19 Results for "

Endoglycosidases

" in MedChemExpress (MCE) Product Catalog:
Products (19)

19 Results for "Endoglycosidases" in MCE Product Catalog:

19
19 Publications Verification
Cat. No.: HY-107910
CAS No.: 37326-33-3
Synonyms: Hyaluronate 4-glycanohydrolase, Bovine testes; Hyaluronoglucosaminidase, Bovine testes
Target:  

NF-κB

Research Areas:  

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 .
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19
19 Publications Verification
Cat. No.: HY-108903A
CAS No.: 37326-33-3
Purity:  95.00%
Research Areas:  

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 .
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2
2 Cited Publications
Cat. No.: HY-E70131
CAS No.: 37278-88-9
Synonyms: Endo-β-N-acetylglucosaminidase H
Target:  

Endonuclease

Research Areas:  

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 .
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Cat. No.: HY-E70135
CAS No.: 37278-88-9
Synonyms: Endo F1
Target:  

Endonuclease

Research Areas:  

Metabolic Disease

Endo-β-N-acetylglucosaminidase F1 (Endo F1) cleaves Asparagine-linked high mannose and some hybrid oligosaccharides .
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Cat. No.: HY-E70133
CAS No.: 37278-88-9
Synonyms: Endo F2
Target:  

Endonuclease

Research Areas:  

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 .
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Cat. No.: HY-E70134
CAS No.: 37278-88-9
Synonyms: Endo F3
Target:  

Endonuclease

Research Areas:  

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 .
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Cat. No.: HY-E70884
Synonyms: EndoS2 D184M
Target:  

Glycosidase

Research Areas:  

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 .
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Cat. No.: HY-E70132
CAS No.: 37278-88-9
Synonyms: Endo D
Target:  

Glycosidase

Research Areas:  

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 .
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Cat. No.: HY-E70883
Synonyms: EndoS D233Q
Target:  

Glycosidase

Research Areas:  

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 .
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Cat. No.: HY-E70879
Synonyms: EndoM N175Q
Target:  

Glycosidase

Research Areas:  

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 .
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Cat. No.: HY-E70136
CAS No.: 52720-51-1
Synonyms: Keratan-sulfate endo-1,4-beta-galactosidase; Keratanase
Target:  

Glycosidase

Research Areas:  

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 .
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Cat. No.: HY-E70880
Synonyms: EndoCC N180H
Target:  

Glycosidase

Research Areas:  

Others

Endoglycosidase CC (N180H mutant) (EndoCC N180H) is a mutant endoglycosidase, which efficiently and specifically recognizes core fucose and O-GlcNAc .
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Cat. No.: HY-E70881
Synonyms: EndoF3 D165A
Target:  

Glycosidase

Research Areas:  

Others

Endoglycosidase F3 (D165A mutant) (EndoF3 D165A) is a mutant endoglycosidase, which efficiently and specifically recognizes core fucose and O-GlcNAc .
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Cat. No.: HY-E70882
Synonyms: EndoD N322Q
Target:  

Glycosidase

Research Areas:  

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 .
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Cat. No.: HY-156231
CAS No.: 2855124-81-9
Target:  

Drug Intermediate

Research Areas:  

Others

Glc-GlcNAc-oxazoline is a disaccharide oxazoline that serves as a transglycosylation donor substrate in endoglycosidase-mediated antibody Fc glycan remodeling, and carries a modifiable azido tag. Glc-GlcNAc-oxazoline can be used in studies related to the synthesis of antibody-drug conjugates (ADCs) via click chemistry .
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Cat. No.: HY-E70880A
Synonyms: EndoCC
Target:  

Glycosidase

Research Areas:  

Others

Endoglycosidase CC (EndoCC), an endoglycosidase, is a substrate of glycopeptide .
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Cat. No.: HY-156230
CAS No.: 2855124-74-0
Research Areas:  

Cancer

Man-GIcNAc-oxazoline is a disaccharide oxazoline based on Manβ1,4GlcNAc. Man-GIcNAc-oxazoline serves as a donor substrate for transglycosylation in endoglycosidase-mediated antibody Fc glycan remodeling. Man-GIcNAc-oxazoline can be modified with azides, PEG-linked azides, fluorescent probes, biotin groups, ligands or prodrugs. Man-GIcNAc-oxazoline can be used for the synthesis of antibody-drug conjugates (ADC). Man-GIcNAc-oxazoline is applicable for cancer research .
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Cat. No.: HY-180467A
Target:  

ADC Linkers

Research Areas:  

Cancer

Neu5Ac-2Galβ1-3Glc-oxazoline-(2)Me (Compound G12) sodium is a disaccharide linker. Neu5Ac-2Galβ1-3Glc-oxazoline-(2)Me sodium 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 sodium can be used for for the synthesis of antibody-conjugated drugs (ADCs) .
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Cat. No.: HY-180467
CAS No.: 2823367-76-4
Target:  

ADC Linkers

Research Areas:  

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) .
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