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Key Documents

P9120

Sigma-Aldrich

PNGase F from Elizabethkingia meningoseptica

recombinant, expressed in E. coli, set of 100 units nanomolar unit

동의어(들):

N-Glycanase®, N-Glycosidase F, PNGase F from Chryseobacterium meningosepticum, PNGase F from Flavobacterium meningosepticum, Peptide N-glycosidase

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About This Item

CAS Number:
효소 위원회 번호:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.54

재조합

expressed in E. coli

Quality Level

결합

(N-linked)

특이 활성도

≥10 units/mg protein

분자량

36 kDa

포장

set of 100 units nanomolar unit

배송 상태

wet ice

저장 온도

2-8°C

유사한 제품을 찾으십니까? 방문 제품 비교 안내

애플리케이션

PNGase F from Elizabethkingia meningoseptica has been used in deglycosylation
  • of recombinant soybean agglutinin (rSBA) in Nicotiana benthamiana (NbrSBA) and Solanum tuberosum (StrSBA)
  • of frontal cortical lysate to verify the glycosylation profile of β-secretase (BACE proteins)
  • of cell lysate for evaluating the siRNA silencing of cellular prion protein (PrPc) post transfection

PNGase F is a glycosylasparaginase used to deglycosylate proteins. It is widely used in structure-function studies of glycoproteins.
Used to deglycosylate protein.

생화학적/생리학적 작용

PNGase F 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 deaminates the asparagine to aspartic acid, but leaves the oligosaccharide intact. PNGase F will not remove oligosaccharides containing α(1-3)-linked core fucose, commonly found in plant glycoproteins. A tripeptide with the oligosaccharide-linked asparagine as the central residue is the minimal substrate for PNGase F.
Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.

포장

Each set includes enzyme, two formulations of 5× reaction buffer (for routine and mass spectrometry downstream analysis), detergent and denaturation solutions

단위 정의

One unit will catalyze the release of N-linked oligosaccharides from 1 micromole 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.

법적 정보

N-Glycanase is a registered trademark of Agilent Technologies Inc

신호어

Danger

유해 및 위험 성명서

Hazard Classifications

Acute Tox. 3 Dermal - Acute Tox. 4 Oral - Aquatic Acute 1 - Aquatic Chronic 1 - Eye Dam. 1 - Repr. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

G E Norris et al.
Structure (London, England : 1993), 2(11), 1049-1059 (1994-11-15)
Peptide:N-glycosidase F (PNGase F) is an enzyme that catalyzes the complete removal of N-linked oligosaccharide chains from glycoproteins. Often called an endoglycosidase, it is more correctly termed an amidase or glycosylasparaginase as cleavage is at the asparagine-sugar amide linkage. The
Mitochondrial respiratory inhibition and oxidative stress elevate beta-secretase (BACE1) proteins and activity in vivo in the rat retina
Xiong K, et al.
Experimental Brain Research. Experimentelle Hirnforschung. Experimentation Cerebrale, 181(3), 435-446 (2007)
PrPc activation induces neurite outgrowth and differentiation in PC12 cells: role for caveolin-1 in the signal transduction pathway
Pantera B, et al.
Journal of Neurochemistry, 110(1), 194-207 (2009)
Reynald Tremblay et al.
Transgenic research, 20(2), 345-356 (2010-06-19)
Soybean agglutinin (SBA) is a specific N-acetylgalactosamine-binding plant lectin that can agglutinate a wide variety of cells. SBA has great potential for medical and biotechnology-focused applications, including screening and treatment of breast cancer, isolation of fetal cells from maternal blood
Amelie Croset et al.
Journal of biotechnology, 161(3), 336-348 (2012-07-21)
Glycosylation is one of the most common posttranslational modifications of proteins. It has important roles for protein structure, stability and functions. In vivo the glycostructures influence pharmacokinetics and immunogenecity. It is well known that significant differences in glycosylation and glycostructures

문서

N-Linked Glycan Strategies; Sigma-Aldrich.com

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