#55512 PLCγ2 (E5U4T) Rabbit mAb
|PLCγ2 (E5U4T) Rabbit mAb recognizes endogenous levels of total PLCγ2 protein.|
|Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human PLCγ2 protein.|
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Western blot analysis of extracts from various cell lines using PLCγ2 (E5U4T) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower).
Immunoprecipitation of PLCγ2 from HCT 116 cell extracts. Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is PLCγ2 (E5U4T) Rabbit mAb. Western blot analysis was performed using PLCγ2 (E5U4T) Rabbit mAb.
Confocal immunofluorescent analysis of HCT 116 cells (left, positive) and 22Rv1 cells (right, negative) using PLCγ2 (E5U4T) Rabbit mAb (green). Actin filaments were labeled with DyLight™ 554 Phalloidin #13054 (red). Samples were mounted in ProLong® Gold Antifade Reagent with DAPI #8961 (blue).
Phosphoinositide-specific phospholipase C (PLC) plays a significant role in transmembrane signaling. In response to extracellular stimuli such as hormones, growth factors, and neurotransmitters, PLC hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG) (1). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ, and PLCε. Phosphorylation is one of the key mechanisms that regulate the activity of PLC. PLCγ is activated by both receptor and non-receptor tyrosine kinases (2). PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783, and 1248 (3). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (4). PLCγ2 is engaged in antigen-dependent signaling in B cells and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at Tyr753, 759, 1197, and 1217 is correlated with PLCγ2 activity (5,6).
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