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Merck
모든 사진(2)

주요 문서

U6253

Sigma-Aldrich

Ubiquitin from bovine erythrocytes

BioUltra, ≥98% (SDS-PAGE), essentially salt-free, lyophilized powder

동의어(들):

ATP-dependent proteolytic factor, Ub

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About This Item

CAS Number:
MDL number:
UNSPSC 코드:
12352200
NACRES:
NA.32

생물학적 소스

bovine erythrocytes

Quality Level

제품 라인

BioUltra

분석

≥98% (SDS-PAGE)

형태

essentially salt-free, lyophilized powder

저장 조건

(Tightly closed. Dry)

기술

western blot: suitable

불순물

salt, essentially free

solubility

water: 1 mg/mL, clear, colorless

UniProt 수납 번호

저장 온도

2-8°C

유전자 정보

bovine ... LOC(101902760)

유사한 제품을 찾으십니까? 방문 제품 비교 안내

일반 설명

Research area: Cancer

Ubiquitin is a highly conserved regulatory protein. It is found in all eukaryotic cells and is virtually identical across all forms of life including yeast, humans, and plants. ubiquitin structure contains seven Lys residues and an N-terminus, all of which are target sites for ubiquitination.
This product is from bovine red blood cells. It is not a recombinant product. The production process is considered proprietary, however it includes heat treatment as well as purification by chromatography and dialysis.

애플리케이션

Ubiquitin from bovine erythrocytes has been used to study the role of exogenous ubiquitin in chronic β-adrenergic receptor (β-AR)-stimulated myocardial remodeling. It has also been used to test the inhibitor of nuclear factor kappa-B kinase subunit beta (IKKβ) ubiquitylation.

Ubiquitin from bovine erythrocytes can be used for in vitro ubiquitinylation assay. The product can also be used as a marker in western blotting.

생화학적/생리학적 작용

Ubiquitination is a post-translational modification process where ubiquitin-protein is attached to a substrate protein. Ubiquitination plays a vital role in the regulation of cellular signaling in various biological processes such as apoptosis, protein processing, immune response, and DNA repair. Ubiquitination mediates protein degradation via the ubiquitin-proteasome pathway. Ubiquitination is implicated in various cellular signaling pathways. Polyubiquitination modulates the signal activation of NF-κ-B inhibitor alpha (IkB-α) in the inflammatory signaling pathway. Elevated levels of ubiquitin have been observed in various diseases such as parasitic and allergic diseases, alcoholic liver disease, type 2 diabetes, β2-microglobulin amyloidosis, and chronic hemodialysis.

제조 메모

Ubiquitin from bovine erythrocytes can dissolved in water at 1 mg/ml to yield a clear, colorless solution.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


시험 성적서(COA)

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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

Takeshi Miura et al.
FEMS microbiology letters, 239(1), 171-179 (2004-09-29)
When Saccharomyces cerevisiae cells are exposed to high hydrostatic pressure, tryptophan permease Tat2 is degraded in a manner dependent on Rsp5 ubiquitin ligase. Consequently, cell growth is arrested in tryptophan auxotrophic strains. Here we show that of 17 ubiquitin-specific protease
The ubiquitin system for protein degradation.
A Hershko et al.
Annual review of biochemistry, 61, 761-807 (1992-01-01)
Errol W Robinson et al.
Analytical chemistry, 80(19), 7508-7515 (2008-08-30)
Field asymmetric waveform ion mobility spectrometry (FAIMS) has emerged as an analytical tool of broad utility, especially in conjunction with mass spectrometry. Of particular promise is the use of FAIMS and 2-D ion mobility methods that combine FAIMS with conventional
A L Schwartz et al.
Annual review of medicine, 50, 57-74 (1999-03-12)
The ubiquitin-proteasome pathway plays a pivotal role in the degradation of short-lived and regulatory proteins important in a variety of basic cellular processes, including regulation of the cell cycle, modulation of cell surface receptors and ion channels, and antigen presentation.
K D Wilkinson et al.
The Journal of biological chemistry, 256(17), 9235-9241 (1981-09-10)
It was previously shown that ubiquitin is very similar to the polypeptide cofactor of the ATP-dependent protein degradation system from rabbit reticulocytes (Wilkinson, K. D., Urban, M. K., and Haas, A. L. (1980) J. Biol. Chem. 255, 7529-7532). We have

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