Render Target: STATIC
Render Timestamp: 2024-11-21T13:42:36.665Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-01 15:28:25.163
Product last modified at: 2024-08-20T20:15:08.539Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-SRPK2 (Ser497) Antibody #23708

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 115
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-SRPK2 (Ser497) Antibody recognizes endogenous levels of SRPK2 protein only when phosphorylated at Ser497. The antibody is specific to SRPK2 (Ser497) due to the absence of an equivalent phosphorylation site in both SPRK1 and SPRK3.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser497 of human SRPK2 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Serine/arginine-rich protein-specific kinases (SRPKs) are a small family of serine/threonine protein kinases that phosphorylates serine residues in sequence regions containing repetitive serine/arginine-rich dipeptides (SR domains). There are three known family members (SRPK1-3), of which SRPK1 and SRPK2 are the most well-studied. Multiple research studies have shown these kinases play an important role in post-transcriptional regulation, notably via phosphorylation of SR-family RNA splicing factors (1). SRPK2 has also been implicated in lipid biogenesis, following activation through sequential phosphorylation by mTORC-activated S6K1 and casein kinase 1 (2). Phosphorylation of SRPK2 at Ser494 and Ser497 promotes nuclear translocation of SRPK2, thereby enabling its regulation of mRNA splicing factors involved in lipid biogenesis. Notably, SRPK1 and SRPK2 have both been implicated in the phosphorylation of key viral proteins (3), including the nucleocapsid protein of the SARS and SARS-CoV-2 coronaviruses (4), a modification that may be essential for viral replication.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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