Recombinant Human SUMO3 Mutant K11R Protein, CF

Recombinant Human SUMO3 Mutant K11R Protein, 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: SUMO3

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. Human SUMO3 shares 83% sequence identity with mouse SUMO3. SUMO3 also has high aa sequence homology to SUMO2 and SUMO4, 87% and 75%, respectively. SUMO3 shares only 47% sequence identity with SUMO1. 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 (1-3). 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 (4,5). In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p (6). Because of the high level of sequence homology most studies report effects of SUMO2/3. For example, addition of SUMO2/3 was shown to modulate the function of ARHGAP21, a RhoGAP protein known to be involved in cell migration (7). Other reports indicate that the conjugation by SUMO2/3, but not SUMO1, may represent an important mechanism to protect neurons during episodes of cerebral ischemia (8,9). However, studies suggest that SUMO2/3 expression is regulated in an isoform-specific manner since oxidative stress downregulated the transcription of SUMO3 but not SUMO2 (10).

Mutation of lysine 11 to arginine renders SUMO-3 unable to form poly-SUMO multimers and is useful to investigate mono-SUMOylation or can be used to reduce poly-SUMO chain formation. Human SUMO-3 contains the VK11TE sequence which allows for the formation of poly-SUMO chains. K11 is the conserved lysine that becomes modified and is the point of attachment for the C-terminal glycine of the preceding SUMO-3. The function of SUMO chains has not yet been fully elucidated.

Related Research Areas

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