추천 제품
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.
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.
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.
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.
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.
이미 열람한 고객
Highly efficient production of peptides: N-glycosidase F for N-glycomics analysis
Protein Expression and Purification, 17-22 (2014)
Integrated proteomic, phosphoproteomic and N-glycoproteomic analyses of chicken eggshell matrix
Food Chemistry, 330 (2020)
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
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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