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E0639

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

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0.2 UNIT

RM 3,056.00

RM 3,056.00


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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

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recombinant

expressed in E. coli

Quality Level

conjugate

(N-linked)

form

solution

specific activity

20 U/mg

mol wt

32 kDa

shipped in

wet ice

storage temp.

2-8°C

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1 of 4

This Item
E2264E9762P9120
specific activity

20 U/mg

specific activity

30 U/mg

specific activity

≥16 U/mg

specific activity

≥10 units/mg protein

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

form

solution

form

solution

form

buffered aqueous solution

form

-

mol wt

32 kDa

mol wt

32 kDa

mol wt

32 kDa

mol wt

36 kDa

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

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.

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

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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
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.
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
Wen-Yi Lo et al.
The Journal of biological chemistry, 285(41), 31348-31361 (2010-07-20)
γ-aminobutyric acid type A (GABA(A)) receptors are heteropentameric glycoproteins. Based on consensus sequences, the GABA(A) receptor β2 subunit contains three potential N-linked glycosylation sites, Asn-32, Asn-104, and Asn-173. Homology modeling indicates that Asn-32 and Asn-104 are located before the α1
Francesco Renzi et al.
PLoS pathogens, 7(6), e1002118-e1002118 (2011-07-09)
C. canimorsus 5 has the capacity to grow at the expenses of glycan moieties from host cells N-glycoproteins. Here, we show that C. canimorsus 5 also has the capacity to deglycosylate human IgG and we analyze the deglycosylation mechanism. We

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

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