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Results for "

n-glycosylation site

" in MedChemExpress (MCE) Product Catalog:

4

Inhibitors & Agonists

2

Peptides

Targets Recommended:
Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-E70568
    Protease (O-glycan Cleaving)

    		Ser/Thr Protease Others
    Protease (O-glycan Cleaving) is recombinantly expressed from E.coli and contains a His tag. Protease (O-glycan Cleaving) is an O-glycan-dependent protease that digests proteins carrying mucin-type O-glycans, including sialylated substrates, glycosylated Ser and Thr residues at the N terminus. Protease (O-glycan Cleaving) digests a variety of O-glycan structures, including sialylated glycosylated core 1 and core 2 structures and Tn antigen. Protease (O-glycan Cleaving) does not digest terminally modified serine or threonine residues, nor does it digest N-glycosylation sites on glycoproteins.
    Protease (O-glycan Cleaving)
  • HY-P4027A
    HCV-1 e2 Protein (554-569) (TFA)

    		HCV Infection
    HCV-1 e2 Protein (554-569) TFA is one of the main antigenic regions of HCV envelope 2 (e2) protein. The HCV-1 e2 Protein (554-569) TFA contains a putative N-glycosylation site, which was previously thought to influence the immune recognition of e2 .
    HCV-1 e2 Protein (554-569) (TFA)
  • HY-176559
    LacNAc-VC-PAB-MMAE

    		Antibody-Drug Conjugates (ADCs) Cancer
    LacNAc-VC-PAB-MMAE is a component of an Antibody-Drug Conjugate (ADC). LacNAc-VC-PAB-MMAE is assembled onto the N-glycosylation site of Trastuzumab (HY-P9907) by WT Endo-S2 .
    LacNAc-VC-PAB-MMAE
  • HY-P4027
    HCV-1 e2 Protein (554-569)

    		HCV Infection
    HCV-1 e2 Protein (554-569) is one of the main antigenic regions of HCV envelope 2 (e2) protein. The HCV-1 e2 Protein (554-569) contains a putative n-glycosylation site, which was previously thought to influence the immune recognition of e2 .
    HCV-1 e2 Protein (554-569)

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