E9762
Endoglycosidase F1 from Elizabethkingia miricola
recombinant, expressed in E. coli, ≥16 U/mg, buffered aqueous solution
동의어(들):
Endo F1, Endo-β-N-acetylglucosaminidase F1, Endoglycosidase F1 from Chryseobacterium meningosepticum, Endoglycosidase F1 from Elizabethkingia meningoseptica, Endoglycosidase F1 from Flavobacterium meningosepticum
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모든 사진(1)
About This Item
추천 제품
일반 설명
Endoglycosidase F1 from Elizabethkingia miricola is a glycan specific enzyme.
애플리케이션
Endoglycosidase F1 from Elizabethkingia miricola has been used to remove binding of human hemochromatosis protein (HFE) to cation independent mannose-6-phosphate receptor (CI-MPR) and to glycosylate fucosylated N-glycopeptides.
Cleaves asparagine-linked or free oligomannose and hybrid, but not complex, oligosaccharides.
생화학적/생리학적 작용
Endoglycosidase F1 from Elizabethkingia miricola plays an important role in cleavage of glycan structures from the protein by cleaving between the two N-acetylglucosamine residues of the chitobiose core. It mediates high mannose and hybrid oligosaccharides cleavage.
포장
Supplied with 5× Reaction Buffer, 250 mM NaH2PO4, pH 5.5.
단위 정의
One unit will release N-linked oligosaccharides from 1 μmole of denatured Ribonuclease B in 1 minute at 37 °C, pH 5.5.
물리적 형태
Aseptically filled solution in 20 mM Tris-HCl pH 7.5
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
Receptor activity-modifying protein 1 determines the species selectivity of non-peptide CGRP receptor antagonists
The Journal of Biological Chemistry, 277, 14294-14298 (2002)
EndoS2 is a unique and conserved enzyme of serotype M49 group A Streptococcus that hydrolyses N-linked glycans on IgG and alpha-acid glycoprotein
BioChemistry: An Indian Journal, 455, 107-118 (2013)
Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM
Journal of proteomics, 189, 67-74 (2018)
In vitro binding of HFE to the cation-independent mannose-6 phosphate receptor
Blood Cells, Molecules and Diseases, 43(2), 180-193 (2009)
Aging, 3(10), 968-984 (2011-10-13)
A distinct conformational transition from the α-helix-rich cellular prion protein (PrPC) into its β-sheet-rich pathological isoform (PrPSc) is the hallmark of prion diseases, a group of fatal transmissible encephalopathies that includes spontaneous and acquired forms. Recently, a PrPSc-like intermediate form
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