Recombinant Human Poly-SUMO2 Wild-type Chains (2-8), CF

Recombinant Human Poly-SUMO2 Wild-type Chains (2-8), CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: Poly-SUMO2

Human Small Ubiquitin-like Modifier 2 (SUMO2), also known as Sentrin2 and SMT3B is synthesized as a 95 amino acid (aa), propeptide with a predicted 11 kDa. SUMO2 contains a two aa C-terminal prosegment and an 18 aa N-terminal protein interacting region between aa 33-50. Poly-SUMO2 represents chains of wild-type recombinant human SUMO2 molecules linked via Lys11, which is the point of attachment for the C-terminal glycine residue of the preceding SUMO2 (1). SUMO2 monomers and dimers (Di-SUMO2) have been removed from the chain mixture. Human SUMO2 shares 100% aa sequence identity with mouse SUMO2. Poly-SUMO2 can be used as a substrate for SUMO-specific isopeptidases (SENPs) and DeSumoylating Isopeptidase 1 that cleave the isopeptide linkage between two SUMO2 molecules (2). It can also be used to investigate mechanisms of binding and recognition by SUMO-activating (E1) enzymes, SUMO-conjugating (E2) enzymes, SUMO ligases (E3s), 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 (3-5). 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 SUMO2 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO2 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 (6,7). In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p (8).

Poly-SUMO-2 chains can be used to investigate mechanisms of chain recognition, binding and hydrolysis by SUMO-specific isopeptidases (SENPs), SUMO-specific E3 ligases or other proteins that contain SUMO-2 binding domains. This product is formed enzymatically with wild type Human Recombinant SUMO-2 linked via lysine 11 which is the point of attachment for the C-terminal glycine of the preceding SUMO-2. Mono-SUMO-2 has been removed from the chain mixture.

Related Research Areas

• NFkB Pathway
• Ubiquitin-like Modifiers (UBLs) and Regulators