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Endoglycosidases

" in MedChemExpress (MCE) Product Catalog:
Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-107910
    Hyaluronidase, Bovine testes
    Maximum Cited Publications
    16 Publications Verification

    Hyaluronate 4-glycanohydrolase, Bovine testes; Hyaluronoglucosaminidase, Bovine testes

    NF-κB Inflammation/Immunology Cancer
    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 .
    Hyaluronidase, Bovine testes
  • HY-E70135

    Endo F1

    Endogenous Metabolite Metabolic Disease
    Endo-β-N-acetylglucosaminidase F1 (Endo F1) cleaves Asparagine-linked high mannose and some hybrid oligosaccharides .
    Endo-β-N-acetylglucosaminidase F1
  • HY-108903A
    Hyaluronidase, Ovine testes
    10+ Cited Publications

    Glycosidase Biochemical Assay Reagents Endocrinology
    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 .
    Hyaluronidase, Ovine testes
  • HY-E70133

    Endo F2

    Others Metabolic Disease
    Endo-β-N-acetylglucosaminidase F2 (Endo F2), a highly specific endoglycosidase, cleaves within the chitobiose core of asparagine-linked complex biantennary and high mannose oligosaccharides from glycoproteins and glycopeptides. Endo F2 cleaves biantennary glycans at a rate approximately 20 times greater than high mannose glycans. The activity of Endo F2 is identical on biantennary structures with and without core fucosylation. Endo F2 is not active on hybrid or tri- and tetra-antennary oligosaccharides .
    Endo-β-N-acetylglucosaminidase F2
  • HY-E70131
    Endo H, Streptomyces picatus
    1 Publications Verification

    Endo-β-N-acetylglucosaminidase H

    Others Metabolic Disease
    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 .
    Endo H, Streptomyces picatus
  • HY-E70134

    Endo F3

    Others Metabolic Disease
    Endo-β-N-acetylglucosaminidase D (Endo F3) cleaves free or Asparagine-linked triantennary oligosaccharides or α1-6 fucosylated biantennary oligosaccharides, as well as triamnnosyl chitobiose core structures .
    Endo-β-N-acetylglucosaminidase F3
  • HY-E70884

    EndoS2 D184M

    Glycosidase Others
    Endoglycosidase S2 (D184M mutant) (EndoS2 D184M) is a mutant endoglycosidase. Endoglycosidase S2 (D184M mutant) promotes the transfer of glyco-oxazoline donors with defined glycoforms to the Fc region of IgG antibodies .
    Endoglycosidase S2 (D184M mutant)
  • HY-E70132

    Endo D

    Glycosidase Metabolic Disease
    Endo-β-N-acetylglucosaminidase D (Endo D), isolated from Streptococcus pneumoniae. Endo-β-N-acetylglucosaminidase D hydrolyzes Fc N-glycan of intact IgG antibodies after sequential removal of the sialic acid, galactose, and internal GlcNAc residues in the N-glycan. Endo-β-N-acetylglucosaminidase D possesses transglycosylation activity with sugar oxazoline as the donor substrate .
    Endo-β-N-acetylglucosaminidase D
  • HY-E70883

    EndoS D233Q

    Glycosidase Others
    Endoglycosidase S (D233Q mutant) (EndoS D233Q) is a mutant endoglycosidase, which catalyzes the glycosylation of Trastuzumab (HY-P9907)-GlcNAc with the functionalized, non-natural glycans to give glycosylated monoclonal Abs (mAbs) carrying two glycans each functionalized with two reaction handles .
    Endoglycosidase S (D233Q mutant)
  • HY-E70879

    EndoM N175Q

    Glycosidase Others
    Endoglycosidase M (N175Q mutant) (EndoM N175Q) can transfer natural N-glycans or oxazoline N-glycans to any peptide or protein with a GlcNAc residue to form a β1-4-glycosidic linkage. Endoglycosidase M (N175Q mutant) is a useful tool in the synthesis of homogeneous glycopeptides and glycoproteins .
    Endoglycosidase M (N175Q mutant)
  • HY-E70136

    Keratan-sulfate endo-1,4-beta-galactosidase; Keratanase

    Others Metabolic Disease
    Endo-β-Galactosidase catalyzes the hydrolysis of internal β1-4 galactose linkages in unbranched, repeating poly-N-acetyllactosamine ([GlcNAc- (1-3)Gal- (1-4)]n) structures .
    Endo-β-Galactosidase
  • HY-E70880

    EndoCC N180H

    Glycosidase Others
    Endoglycosidase CC (N180H mutant) (EndoCC N180H) is a mutant endoglycosidase, which efficiently and specifically recognizes core fucose and O-GlcNAc .
    Endoglycosidase CC (N180H mutant)
  • HY-E70881

    EndoF3 D165A

    Glycosidase Others
    Endoglycosidase F3 (D165A mutant) (EndoF3 D165A) is a mutant endoglycosidase, which efficiently and specifically recognizes core fucose and O-GlcNAc .
    Endoglycosidase F3 (D165A mutant)
  • HY-E70882

    EndoD N322Q

    Glycosidase Others
    Endoglycosidase D (N322Q mutant) (EndoD N322Q) is a mutant endoglycosidase, which can be highly efficient to transfer Man5GlcNAc oxazoline to a similar cyclic glycopeptide carrying two free GlcNAc moieties to give a doubly glycosylated peptide .
    Endoglycosidase D (N322Q mutant)
  • HY-E70880A

    EndoCC

    Glycosidase Others
    Endoglycosidase CC (EndoCC), an endoglycosidase, is a substrate of glycopeptide .
    Endoglycosidase CC
  • HY-180467

    ADC Linker Cancer
    Neu5Ac-2Galβ1-3Glc-oxazoline-(2)Me (Compound G12) is a disaccharide linker. Neu5Ac-2Galβ1-3Glc-oxazoline-(2)Me can be efficiently recognized by the endo-glycosidase Endo-S2 and can be directedly transferred to the conserved N-glycosylation site (Asn297 position) of the antibody's Fc domain through enzymatic catalytic reactions, thereby achieving site-specific modification of the antibody. Neu5Ac-2Galβ1-3Glc-oxazoline-(2)Me can be used for for the synthesis of antibody-conjugated drugs (ADCs) .
    Neu5Ac-2Galβ1-3Glc-oxazoline-(2)Me

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