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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

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0.2 UNIT
€475.00

€475.00

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0.2 UNIT
€475.00

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

€475.00

Please contact Customer Service for Availability

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

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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

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Certificates of Analysis (COA)

Lot/Batch Number
0000395651
0000349231
0000343916
0000340033
0000327213

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

Sigma-Aldrich

P7367

PNGase F from Elizabethkingia meningoseptica

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.
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
John E Schiel et al.
Journal of mass spectrometry : JMS, 46(7), 649-657 (2011-06-28)
The current project describes the chemoenzymatic modification of bovine ribonuclease B (RNase B) to contain a single glycosylation site with a known glycan. A reactive disaccharide oxazoline derivative was synthesized and stereospecifically added to deglycosylated RNase B through endo-β-N-acetylglucosaminidase M
Wei Zhang et al.
Talanta, 85(1), 499-505 (2011-06-08)
Endoglycosidase is a class of glycosidases that specifically cleaves the glycosidic bond between two proximal residues of GlcNAc in the pentasaccharide core of N-glycan, leaving the innermost GlcNAc still attached to its parent protein, which provides a different diagnostic maker
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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Strategies for Deglycosylating N-Linked Glycans

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

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