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E0639

Endoglycosidase F2 from Elizabethkingia miricola

Name: Endoglycosidase F2 from <I>Elizabethkingia miricola</I>
Brand: SIGMA

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

Synonyme(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

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A propos de cet article

Numéro CAS:

37278-88-9

UNSPSC Code:

12352204

NACRES:

NA.32

Numéro CE :

3.2.1.96 (BRENDA, IUBMB)

MDL number:

MFCD00151069

Specific activity:

20 U/mg

Recombinant:

expressed in E. coli

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Propriétés

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

Description

Packaging

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

Physical form

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

Other Notes

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

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Cet article	E2264	E9762	324726
Sigma-Aldrich E0639 Endoglycosidase F2 from Elizabethkingia miricola	Sigma-Aldrich E2264 Endoglycosidase F3 from Elizabethkingia miricola	Sigma-Aldrich E9762 Endoglycosidase F1 from Elizabethkingia miricola	Sigma-Aldrich 324726 Endoglycosidase F2, Elizabethkingia meningosepticum, Recombinant, E. coli
specific activity 20 U/mg	specific activity 30 U/mg	specific activity ≥16 U/mg	specific activity ≥20 units/mg protein, ≥5 units/mL
form solution	form solution	form buffered aqueous solution	form liquid
recombinant expressed in E. coli	recombinant expressed in E. coli	recombinant expressed in E. coli	recombinant expressed in E. coli
storage temp. 2-8°C	storage temp. 2-8°C	storage temp. 2-8°C	storage temp. 2-8°C
shipped in wet ice	shipped in wet ice	shipped in wet ice	shipped in wet ice
mol wt 32 kDa	mol wt 32 kDa	mol wt 32 kDa	mol wt -

Classe de stockage

10 - Combustible liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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Certificats d'analyse (COA)

Lot/Batch Number

0000545872

0000490687

0000446699

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Contenu apparenté

Product Information Sheet - E0639

Instructions

An endo-β-N-acetylglucosaminidase from Enterococcus faecalis V583 responsible for the hydrolysis of high-mannose and hybrid-type N-linked glycans.

Liv Anette Bøhle et al.

FEMS microbiology letters, 325(2), 123-129 (2011-11-19)

It has been demonstrated previously that Enterococcus faecalis produces secreted endoglycosidases that enable the bacteria to remove N-linked glycans from glycoproteins. One enzyme potentially responsible for this activity is EF0114, comprising a typical GH18 endoglycosidase domain and a GH20 domain.

Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase.

Helena Ryšlavá et al.

The FEBS journal, 278(14), 2469-2484 (2011-05-14)

Fungal β-N-acetylhexosaminidases are inducible extracellular enzymes with many biotechnological applications. The enzyme from Penicillium oxalicum has unique enzymatic properties despite its close evolutionary relationship with other fungal hexosaminidases. It has high GalNAcase activity, tolerates substrates with the modified N-acyl group

Remarkable transglycosylation activity of glycosynthase mutants of endo-D, an endo-β-N-acetylglucosaminidase from Streptococcus pneumoniae.

Shu-Quan Fan et al.

The Journal of biological chemistry, 287(14), 11272-11281 (2012-02-10)

Endo-β-N-acetylglucosaminidase from Streptococcus pneumoniae (Endo-D) is an endoglycosidase capable of hydrolyzing the Fc N-glycan of intact IgG antibodies after sequential removal of the sialic acid, galactose, and internal GlcNAc residues in the N-glycan. Endo-D also possesses transglycosylation activity with sugar

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Numéro d'article de commerce international

Référence	GTIN
E0639-.2UN	04061833601198

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