More Information Product Details
Synonyms Small Ubiquitin-related Modifier 1; GAP-modifying Protein 1; SMT3C, SMT3H3, UBL1; Sentrin; Ubiquitin-homology Domain Protein PIC1 |
Product Type Protein |
Properties
Source/Host E. coli |
Sequence Human SUMO1 (Accession Nr. P63165) tagged to vinyl sulfone. |
Crossreactivity Human |
Formulation Liquid. In 50mM Hepes pH 7.0, 150mM NaCl, 10% glycerol. |
Other Product Data Use: Potent and highly specific inhibitor of SUMO-specific isopeptidases (SENPs). Blocks the hydrolysis of poly-SUMO chains on substrate proteins in vitro and thus enhances poly-SUMO chain accumulation. Add directly to in vitro assay from the stock solution. Depending on conditions, typical concentrations to fully inhibit SENPs in vitro are 1-5μM. |
Declaration Manufactured by Boston Biochem |
Shipping and Handling
Shipping DRY ICE |
Short Term Storage -20°C |
Long Term Storage -80°C |
Handling Advice Aliquot to avoid freeze/thaw cycles. |
Use/Stability Stable for at least 1 year after receipt when stored at -80°C. |
Documents
MSDS No |
Product Specification Sheet
Datasheet Download PDF |
Small Ubiquitin-like Modifier 1 (SUMO1), also known as Sentrin, UBL1, and SMT3C, is synthesized as a 101 amino acid (aa) propeptide with a predicted molecular weight of 11.5 kDa. Human SUMO1 is the most unique of the four identified SUMO proteins and shares only 44%, 47%, and 41% aa sequence identity with SUMO2, SUMO3, and SUMO4, respectively. In contrast, human SUMO1 shares 100% aa sequence identity with the mouse ortholog. SUMOs are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed SUMOylation. All SUMO proteins share a conserved ubiquitin domain and a C-terminal diglycine cleavage/attachment site. Following cleavage of a four aa C-terminal prosegment, the C-terminal glycine residue of SUMO1 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO1 is conjugated to a variety of molecules in the presence of the SAE1/UBA2 SUMO-activating (E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme. In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p. SUMOylation can occur without the requirement of a specific SUMO ligase (E3), where SUMO1 is transferred directly from UBE2I/Ubc9 to specific substrates. In Alzheimers disease models SUMO1 has been shown to influence the generation of amyloid-β peptide by promoting the accumulation of BACE-1. Covalent modification of PTEN by SUMO1 is thought to regulate tumorigenesis by retaining PTEN at the plasma membrane, an effect that suppresses PI 3-Kinase/Akt-dependent tumor growth.