SRPK2 (serine/arginine- rich protein-specific kinase 2) belongs to the family of mitosis-regulated kinases called SRPK. This protein primarily resides in the cytoplasm, and contains bipartite kinase domains, which are separated by a spacer region. This protein has a molecular weight of 115kDa.
Synonyms: Anti-SFRS protein kinase 2; Anti-SR-protein-specific kinase 2; Anti-Serine/arginine- rich protein-specific kinase 2; Anti-Serine/threonine-protein kinase SRPK2
MDL Number: MFCD02264113
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: SRPK2 (serine/arginine- rich protein-specific kinase 2) leads to elevated expression cyclin A1, by interacting with and binding acinus protein. This protein is a Ser/Arg (SR), which plays an essential role in the splicing of RNA. Phosphorylation of this protein by SRPK2 results in the movement of this protein to nucleoplasm from nucleus speckles. Acinus protein mediates cell growth and proliferation. The expression of both these proteins is up-regulated in human myeloid hematological malignancies. SRPK2 also phosphorylates Srp75, an SR protein, which results in elevated expression of human immunodeficiency virus (HIV). It phosphorylates the RS motif of BLRF2 protein of Epstein-Barr virus (EBV), which is essential for the replication of EBV. It is also essential for the replication of hepatitis C virus, and thus has potential as a therapeutic target for novel antiviral agents.
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