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G1549

PNGase F Glycosidase

de-glycosylates N-linked glycoproteins for analysis, suitable for mass spectrometry, recmobinant, expressed in E. coli

Synonym(e):

N-Glycosidase F, PNGase F aus Chryseobacterium meningosepticum, PNGase F aus Flavobacterium meningosepticum, Peptid-N-Glycosidase

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Ihnen/SKUVerfügbarkeitPreis
50 units
Warenkorb auf Verfügbarkeit prüfen
€ 264,00
300 units
Warenkorb auf Verfügbarkeit prüfen
€ 1.330,00

Über diesen Artikel

CAS-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.54
EG-Nummer:
MDL number:
Specific activity:
≥1000 U/mg
Recombinant:
expressed in E. coli
Shelf life:
≥1 yr at -20 °C

€ 264,00


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Produktname

PNGase F aus Elizabethkingia meningoseptica, ready-to-use solution, recombinant, expressed in E. coli

recombinant

expressed in E. coli

Quality Segment

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

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 and in deglycosylation of chondroitin sulfate proteoglycan.
Wird zur Deglykolisierung von Protein verwendet.

Biochem/physiol Actions

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. It is cost-effectively produced on a large scale in prokaryotic hosts and requires divalent zinc ions for its enzymatic activity.
Spaltet ein gesamtes Glykan von einem Glykoprotein ab, vorausgesetzt, die glykolysierte Asparagineinheit ist an ihrem Amino- und Carboxyterminus mit einer Polypeptidkette substituiert.

Physical form

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

Other Notes

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.

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Dieser Artikel
P9120F8435P7367
specific activity

≥1000 U/mg

specific activity

≥10 units/mg protein

specific activity

≥1,000 U/mg

specific activity

-

grade

Proteomics Grade

grade

-

grade

Proteomics Grade

grade

-

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

form

ready-to-use solution

form

-

form

lyophilized powder

form

powder

shelf life

≥1 yr at -20 °C

shelf life

-

shelf life

≥1 weeks at 2‑8 °C (for reconstituted solution), ≥1 yr at -20 °C

shelf life

≥1 weeks at 2‑8 °C (for a reconstituted solution >500 units/ml), ≥1 yr at 2‑8 °C, Solution is stable for at least 3 freeze-thaw cycles

mol wt

~36 kDa

mol wt

36 kDa

mol wt

~36 kDa

mol wt

~36 kDa


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Lagerklasse

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable



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