|Calculated MW||148532 Da|
|Other Names||1-phosphatidylinositol 4, 5-bisphosphate phosphodiesterase gamma-1, PLC-148, Phosphoinositide phospholipase C-gamma-1, Phospholipase C-II, PLC-II, Phospholipase C-gamma-1, PLC-gamma-1, PLCG1, PLC1|
|Target/Specificity||A synthetic peptide corresponding to residues near the C-terminus of human PLCgamma1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PLC-I Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand- mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration.|
|Cellular Location||Cell projection, lamellipodium. Cell projection, ruffle. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment|
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Provided below are standard protocols that you may find useful for product applications.
Enzymes of the phospholipase C family catalyze the hydrolysis of phospholipids to yield diacylglycerols and water-soluble phosphorylated derivatives of the lipid head groups (1). Phospholipase C gamma 1 (PLC-gamma 1) hydrolyses phosphatidylinositol-4,5-bisphosphate to the second messengers inositol-1,4,5-trisphosphate and diacylglycerol. PLC-gamma 1 also has mitogenic activity upon growth-factor-dependent tyrosine phosphorylation; however, this activity is not dependent on the phospholipase activity of PLC-gamma 1, but requires an SH3 domain (2). Also, results indicate a lipase-independent role of PLC-gamma in the physiological agonist-induced activation of Ca2+ entry (3). Insulin increased PLCgamma1 tyrosine phosphorylation at Tyr-783 and its colocalization with the IR in punctated structures enriched in cortical actin at the dorsal plasma membrane. This association was found to be independent of PLCgamma1 Src homology 2 domains (4).
1. Argeson AC, et al. Genomics 25(1):29-35, 1995
2. Ye, K, et al. Nature 415(6871):514-4, 2002
3. Patterson RL, et al Cell, 111(4):529-41, 2002
4. Kwon YK et al. J Cell Biol 163(2):375-84, 2003
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