Adipogen/Poly-SUMO3 Wild-type Chains (3-8) (human) (rec.)/AG-40T-0325-C025/25 µg

来自 : 发布时间：2024-05-12

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Small Ubiquitin-related Modifier 3; HSMT3; SMT3 Homolog 1; Ubiquitin-like Protein SMT3B

Protein

E. coli

3-8 human SUMO3 (Accession Nr. P0CG47) covalently linked through an isopeptide bond at K11 residue of one SUMO3 molecule and the C-terminal glycine residue of another SUMO3 molecule.

Human

Liquid. In HEPES, NaCl and DTT.

Use: Formed enzymatically with wild type human recombinant SUMO-3 linked via lysine 11 which is the point of attachment for the C-terminal glycine of the preceding SUMO-3. Mono-SUMO-3 has been removed from the chain mixture. Ideal for investigating SUMO-binding proteins and as substrates for SUMO-specific proteases. Reaction conditions will need to be optimized for each specific application.

Manufactured by Boston Biochem

DRY ICE

-20°C

-80°C

Aliquot to avoid freeze/thaw cycles.

Stable for at least 1 year after receipt when stored at -80°C.

No

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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. Human SUMO3 shares 83% sequence identity with mouse SUMO3. 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. 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.