Skip to Content
Merck
All Photos(1)

Documents

E0639

Sigma-Aldrich

Endoglycosidase F2 from Elizabethkingia miricola

recombinant, expressed in E. coli, 20 U/mg

Synonym(s):

Elizabethkingia miricola, Endo-β-N-acetylglucosaminidase F2, Endo F2, Endoglycosidase F2 from Chryseobacterium meningosepticum, Endoglycosidase F2 from Elizabethkingia meningoseptica, Endoglycosidase F2 from Flavobacterium meningosepticum

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

CAS Number:
37278-88-9
Enzyme Commission number:
3.2.1.96 (BRENDA, IUBMB)
MDL number:
MFCD00151069
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

200

conjugate

(N-linked)

form

solution

specific activity

20 U/mg

mol wt

32 kDa

shipped in

wet ice

storage temp.

2-8°C

Looking for similar products? Visit Product Comparison Guide

Related Categories

Packaging

Supplied with 5× Reaction Buffer, 250 mM sodium acetate, pH 4.5

Unit Definition

One unit will release N-linked oligosaccharides from 1 μmole of denatured porcine fibrinogen in 1 minute at 37 °C, pH 4.5.

Physical form

Aseptically filled solution in 10 mM sodium acetate, 25 mM sodium chloride, pH 4.5

Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Customers Also Viewed

Slide 1 of 1

1 of 1

PNGase F from Elizabethkingia meningoseptica BioReagent, ≥95% (SDS-PAGE), for proteomics

Sigma-Aldrich

P7367

PNGase F from Elizabethkingia meningoseptica

D Wade Abbott et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 67(Pt 4), 429-433 (2011-04-21)
EndoD is an architecturally complex endo-β-1,4-N-acetylglucosamidase from Streptococcus pneumoniae that cleaves the chitobiose core of N-linked glycans and contributes to pneumococcal virulence. Although the glycoside hydrolase family 85 catalytic module has been structurally and functionally characterized, nothing is known about
Midori Umekawa et al.
Biochimica et biophysica acta, 1800(11), 1203-1209 (2010-07-22)
An efficient method for synthesizing homogenous glycoproteins is essential for elucidating the structural and functional roles of glycans of glycoproteins. We have focused on the transglycosylation activity of endo-ß-N-acetylglucosaminidase from Mucor hiemalis (Endo-M) as a tool for glycoconjugate syntheses, since
Eric M Rubenstein et al.
The Journal of cell biology, 197(6), 761-773 (2012-06-13)
Little is known about quality control of proteins that aberrantly or persistently engage the endoplasmic reticulum (ER)-localized translocon en route to membrane localization or the secretory pathway. Hrd1 and Doa10, the primary ubiquitin ligases that function in ER-associated degradation (ERAD)
Roger S Zou et al.
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
Yusuke Tomabechi et al.
Carbohydrate research, 345(17), 2458-2463 (2010-10-12)
To determine the structural specificity of the glycosyl acceptor of the transglycosylation reaction using endo-β-N-acetylglucosaminidase (ENGase) (EC 3.2.1.96) from Mucor hiemalis (Endo-M), several acceptor derivatives were designed and synthesized. The narrow regions of the 1,3-diol structure from the 4- to
View All Related Papers

Articles

Strategies for Deglycosylating N-Linked Glycans

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service