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     Western blot analysis of Phospho-CSK (Ser364) in HUVEC lysates using Phospho-CSK (Ser364) antibody.    

  
  

The Phospho-CSK (Ser364) antibody detects the phosphorylated form of C-terminal Src kinase (CSK) at serine residue 364. a key post-translational modification involved in regulating CSK activity and function. CSK is a non-receptor tyrosine kinase that negatively regulates Src-family kinases (SFKs) by phosphorylating their C-terminal inhibitory tyrosine residues. This suppression is critical for maintaining cellular homeostasis, particularly in signaling pathways related to cell adhesion, proliferation, and immune responses.

Phosphorylation at Ser364 modulates CSK’s subcellular localization, enzymatic activity, or interactions with binding partners. Studies suggest this modification may be mediated by kinases such as protein kinase A (PKA) or protein kinase C (PKC), linking CSK activity to downstream pathways like integrin signaling or T-cell receptor activation. Dysregulation of CSK or its phosphorylation has been implicated in pathologies, including immune disorders and cancer metastasis.

The Phospho-CSK (Ser364) antibody is widely used in research to investigate CSK activation dynamics, particularly in contexts such as immune cell signaling, cytoskeletal reorganization, and cancer progression. It enables detection of phosphorylated CSK via techniques like western blotting, immunofluorescence, or immunoprecipitation, helping elucidate mechanisms of SFK regulation and its impact on cellular behavior. Validation typically includes knockout/knockdown controls and peptide competition assays to ensure specificity.