|Detection of Human SRPK2 by Western Blot. Western blot shows lysates of MCF‑7 human breast cancer cell line, U937 human histiocytic lymphoma cell line, and A431 human epithelial carcinoma cell line. PVDF membrane was probed with 2 µg/mL of Human SRPK2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5530) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for SRPK2 at approximately 115 to 120 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
SRPK2 (Ser/Arg-rich protein specific kinase 2) is a cytoplasmic, 115‑120 kDa member of the CMGC Ser/Thr protein kinase family of enzymes. It is expressed in many experimental cell lines and serves to selectively phosphorylate Ser on RS domain-containing proteins. This phosphorylation activates RS domain-containing non-snRNP proteins in the spliceosome complex, and initiates mRNA splicing. Human SRPK2 is 688 amino acids (aa) in length. It contains a Pro-rich region (aa 21‑45) that may interact with WW domain-containing proteins, and a split kinase domain (aa 79‑226 and 524‑646). Phosphorylation on S52 and S588 regulates activity. There are at least two splice variants. One shows a 24 aa substitution for aa 1‑13, while a second shows a nine aa substitution for aa 538‑688.
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