2. Enzyme
  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 (278):

Cat. No. Product Name CAS No.  
  • HY-107910
    Hyaluronidase, Bovine testes 37326-33-3  
    Hyaluronidase, Bovine testes (Hyaluronate 4-glycanohydrolase; Hyaluronoglucosaminidase) is an endoglycosidase that depolymerizes Hyaluronic acid (HA) (HY-B0633A) by cleavage of glycosidic bonds. Hyaluronidase degrades HA and activates membrane receptors that trigger pathways converging in NF-κB activation. Hyaluronidase is employed in the research of granulomatous foreign body reactions, soft-tissue necrosis caused by vascular compromise and uncomplicated nodules, overcorrection, inflamed nodules or tissue ischemia associated with HA filler injection.
  • 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-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-P3208
    Endoproteinase Lys-C 72561-05-8  
    Endoproteinase Lys-C is a protease that cleaves proteins on the C-terminal side of lysine residues and is commonly used for protein sequencing.
  • HY-B2220
    Cellulase 9012-54-8  
    Cellulase is an enzyme catalyzing the hydrolysis of certain linkages in cellulose and other carbohydrates.
  • HY-P3187
    exo-β-1,4-Xylosidase, Cellulosimicrobium cellulans sp. 21 9025-53-0  
    Exo-1,4-β-xylosidase is an exonuclease that specifically acts on the β-1,4 glycosidic bonds at the non-reducing ends of xylan and xylooligosaccharides. Exo-1,4-β-xylosidase is Ca2+-dependent and reversibly binds to metal ions to catalyze the hydrolysis of β-1,4 glycosidic bonds, thereby degrading xylan to produce xylose. Exo-1,4-β-xylosidase can be used in research fields such as lignocellulose bioconversion, bioethanol production, and optimization of xylan saccharification processes.
  • HY-E70565
    O-Glycoprotease  
    O-Glycoprotease is an O-glycoprotein-specific endoprotease that catalyzes the hydrolysis of peptide bonds directly adjacent to the O-polymer in native mucin-type O-glycosylated proteins. O-Glycoprotease sequence is from Akkermansia muciniphila, recombinantly expressed in E.coli, with a 6×His tag at the C-terminus.
    The enzyme maintains high activity between pH 5.5-7.5 and is resistant to 1M NaCl, but is highly sensitive to EDTA (0.5 mM EDTA) and can be inhibited by Zn2+.
  • HY-E70573
    Endo SH  
    Endo SH is a fusion protein of Endo S (from Streptococcus pyogenes) and Endo H (from Streptomyces plicatus), expressed in Escherichia coli. Endo SH can cleave the chitobiose core structure of high mannose, complex and some hybrid oligosaccharides in N-glycoproteins, remove N-linked high mannose in glycoproteins, and can completely replace Endo S and Endo H.
  • 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-126386
    Pectinase, aspergillus niger 9032-75-1  
    Pectinase (EC 3.2.1.15) is a mixed enzymes that hydrolyze pectic substances, it mostly presents in microorganisms and higher plants. Pectinase is involved in the metabolism of the cell wall as well as in the growth of the cell, senescence, ripening of fruits, pathogenesis and abscission process.
  • 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-E70306
    Zymolyase, Arthrobacter luteus  
    Zymolyase, Arthrobacter luteus, is a zymolyase mainly found in Arthrobacter luteus. Enzyme, an enzyme with beta-1,3 glucanase activity, removes the electron-dense outer layer of the Plasmodium karinii cell wall, exposing an electron-lucent layer.
  • 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-B2193
    α-Amylase 9000-90-2  
    α-Amylase is a hydrolase enzyme that catalyses the hydrolysis of internal α-1, 4-glycosidic linkages in starch to yield products like glucose and maltose.
  • 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-E70097
    Sialidase (α2-3-6-8-9)  
    Sialidase (α2-3-6-8-9) is a broadly specific sialidase that cuts linear and branched non-reducing terminal sialic acid residues from glycoproteins, glycopeptides, and oligosaccharides. Sialidase (α2-3-6-8-9) can be used for in vitro and in vivo polysaccharide analysis and characterization as well as complete glycoprotein remodeling.
  • HY-108903A
    Hyaluronidase, Ovine testes 37326-33-3  
    Hyaluronidase, Ovine testes is an endoglycosidase. Hyaluronidase, Ovine testes specifically degrades Hyaluronic acid (HY-B0633A) and Chondroitin sulfate (HY-B2162) by hydrolyzing β-glycosidic bonds in acidic mucopolysaccharides. Hyaluronidase, Ovine testes disperses follicular cells during fertilization by breaking down the hyaluronic acid-rich cumulus. Hyaluronidase, Ovine testes can be used in the study of fertility-related diseases.
  • 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-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-P2857
    Amyloglucosidase, Aspergillus niger 9032-08-0  
    Amyloglucosidase, Aspergillus niger is an enzyme derived from many sources including plants, animals and microorganisms, can be use for industrial production. Amyloglucosidase can be widely used for starch saccharification, brewing and distilling industry.