|Detection of Human SUMO2/3/4 by Western Blot. Western blot shows lysates of K562 human chronic myelogenous leukemia cell line and DU145 human prostate carcinoma cell line. PVDF membrane was probed with 1 µg/mL of Human/Mouse SUMO2/3/4 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3020) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for SUMO2/3/4 at approximately 12 kDa (as indicated) along with multiple sumoylated proteins. This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 4.|
Small Ubiquitin-like Modifiers (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 ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. All SUMO proteins share the conserved ubiquitin domain and the C-terminal diglycine cleavage/attachment site. Human SUMO2, also known as Sentrin2 and SMT3B is synthesized as a 95 amino acid (aa), 11 kDa propeptide that contains a two aa C-terminal prosegment, and an 18 aa N-terminal protein interacting region (aa 33‑50). Following prosegment cleavage, the C-terminal glycine is enzymatically attached to a lysine on a target protein. Human SUMO2 shares 100% sequence identity to SUMO-2 from mouse. SUMO2 also has very high sequence homology to SUMO3 and SUMO4, 86 % and 85%, respectively. SUMO2 shares only 44% sequence identity to SUMO1.
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