydrolysis of N-linked oligosaccharides.
  • HY-P2767
    Urease, Jack bean 9002-13-5  
    Urease, Jack bean is derived from jack bean and Catalyzes hydrolysis of urea to carbon dioxide and ammonia. Urease, Jack bean is useful in the determination of urea in body fluids.
  • HY-P3004
    Endo-1,3-β-glucanase 9025-37-0  
    Endo-1,3-β-glucanase (Lyticase) is an endoenzyme that can specifically cleave β-1,3-glycosidic bonds. Endo-1,3-β-glucanase recognizes and binds to β-1,3-glucan chains, catalyzing the cleavage of glycosidic bonds and hydrolyzing polysaccharides into oligosaccharides. Endo-1,3-β-glucanase eliminates vaginal Candida. Endo-1,3-β-glucanase can be used in the study of recurrent Candida vaginitis.
  • HY-E70013
    Lichenase, Microorganism 37288-51-0  
    Lichenase, Microorganism (endo-1,3:1,4-β-D-Glucanase) is a specific, endo-(1-3),(1-4)-β-D-glucan 4-glucanohydrolase. Lichenase, Microorganism solubilizes β-glucans from cereal grains and gives gluco-oligosaccharides (GOS). Lichenase, Microorganism can be used in the degradation of polysaccharides in the cell walls.
  • HY-P2988
    Neuraminidase, Microorganism 9001-67-6  
    Neuraminidase, Microorganism (Exo-α-sialidase) is an exosialidase, is often used in biochemical studies. Neuraminidase cleaves α-ketosidic linkage between the sialic (N-acetylneuraminic) acid and an adjacent sugar residue. Neuraminidase, derived from mucosal pathogens, is a virulence factor that modifies the host's response to infection.
  • HY-P2979
    Invertase, baker's yeast (S. cerevisiae) 9001-57-4  
    Invertase, baker's yeast (S. cerevisiae) is a major enzyme present in plants and microorganisms, is often used in biochemical studies. Invertase catalyzes the hydrolysis of the disaccharide sucrose into glucose and fructose.
  • HY-E70285
    beta-1,4-Galactosyltransferase 1 (Y285L)  
    beta-1,4-Galactosyltransferase 1 (Y285L) can enzymatic synthesis of the LacdiNAc motif. beta-1,4-Galactosyltransferase 1 (Y285L) can transfer of GalNAc from UDP-GalNAc.
  • HY-E70110
    Endo-1,4-β-mannanase 37288-54-3  
    Endo-1,4-β-mannanase is an important catalytic agent that randomly cleave the β-1,4-linkage in the mannan backbone and release short β-1,4-mannooligosaccharides and mannose.
  • HY-P2869
    β-Galactosidase, E. coli 9031-11-2  
    β-Galactosidase, E. coli (EC 3.2.1.23; GAL) is a glycoside hydrolase that hydrolyzes the β-glycosidic bonds formed between galactose and its organic moieties. β-Galactosidase, E. coli 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.
  • HY-P2857
    Glucoamylase, Aspergillus niger 9032-08-0  
    Amyloglucosidase, Aspergillus niger (Amyloglucosidase, Aspergillus niger) is a starch-hydrolyzing enzyme with high catalytic efficiency towards soluble starch and raw starch. Amyloglucosidase, Aspergillus niger hydrolyzes α-1,4 and α-1,6 glycosidic linkages in starch and similar substrates, and primarily releases β-glucose molecules from the non-reducing ends. Amyloglucosidase, Aspergillus niger participates in glycogen metabolism and is associated with type II glycogen storage disease. Amyloglucosidase, Aspergillus niger converts starch into glucose, and is applicable to the industrial production of high-fructose syrup, ethanol and other fermented products.
  • HY-E70024
    CMP-sialic acid synthetase (NmCSS) 9067-82-7  
    CMP-sialic acid synthetase (NmCSS) is an essential enzyme involved in the biosynthesis of carbohydrates and glycoconjugates containing sialic acids. CMP-sialic acid synthetase (NmCSS) activates free Sia, converting it to CMP-Sia, which is the only donor substrate for all sialyltransferases.
  • HY-P2929A
    PNGase F-Fast 83534-39-8  
    PNGase F-Fast is a glycosidase that catalyzes the cleavage of internal glycosidic bonds in oligosaccharides. PNGase F-Fast removes almost all N-linked oligosaccharides from glycoproteins. PNGase F-Fast can release N-glycans from glycoproteins in the sugar analysis workflow. The cleavage site is: the glycosidic bond between the innermost N-acetylglucosamine and asparagine. PNGase F-Fast is an improved reagent that allows for rapid deglycosylation of antibodies and antibody fusions within minutes.
  • HY-P2775
    β-Glucosidase, almond 9001-22-3  
    β-Glucosidase, almond is the rate-limiting enzyme in cellulose degradation. β-Glucosidase is a major group among glycoside hydrolases. β-Glucosidase is involved in the degradation of cellulose in soils and has potential for monitoring soil quality.