Phospholipase Cβ1 Mouse, Unlabeled, Clone: 16, BD
Mouse Monoclonal Antibody
Supplier: BD Biosciences 610924
Phospholipase C (PLC) hydrolyzes inositol phospholipids into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). The former causes release of Ca2+ from intracellular stores, while the latter is an activator of PKC. At least three isozymes are known: PLCβ, PLCγ, and PLCδ. They recognize phosphatidylinositol (PI), phosphatidylinositol 4-phosphate (PIP2), and phospatidylinositol 4,5 bisphosphate (PIP2) and carry out the Ca2+-dependent hydrolysis of these inositol phospholipids. All three classes contain two highly conserved regions, designated “X” and “Y”, whose structural integrity is essential for a functional catalytic core. The PLCβ subfamily has been reported to contain at least four members: β1, β2, β3 and β4. PLCβ1 has been reported to have been identified and cloned from brain tissue where the PLCβ1 gene encodes for two different mRNAs. The resulting protein products, PLCβ1a (121 aa) and PLCβ1b (1173 aa) differ only at their C-termini. Although PLCγ activity is induced by receptor tyrosine kinase phosphorylation, PLCβ is regulated by G protein α subunits or βγ subunits. In particular, Gαq has been reported to activate PLCβ1.
Immunofluorescence, Western Blotting
|Immunofluorescence, Western Blot|
|Rat Phospholipase Cβ1 aa. 4-159|
|Human, Mouse, Rat|
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