Phospholipase Cβ4 Mouse, Unlabeled, Clone: 56, BD

Description

• 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
• Host Species: Mouse Clone: 56 Isotype: IgG1 Species Reactivity: Rat Immunogen: Human Phospholipase Cβ4 aa
• 752-961 Formula Weight [Chemical]: 130kDa Immunofluorescence, Western Blotting