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.
原厂资料:
注意事项:
1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.