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Beijing Shengxia Protein O-Glycoproteinase

NegotiableUpdate on 05/06
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Overview

Beijing Shengxia protein O-glycoprotein has broad specificity and is an O-glycoprotein cloned from Pseudomonas aeruginosa. This enzyme can recognize mucin type O-glycans (including branching and sialylation structures) in glycoproteins or glycopeptide chains, and cleave peptide bonds into glycosylated serine or threonine residues (cleavage at the N-terminus).

Product Details

Common types of O-glycoproteases

(1) O-Glycosidase

  • source: Usually comes fromEnterococcus faecalisorStreptococcus pneumoniae.

  • specificity

    • cuttingCore 1(Gal β 1-3GalNAc) andCore 3(GlcNAc β 1-3GalNAc) O-sugar chain, but cannot cleave sialylated O-sugar chain (sialic acid needs to be removed first).

    • Not applicable to other core structures (such as core 2/4).

  • applicationSimplified O-chain analysis, commonly used for mass spectrometry or HPLC pretreatment.

(2) Non-specific O-chain releasing enzyme

  • chemical method

    • β - elimination reaction (alkaline conditions)If treated with NaOH/NaBH ₄, the O-sugar chain is released and its end is reduced, but it will damage the peptide chain.

  • Enzymatic combination

    • Sialidase+O-glucosidaseThe sialic acid residues need to be removed first, and then the core structure needs to be enzymatically cleaved.

Our company independently develops-Beijing Shengxia Protein O-Glycoproteinase(IMPa), Also known as immunomodulatory protease (IMPa), it is a type of enzyme derived from Pseudomonas aeruginosa(Pseudomonas aeruginosa), O-glycosidase with broad-spectrum specificity. It recognizes mucin type O-linked sugar chains in glycoproteins or glycopeptides, including sugar chains with branched and sialylated structures, and cleaves the N-terminal peptide bond adjacent to glycosylated serine or threonine residues. It can be used in the experimental process of glycoproteomics to determine the O-glycosylation site map and perform structural analysis on the O-sugar chains present at each glycosylation site. O-glycoprotein contains 6 × His tags, which can be easily removed from the reaction system using nickel affinity resin.

Product Features

Used for O-glycosylation site determination and O-sugar structure determination

Effectively cleaves glycoproteins (regardless of sialylation) without the need for neuraminidase treatment

For recombinant enzymes, without contamination from other proteases

Can be used under both denaturing and non denaturing conditions

Free of glycerol, easy to achieve excellent results in HPLC and MS analysis

Provided in solution form; Excellent activity and stability for up to 24 months

Beijing Shengxia Protein O-GlycoproteinaseContaining 6 × His tags, it can be easily removed from the reaction system using nickel affinity resin