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Key Documents

S0439

Sigma-Aldrich

SUMO-1 human

≥95% (SDS-PAGE), recombinant, expressed in E. coli (GST-tagged)

Synonyma:

Sentrin-1

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

recombinant

expressed in E. coli (GST-tagged)

assay

≥95% (SDS-PAGE)

mol wt

38.5 kDa

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... SUMO1(7341)

General description

Small ubiquitin-like modifier 1 (SUMO-1), a protein, is one of the 5 SUMO paralogs expressed in mammalian cells with a low but significant homology with ubiquitin. This SUMO-1-GST fusion protein is produced from a DNA sequence corresponding to human SUMO-1 fused to a glutathione S-transferase (GST)-tag and is expressed in E. coli cells.

Application

SUMO-1 human has been used in pre-absorption for negative immunostaining to confirm the specificity of the small ubiquitin like modifier 1 (SUMO-1) antibody.

Biochem/physiol Actions

Small ubiquitin-like modifier 1 (SUMO-1) plays a key role in modulating survival, migration, and signal transduction in some cell lines. It can prevent in vitro migration and invasion of RA fibroblast-like synoviocytes (FLSs). Higher expression of SUMO-1 may result in joint destruction in rheumatoid arthritis (RA).
Conjugated to a variety of proteins by UbcH9, including RanGAP1, IκBα, and PML without the requirement of an equivalent E3 ubiquitin ligase.

Physical form

Solution in 50 mM HEPES, pH 8.0, 150 mM NaCl and 1 mM DTT.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Navštívit knihovnu dokumentů

Small ubiquitin-related modifier paralogs are indispensable but functionally redundant during early development of zebrafish.
Yuan, et al.
Cell research, 20, 185-196 (2010)
Minxi Lao et al.
Experimental cell research, 375(1), 52-61 (2018-12-19)
Rheumatoid arthritis (RA) is featured by erosive cartilage and bone destruction. The enhancing aggressive property of fibroblast-like synoviocytes (FLSs) plays a critical role in this process. Small ubiquitin-like modifier (SUMO) proteins, including SUMO-1, SUMO-2, SUMO-3 and SUMO-4, participate in regulating
Kaoru Takahashi et al.
Neuroscience letters, 441(1), 90-93 (2008-07-01)
Sumoylation is a post-translational modification process that is supposed to be implicated in the pathogenesis of several neurodegenerative diseases. Recently, the microtubule-associated protein Tau was identified as a target for sumoylation in the analysis of the transfected cells. We investigated
J M Desterro et al.
Molecular cell, 2(2), 233-239 (1998-09-12)
Activation of NF-kappaB is achieved by ubiquitination and proteasome-mediated degradation of IkappaBalpha. We have detected modified IkappaBalpha, conjugated to the small ubiquitin-like protein SUMO-1, which is resistant to signal-induced degradation. In the presence of an E1 SUMO-1-activating enzyme, Ubch9 conjugated
J M Desterro et al.
FEBS letters, 417(3), 297-300 (1997-12-31)
Ubiquitin conjugating enzymes participate in the thioester cascade that leads to protein ubiquitination. Although Ubc9 is homologous to E2 ubiquitin conjugating enzymes we have shown that it is unable to form a thioester with ubiquitin, but can form a thioester

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