|Detection of Human SUMO1 by Western Blot. Western blot shows lysates of K562 human chronic myelogenous leukemia cell line, DU145 human prostate carcinoma cell line, and C2C12 mouse myoblast cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human SUMO1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3289) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). 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 SUMO1, also known as Sentrin, UBL1, and SMT3C, is synthesized as a 101 amino acid (aa) propeptide that contains a four aa C-terminal prosegment. Following prosegment cleavage, the C-terminal glycine is enzymatically attached to a lysine on a target protein. Human SUMO1 shares 100% sequence identity to SUMO1 from mouse. SUMO1 is the most unique of the four identified SUMO proteins and shares only 44%, 47%, and 41% sequence identity to SUMO2, SUMO3, and SUMO4, respectively.
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