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ELISA Kit for Bovine 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

SKU : BHE13808250

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E0269b
Alternative Names	PLC-148 ; Phosphoinositide phospholipase C-gamma-1 ; Phospholipase C-II ; PLC-II ; Phospholipase C-gamma-1 ; PLC-gamma-1
Categories	Elisa
Function	Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as fibroblast growth factor receptors. Plays a role in actin reorganization and cell migration.
Specificity	Natural and recombinant Bovine 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Subcellular Location	Cell projection lamellipodium Cell projection ruffle Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment.
Entryname	PLCG1_BOVIN
Platform	PF00168
Protein Name	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Sequence	50: MAGAASPCAN ; GCGPSAPSDA ; EVVHLCRSLE ; VGTVMTLFYS ; KKSQRPERKT ; 100: FQVKLETRQI ; TWSRGADKIE ; GAIDIREIKE ; IRPGKTSRDF ; DRYQEDPAFR ; 150: PDQSHCFVIL ; YGMEFRLKTL ; SLQATSEDEV ; NMWIRGLTWL ; MEDTLQAATP ; 200: LQIERWLRKQ ; FYSVDRNRED ; RISAKDLKNM ; LSQVNYRVPN ; MRFLRERLTD ; 250: LEQRTSDITY ; GQFAQLYRSL ; MYSAQKTMDL ; PFLEASALRA ; GERPELCRVS ; 300: LPEFQQFLLE ; YQGELWAVDR ; LQVQEFMLSF ; LRDPLREIEE ; PYFFLDEFVT ; 350: FLFSKENSIW ; NSQLDEVCPD ; TMNNPLSHYW ; ISSSHNTYLT ; GDQFSSESSL ; 400: EAYARCLRMG ; CRCIELDCWD ; GPDGMPVIYH ; GHTLTTKIKF ; SDVLHTIKEH ; 450: AFVASEYPVI ; LSIEDHCSIA ; QQRNMAQYFK ; KVLGDTLLTK ; PVDIAADGLP ; 500: SPNQLKRKIL ; IKHKKLAEGS ; AYEEVPTSVM ; YSENDISNSI ; KNGILYLEDP ; 550: VNHEWYPHYF ; VLTSSKIYYS ; EETSSDQGNE ; DEEEPKEASG ; STELHSNEKW ; 600: FHGKLGAGRD ; GRHIAERLLT ; EYCIETGAPD ; GSFLVRESET ; FVGDYTLSFW ; 650: RNGKVQHCRI ; HSRQDAGTPK ; FFLTDNLVFD ; SLYDLITHYQ ; QVPLRCNEFE ; 700: MRLSEPVPQT ; NAHESKEWYH ; ASLTRAQAEH ; MLMRVPRDGA ; FLVRKRNEPN ; 750: SYAISFRAEG ; KIKHCRVQQE ; GQTVMLGNSE ; FDSLVDLISY ; YEKHPLYRKM ; 800: KLRYPINEEA ; LEKIGTAEPD ; YGALYEGRNP ; GFYVEANPMP ; TFKCAVKALF ; 850: DYKAQREDEL ; TFTKSAIIQN ; VEKQEGGWWR ; GDYGGKKQLW ; FPSNYVEEMV ; 900: SPAALEPERE ; HLDENSPLGD ; LLRGVLDVPA ; CQIAVRPEGK ; NNRLFVFSIS ; 950: MASVAHWSLD ; VAADSQEELQ ; DWVKKIREVA ; QTADARLTEG ; KMMERRKKIA ; 1000: LELSELVVYC ; RPVPFDEEKI ; GTERACYRDM ; SSFPETKAEK ; YVNKAKGKKF ; 1050: LQYNRLQLSR ; IYPKGQRLDS ; SNYDPLPMWI ; CGSQLVALNF ; QTPDKPMQMN ; 1100: QALFLAGGHC ; GYVLQPSVMR ; DEAFDPFDKS ; SLRGLEPCAI ; CIEVLGARHL ; 1150: PKNGRGIVCP ; FVEIEVAGAE ; YDSIKQKTEF ; VVDNGLNPVW ; PAKPFHFQIS ; 1200: NPEFAFLRFV ; VYEEDMFSDQ ; NFLAQATFPV ; KGLKTGYRAV ; PLKNNYSEGL ; 1250: ELASLLVKID ; VFPAKQENGD ; LSPFGGASLR ; ERSCDASGPL ; FHGRAREGSF ; 1291: EARYQQPFED ; FRISQEHLAD ; HFDGRDRRTP ; RRTRVNGDNR ; L
Sequence Length	1291
String	P08487
Sub Unit	Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts (via SH3 domain) with AGAP2. Interacts with LAT (phosphorylated) upon TCR activation. Interacts (via SH3 domain) with the Pro-rich domain of TNK1. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts (via SH3 domain) with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and CLNK (By similarity). Interacts with RALGPS1 (By similarity). Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts with AXL and KIT (By similarity). Interacts (via SH2 domain) with RET.

Uniprot	P08487
Gene Name	PLCG1
Immunogen Species	Bos Taurus (Cattle)
Kegg	bta:281987
Unigene	Bt.307

Reference	1. "Sequence similarity of phospholipase C with the non-catalytic region of src." Stahl M.L., Ferenz C.R., Kelleher K.L., Kriz R.W., Knopf J.L. Nature332:269-272(1988) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PARTIAL PROTEIN SEQUENCE 2. "Tyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro." Kim J.W., Sim S.S., Kim U.H., Nishibe S., Whal M.I., Carpenter G., Rhee S.G. J. Biol. Chem.265:3940-3943(1990) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254 3. "Identification of two epidermal growth factor-sensitive tyrosine phosphorylation sites of phospholipase C-gamma in intact HSC-1 cells." Whal M.I., Nishibe S., Kim J.W., Kim H.K., Rhee S.G., Carpenter G. J. Biol. Chem.265:3944-3948(1990) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254 4. "Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors." Anderson D., Koch C.A., Grey L., Ellis C., Moran M.F., Pawson T. Science250:979-982(1990) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH PDGFRA 5. "PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254." Kim H.K., Kim J.W., Zilberstein A., Margolis B., Kim J.G., Schlessinger J., Rhee S.G. Cell65:435-441(1991) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT TYR-783 AND TYR-1254 6. "Direct association between the Ret receptor tyrosine kinase and the Src homology 2-containing adapter protein Grb7." Pandey A., Liu X., Dixon J.E., Di Fiore P.P., Dixit V.M. J. Biol. Chem.271:10607-10610(1996) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH RET 7. "Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide." Pascal S.M., Singer A.U., Gish G., Yamazaki T., Shoelson S.E., Pawson T., Kay L.E., Forman-Kay J.D. Cell77:461-472(1994) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: STRUCTURE BY NMR OF 663-759

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