Phospholipase Cβ4 Mouse, Unlabeled, Clone: 56, BD
Mouse Monoclonal Antibody
Manufacturer: BD Biosciences 612646
Phospholipase C (PLC) hydrolyzes inositol phospholipids into diacylglycerol and inositol 1,4,5-trisphosphate (IP3). Multiple distinct PLC isoenzymes have been identified and divided into three structural types: α, β, and γ. This classification is based primarily on the location of the conserved X and Y domains, whose structural integrity is essential for a functional catalytic core. The activation of PLCβ isoenzymes is uniquely regulated by G protein subunits, while PLCγ is activated following phosphorylation by protein tyrosine kinases. The β subfamily of PLC consists of at least four members: β1, β2, β3, and β4. PLCβ4 differs from the other members in that it is not activated by G protein βγ subunits, it is not found in the liver or kidney, and it is inhibited by ribonucleotides. Various isoforms of PLβC4 result from alternative splicing or proteolytic cleavage. PLCβ4 is expressed in retina and brain and knockout mice display ataxia and abnormalities in metabotropic glutamate receptor function in the cerebellum. Thus, PLCβ4 is primarily found in neuronal tissues where it is thought to be important in neurotransmitter signaling pathways.
Immunofluorescence, Western Blotting
|Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.|
|Store undiluted at -20°C.|
|Human Phospholipase Cβ4 aa. 752-961|
|Fly, Human, Murine, Rat|
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