The antibody is widely used to monitor PLCG1 activation in response to growth factors such as PDGF and EGF. For example, studies employing this antibody have demonstrated that PDGF stimulation induces Tyr783 phosphorylation in NIH/3T3 fibroblasts, correlating with PLCG1 enzymatic activity . Similarly, EGFR-dependent activation of PLCG1 has been quantified in HEK293 cells using this reagent, highlighting its role in receptor-mediated signaling .
PLCG1 is critical for T-cell receptor (TCR)-mediated interleukin-2 (IL-2) production. Antibodies detecting Tyr783 phosphorylation revealed that mutations in the SH2C domain or Tyr783 site impair IL-2 promoter activation, underscoring the necessity of this phosphorylation event in transcriptional regulation .
Western Blotting:
Flow Cytometry:
PLCG1 dysregulation is implicated in cancers (e.g., chronic myeloid leukemia) and autoimmune diseases. Antibodies targeting Tyr783 phosphorylation are critical tools for studying PLCG1 activation in disease contexts. Structural insights from PLCG1 crystallography (e.g., autoinhibitory lobe displacement) inform drug design targeting this enzyme .