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

SKU : BHE13809105

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E0269r
Alternative Names	Phosphoinositide phospholipase C-gamma-1 ; 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 Rat 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.
Detection Range	0.312-20ng/mL
Entryname	PLCG1_RAT
Method Type	Sandwich
Platform	PF00168
Protein Name	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Sensitivity	0.169ng/mL
Sequence	50: MAGVGTPCAN ; GCGPSAPSEA ; EVLHLCRSLE ; VGTVMTLFYS ; KKSQRPERKT ; 100: FQVKLETRQI ; TWSRGADKIE ; GSIDIREIKE ; IRPGKTSRDF ; DRYQEDPAFR ; 150: PDQSHCFVIL ; YGMEFRLKTL ; SLQATSEDEV ; NMWIKGLTWL ; MEDTLQAATP ; 200: LQIERWLRKQ ; FYSVDRNRED ; RISAKDLKNM ; LSQVNYRVPN ; MRFLRERLTD ; 250: FEQRSGDITY ; GQFAQLYRSL ; MYSAQKTMDL ; PFLETNTLRT ; GERPELCQVS ; 300: LSEFQQFLLE ; YQGELWAVDR ; LQVQEFMLSF ; LRDPLREIEE ; PYFFLDELVT ; 350: FLFSKENSVW ; NSQLDAVCPE ; TMNNPLSHYW ; ISSSHNTYLT ; GDQFSSESSL ; 400: EAYARCLRMG ; CRCIELDCWD ; GPDGMPVIYH ; GHTLTTKIKF ; SDVLHTIKEH ; 450: AFVASEYPVI ; LSIEDHCSIA ; QQRNMAQHFR ; KVLGDTLLTK ; PVDIAADGLP ; 500: SPNQLKRKIL ; IKHKKLAEGS ; AYEEVPTSVM ; YSENDISNSI ; KNGILYLEDP ; 550: VNHEWYPHYF ; VLTSSKIYYS ; EETSSDQGNE ; DEEEPKEASG ; STELHSSEKW ; 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 ; VEKQDGGWWR ; GDYGGKKQLW ; FPSNYVEEMI ; 900: NPAILEPERE ; HLDENSPLGD ; LLRGVLDVPA ; CQIAIRPEGK ; NNRLFVFSIS ; 950: MPSVAQWSLD ; VAADSQEELQ ; DWVKKIREVA ; QTADARLTEG ; KMMERRKKIA ; 1000: LELSELVVYC ; RPVPFDEEKI ; GTERACYRDM ; SSFPETKAEK ; YVNKAKGKKF ; 1050: LQYNRLQLSR ; IYPKGQRLDS ; SNYDPLPMWI ; CGSQLVALNF ; QTPDKPMQMN ; 1100: QALFMAGGHC ; GYVLQPSTMR ; DEAFDPFDKS ; SLRGLEPCVI ; CIEVLGARHL ; 1150: PKNGRGIVCP ; FVEIEVAGAE ; YDSTKQKTEF ; VVDNGLNPVW ; PAKPFHFQIS ; 1200: NPEFAFLRFV ; VYEEDMFSDQ ; NFLAQATFPV ; KGLKTGYRAV ; PLKNNYSEDL ; 1250: ELASLLIKID ; IFPAKENGDL ; SPFSGTSLRE ; RASDASSQLF ; HVRAREGSFE ; 1290: ARYQQPFEDF ; RISQEHLADH ; FDSRERRAPR ; RTRVNGDNRL ;
Sequence Length	1290
String	P10686
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. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with RET (By similarity). Interacts with AXL and KIT.

Uniprot	P10686
Gene Name	Plcg1
Immunogen Species	Rattus norvegicus (Rat)
Kegg	rno:25738
Unigene	Rn.11243

Reference	1. "Inositol phospholipid-specific phospholipase C: complete cDNA and protein sequences and sequence homology to tyrosine kinase-related oncogene products." Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G. Proc. Natl. Acad. Sci. U.S.A.85:5419-5423(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] 2. "Promoter region of the rat phospholipase C-gamma 1 gene." Lee S.J., Ryu S.H., Suh P.G. Biochem. Biophys. Res. Commun.194:294-300(1993) [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 [GENOMIC DNA] OF 1-29 3. "Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1." Vainikka S., Joukov V., Wennstrom S., Bergman M., Pelicci P.G., Alitalo K. J. Biol. Chem.269:18320-18326(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: INTERACTION WITH FGFR4;PHOSPHORYLATION 4. "Phospholipase C gamma 1 is a physiological guanine nucleotide exchange factor for the nuclear GTPase PIKE." Ye K., Aghdasi B., Luo H.R., Moriarity J.L., Wu F.Y., Hong J.J., Hurt K.J., Bae S.S., Suh P.-G., Snyder S.H. Nature415:541-544(2002) [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 AGAP2;MUTAGENESIS OF PRO-842 5. "Structural characterization of the split pleckstrin homology domain in phospholipase C-gamma1 and its interaction with TRPC3." Wen W., Yan J., Zhang M. J. Biol. Chem.281:12060-12068(2006) [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 489-553 AND 663-759

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