F8435
PNGase F from Elizabethkingia meningoseptica
lyophilized powder, recombinant, expressed in E. coli
동의어(들):
N-Glycosidase F, PNGase F from Chryseobacterium meningosepticum, PNGase F from Flavobacterium meningosepticum, Peptide N-glycosidase
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모든 사진(1)
About This Item
CAS Number:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.54
추천 제품
재조합
expressed in E. coli
Quality Level
결합
(N-linked)
Grade
Proteomics Grade
양식
lyophilized powder
특이 활성도
≥1,000 U/mg
유통기한
≥1 weeks at 2‑8 °C (for reconstituted solution)
≥1 yr at -20 °C
분자량
~36 kDa
배송 상태
wet ice
저장 온도
−20°C
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애플리케이션
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-teminal 6x histidine fusion tag.
Used to deglycosylate protein.
생화학적/생리학적 작용
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
PNGase F was used for deglycosylation of P-glycoprotein in a study to investigate the dual impact of statins on p-glycoprotein and its effect on doxorubicin cytotoxicity in human neuroblastoma cells. It was used to treat a purified protein, mouse cone ultraviolet (MUV) pigment, before use in quantitative immunoblot analysis in a study It is used to deglycosylate N-linked glycoproteins. 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-teminal 6x histidine fusion tag.
단위 정의
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.
신호어
Danger
유해 및 위험 성명서
예방조치 성명서
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
이미 열람한 고객
Maria Nordgren et al.
Methods in molecular biology (Clifton, N.J.), 2271, 155-167 (2021-04-29)
O-glycosylation is a difficult posttranslational modification to analyze. O-glycans are labile and often cluster making their analysis by LC-MS very challenging. OpeRATOR is an O-glycan specific protease that cleaves the protein backbone N-terminally of glycosylated serine and threonine residues. This
Lauren L Daniele et al.
Investigative ophthalmology & visual science, 46(6), 2156-2167 (2005-05-26)
To test the hypothesis that Nrl(-)(/)(-) photoreceptors are cones, by comparing them with WT rods and cones using morphological, molecular, histochemical, and electrophysiological criteria. The photoreceptor layer of fixed retinal tissue of 4- to 6-week-old mice was examined in plastic
T H Plummer et al.
The Journal of biological chemistry, 259(17), 10700-10704 (1984-09-10)
Endo-beta-N-acetylglucosaminidase F preparations from Flavobacterium meningosepticum have been found to contain peptide:N-glycosidase activity. Only the second activity, designated as peptide:N-glycosidase F, readily cleaves the beta-aspartylglycosylamine linkage of a fetuin triantennary complex glycopeptide, as shown by the isolation of the corresponding
Evelyn Sieczkowski et al.
International journal of cancer, 126(9), 2025-2035 (2009-09-10)
The development of multidrug resistance (MDR) is a major problem during cancer treatment. Drug efflux via ATP-binding cassette (ABC) transporters is the main mechanism responsible for resistance to chemotherapeutics. We have recently observed that statins enhance susceptibility to doxorubicin-induced apoptosis
Ulla-Maja Bailey et al.
Journal of proteome research, 11(11), 5376-5383 (2012-10-09)
Asparagine-linked glycosylation is a common post-translational modification of proteins in eukaryotes. Mutations in the human ALG3 gene cause changed levels and altered glycan structures on mature glycoproteins and are the cause of a severe congenital disorder of glycosylation (CDG-Id). Diverse
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