S0439
SUMO-1 human
≥95% (SDS-PAGE), recombinant, expressed in E. coli (GST-tagged)
Synonym(s):
Sentrin-1
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About This Item
recombinant
expressed in E. coli (GST-tagged)
Quality Level
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
Conjugated to a variety of proteins by UbcH9, including RanGAP1, IκBα, and PML without the requirement of an equivalent E3 ubiquitin ligase.
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).
Physical form
Solution in 50 mM HEPES, pH 8.0, 150 mM NaCl and 1 mM DTT.
Storage Class
10 - Combustible liquids
wgk
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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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