PLC-β3 antibodies are immunoglobulin-based reagents designed to bind specifically to the Phospholipase C beta 3 enzyme (UniProt ID: Q01970), which catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP₂) into second messengers diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP₃) . These antibodies are essential for detecting PLC-β3 expression in human, mouse, and rat samples across techniques like Western blot (WB), immunohistochemistry (IHC), and immunofluorescence (IF) .
Western Blot Validation: Detects PLC-β3 at ~139 kDa (human) and ~150 kDa (murine) .
Functional Studies: Used to explore PLC-β3's role in immune cell activation, neutrophil differentiation, and cancer progression .
Post-Translational Modification Analysis: Phospho-specific antibodies (e.g., anti-Ser537) identify activated PLC-β3 in signaling pathways .
PLC-β3 regulates Stat5 activity in hematopoietic stem cells (HSCs) by forming a multi-molecular complex (SPS complex) with the phosphatase SHP-1. This interaction inhibits Stat5 phosphorylation, thereby suppressing myeloproliferative neoplasms (MPNs) and aberrant neutrophil production .
In macrophages, PLC-β3 deficiency increases sensitivity to apoptosis due to reduced Bcl-XL expression, implicating its role in atherosclerosis and tumor survival .
Overexpression studies in prostate (DU145) and cervical (HeLa) cancer cells reveal PLC-β3's involvement in chemokine-mediated ERK activation and metastasis .
PLC-β3 is highly expressed in brain tissues, where it modulates G protein-coupled receptor (GPCR) signaling. Dysregulation correlates with neurological disorders and hypertension .
Human Samples: Strong reactivity in HeLa, OVCAR3, and MCF7 cell lines .
Murine/Rat Samples: Detected in RAW 264.7 macrophages and brain tissues .
Specificity Controls: No cross-reactivity with PLC-β1, β2, or β4 isoforms .
Anti-phospho-Ser537 antibodies confirm PLC-β3 activation in UV-treated MCF-7 cells and brain lysates, highlighting its role in stress responses .
PLC-β3 antibodies have identified the enzyme as a potential biomarker for: