Phospholipase C beta 4 (PLCb4) (AA 752-961) antibody

Details for Product No. ABIN968900
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Synonyms ARCND2, PI-PLC, A930039J07Rik, AI854601, C230058B11Rik, Beta4aa, RATBETA4AA
AA 752-961
(2), (1)
(2), (1)
Clonality (Clone)
Monoclonal ()
Western Blotting (WB), Immunofluorescence (IF)
(3), (2)
Pubmed 4 references available
Quantity 50 μg
Shipping to United States (Change)
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Catalog No. ABIN968900
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Immunogen Human Phospholipase C beta4
Clone 56
Isotype IgG1
Cross-Reactivity Fruit Fly (Drosophila melanogaster), Mouse (Murine), Rat (Rattus)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. 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.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name Phospholipase C beta 4
Background 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: alpha, beta, and gamma. 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 PLCbeta isoenzymes is uniquely regulated by G protein subunits, while PLCgamma is activated following phosphorylation by protein tyrosine kinases. The beta subfamily of PLC consists of at least four members: beta1, beta2, beta3, and beta4. PLCbeta4 differs from the other members in that it is not activated by G protein betagamma subunits, it is not found in the liver or kidney, and it is inhibited by ribonucleotides. Various isoforms of PLbetaC4 result from alternative splicing or proteolytic cleavage. PLCbeta4 is expressed in retina and brain and knockout mice display ataxia and abnormalities in metabotropic glutamate receptor function in the cerebellum. Thus, PLCbeta4 is primarily found in neuronal tissues where it is thought to be important in neurotransmitter signaling pathways.
Synonyms: PLCbeta4
Molecular Weight 130 kDa
Application Notes The Drosophila melanogaster gene, no receptor potential A (abbreviated as norpA), encodes a 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase involved in calcium-mediated signaling, which is a component of the membrane fraction. Its amino acid sequence contains a phosphatidylinositol-specific phospholipase C (X domain), a phosphoinositide-specific phospholipase C (PLC) and a phosphatidylinositol-specific phospholipase C (Y domain). Similar sequences have been identified in C. elegans, Homo sapiens, Mus musculus, Rattus norvegicus, and Saccharomyces cerevisiae. It has been mapped by recombination to 1-6.5 and cytologically to 4C1.

Related Products: ABIN967389, ABIN968539, ABIN968583

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-Phospholipase C beta 4 (PLCb4) (AA 752-961) antibody Western blot analysis of Phospholipase Cbeta4. Lysates from PC12 cells (Rat neuroblastoma, ATCC CRL-1721) (10 myg/lane), S2 cells (15 myg/lane), and 0-12 hour Drosophila embryos (15 myg/lane) were probed with the mouse anti-Phospholipase Cbeta4 antibody at concentrations of 1.0 myg/ml (lane 1), 0.5 myg/ml (lane 2), and 0.25 myg/ml (lane 3). This antibody detects a band of 130 kDa in all lysates.
Product cited in: Kano, Hashimoto, Watanabe et al.: "Phospholipase cbeta4 is specifically involved in climbing fiber synapse elimination in the developing cerebellum." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, Issue 26, pp. 15724-9, 1999 (PubMed).

Kim, Jun, Lee et al.: "Phospholipase C isozymes selectively couple to specific neurotransmitter receptors." in: Nature, Vol. 389, Issue 6648, pp. 290-3, 1997 (PubMed).

Alvarez, Ghalayini, Xu et al.: "cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4)." in: Genomics, Vol. 29, Issue 1, pp. 53-61, 1996 (PubMed).

Lee, Park, Lee et al.: "Purification, molecular cloning, and sequencing of phospholipase C-beta 4." in: The Journal of biological chemistry, Vol. 268, Issue 28, pp. 21318-27, 1993 (PubMed).

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