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Merck
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문서

NGLYFL-RO

Roche

N-Glycosidase F

recombinant form of the gene from Flavobacterium meningosepticum

동의어(들):

N-Glycosidase F, PNGase F, Peptide-N-glycosidase F, Peptide-N4-(acetyl-β-glucosaminyl)-asparagine amidase

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About This Item

효소 위원회 번호:
UNSPSC 코드:
12352204

생물학적 소스

bacterial (Flavobacterium meningosepticum)

Quality Level

재조합

expressed in E. coli

결합

(N-linked)

분석

≥90% (SDS-PAGE)

형태

lyophilized

특이 활성도

>25000 units/mg protein

분자량

35.5 kDa

정제법

electrophoresis

포장

pkg of 100 U (11365185001)
pkg of 250 U (11365193001)

제조업체/상표

Roche

저장 조건

(Keep container tightly closed in a dry and well-ventilated place.)

기술

activity assay: suitable

색상

colorless

최적 pH

7.0-8.0

solubility

water: soluble

적합성

suitable for enzyme test

외래 활성


Endoglycosidase F, none detected

a-Fucosidase, present
b-Galactosidase, present
b-N-Acetylhexosaminidase, present
dA(17h ≤100 units, present

저장 온도

2-8°C

일반 설명

N-Glycosidase F (PNGase F) is a potent enzyme which hydrolyzes at glycosylamine linkage. It also helps in generating a carbohydrate-free peptide and oligosaccharide with di-N-acetylchitobiose unit.

N-glycosidase F, also known as PNGase F, is an asparagine amidase enzyme derived from Flavobacterium meningosepticum. It is widely used as a valuable tool in protein research to investigate and analyze N-glycosylation.

특이성

Hydrolyzes all types of N-glycan chains from glycopeptides and glycoproteins unless they carry α1,3-linked core fucose residues present in insect and plant glycoproteins. Free of contaminating proteolytic activities (x = H or sugar[s]) according to current quality control procedures.

애플리케이션

N-Glycosidase F has been used for deglycosylation of N-glycoproteins.

Use N-glycosidase F to cleave all types of asparagine-bound N-glycans, provided that the amino group as well as the carboxyl group are present in a peptide linkage, and that the oligosaccharide has the minimum length of the chitobiose core unit. The reaction products are ammonia, aspartic acid (in the peptide chain), and the complete oligosaccharide.
Note: N-Glycosidase F, recombinant is also available as a solution.

단위 정의

One unit is the enzyme activity which hydrolyzes 1 nmol dabsyl fibrin glycopeptide or 0.2 nmol dansyl fetuin glycoprotein within 1 minute at 37 °C and pH 7.8.

물리적 형태

Clear, colorless solution after reconstitution

제조 메모

Storage conditions (working solution): 2 to 8 °C
The reconstituted solution is stable at 2 to 8 °C for at least four weeks.

재구성

Dissolving the content in 0.1 ml redist water (100 unit package) or 0.25 ml double-dist. water (250 unit package) respectively, results in a concentration of 100 mM sodium phosphate buffer, 25 mM EDTA, pH 7.2.
Note: N-Glycosidase F, recombinant is also available as solution with 50% glycerol.

기타 정보

For life science research only. Not for use in diagnostic procedures.

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 2

Flash Point (°F)

does not flash

Flash Point (°C)

does not flash


시험 성적서(COA)

제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.

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문서 라이브러리 방문

Highly efficient production of peptides: N-glycosidase F for N-glycomics analysis
Hua L, et al.
Protein Expression and Purification, 17-22 (2014)
Integrated proteomic, phosphoproteomic and N-glycoproteomic analyses of chicken eggshell matrix
Yang R, et al.
Food Chemistry, 330 (2020)
Xueyan Cao et al.
Food chemistry, 276, 266-273 (2018-11-10)
Milk glycoproteins are crucial nutrients with a variety of functions. However, whey N-glycoproteomes in human and bovine milks have not been characterized during lactation. Herein, using lectin enrichment and liquid chromatography tandem mass spectrometry, 68, 58, 100, and 98 N-glycoproteins
A L Tarentino et al.
Biochemistry, 24(17), 4665-4671 (1985-08-13)
Endo-beta-N-acetylglucosaminidase F (Endo F) and peptide:N-glycosidase F (PNGase F) were purified from cultures of Flavobacterium meningosepticum by ammonium sulfate precipitation followed by gel filtration on TSK HW-55(S). This system separated the two enzymes and provided PNGase F in a high

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