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G1549

Sigma-Aldrich

PNGase F from Elizabethkingia meningoseptica

ready-to-use solution, recombinant, expressed in E. coli

Synonym(s):

PNGase F from Elizabethkingia meningoseptica, N-Glycosidase F, PNGase F from Chryseobacterium meningosepticum, PNGase F from Flavobacterium meningosepticum, Peptide N-glycosidase

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25 G
CA$93.40
500 G
CA$1,630.00

CA$93.40


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25 G
CA$93.40
500 G
CA$1,630.00

About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

CA$93.40


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recombinant

expressed in E. coli

Quality Level

conjugate

(N-linked)

grade

Proteomics Grade

form

ready-to-use solution

specific activity

≥1000 U/mg

shelf life

≥1 yr at -20 °C

mol wt

~36 kDa

shipped in

wet ice

storage temp.

−20°C

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This Item
233279233480219370
form

liquid

form

liquid

form

liquid

form

liquid

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

specific activity

≥85 units/mg protein (clotting assay)

specific activity

≥150 units/mg protein (clotting assay)

specific activity

≥170 units/mg protein (clotting assay)

specific activity

≥25,000 PEU/mg protein (clotting assay)

Quality Level

100

Quality Level

200

Quality Level

100

Quality Level

100

Application

Recombinant PNGase F has been purified by affinity chromatography and dialyzed into a 50% glycerol solution with 10 mM potassium phoosphate pH 7.5 to produce a stable product. The product contains low levels of buffer salts. This highly purified material can be used for preparative deglycosylation or for analytical applications in gel, in solution, or on blot membranes. The enzyme can be removed from preparative operations by utilizing its C-terminal 6x histidine fusion tag. PNGase F from Elizabethkingia meningoseptica has been used in deglycosylation assay in human plasma samples[1] and in deglycosylation of chondroitin sulfate proteoglycan.[2]
Used to deglycosylate protein.

Biochem/physiol Actions

Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.
PNGase F from Elizabethkingia meningoseptica has glycan-binding catalytic domain and a bowl-like domain at the N-terminus. It cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.[3] It is cost-effectively produced on a large scale in prokaryotic hosts and requires divalent zinc ions for its enzymatic activity.[4]

Unit Definition

One unit will catalyze the release of N-linked oligosaccharides from 1 nanomole of denatured ribonuclease B in one minute at 37°C at pH 7.5 monitored by SDS-PAGE. One Sigma unit of PNGase F activity is equal to 1 IUB milliunit.

Physical form

Supplied as 300 Units/mL enzyme in 50% (v/v) glycerol and 50% (v/v) 20 mM Potassium Phosphate, pH 7.5.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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    W.B. Guenther
    Analytical Letters, 12A, 1305-1305 (1979)
    Improvements on the Prescott-Jones method for the colorimetric analysis of ureido compounds.
    D B Shindler et al.
    Analytical biochemistry, 97(2), 421-422 (1979-09-01)
    Multiple Effects of 2, 3-Butanedione Monoxime.
    Sellin LC and McArdle JJ/
    Pharmacology & Toxicology, 74 (4-5), 305-313 (1994)
    2, 3-Butanedione monoxime (BDM) as a myosin inhibitor.
    Ostap EM.
    Journal of Muscle Research and Cell Motility, 23 (4), 305-308 (2002)
    Chang Liu et al.
    Molecular plant, 11(11), 1389-1399 (2018-10-09)
    The process of pollen germination is crucial for flowering plant reproduction, but the mechanisms through which pollen grains establish polarity and select germination sites are not well understood. In this study, we report that a formin family protein, AtFH5, is localized

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