Recombinant Human Di-SUMO3 Wild-type Chains Protein, CF Summary
Details of Functionality
The function of SUMO chains is an area of intense research. K11-linked di-SUMO3 WT Chains are ideal for investigating SUMO-binding proteins and as substrates for SUMO-specific proteases. Reaction conditions will need to be optimized for each specific application.
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -70 °C as supplied.
3 months, -70 °C under sterile conditions after opening.
Supplied as a solution in HEPES, NaCl and DTT.
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Di-SUMO3 Wild-type Chains Protein, CF
Human Small Ubiquitin-like Modifier 3 (SUMO3), also known as SMT3A, is synthesized as a 103 amino acid (aa), propeptide with a predicted 11.5 kDa. SUMO3 contains a two aa C-terminal prosegment. Di-SUMO3 represents two wild-type recombinant human SUMO3 molecules linked via Lys11, which is the point of attachment for the C-terminal glycine residue of the preceding SUMO3. Human SUMO3 shares 83% sequence identity with mouse SUMO3. Di-SUMO3 can be used as a substrate for SUMO-specific isopeptidases (SENPs) and DeSUMOylating Isopeptidase 1 that cleave the isopeptide linkage between two adjacent SUMO3 molecules. Di-SUMO3 can also be used to investigate mechanisms of binding and recognition by SUMO-activating (E1) enzymes, SUMO-conjugating (E2) enzymes, SUMO E3 ligases, and other proteins that contain SUMO binding domains.
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. Unlike SUMO1 which is usually conjugated to proteins as a monomer, SUMO2 and SUMO3 form high molecular weight polymers on proteins. All SUMO proteins share a conserved Ubiquitin domain and a C-terminal diglycine cleavage/attachment site. Following prosegment cleavage, the C-terminal glycine residue of SUMO3 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO3 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.
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