AFfirm™ PLCG1 Mouse Monoclonal Antibody - #BF8162
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Fold/Unfold
1 phosphatidyl D myo inositol 4 5 bisphosphate; 1 phosphatidylinositol 4 5 bisphosphate phosphodiesterase gamma 1; 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1; Inositoltrisphosphohydrolase; Monophosphatidylinositol phosphodiesterase; NCKAP3; Phosphatidylinositol phospholipase C; Phosphoinositidase C; Phosphoinositide phospholipase C; Phosphoinositide phospholipase C-gamma-1; Phospholipase C 148; Phospholipase C gamma 1; Phospholipase C-gamma-1; Phospholipase C-II; PLC gamma 1; PLC II; PLC-148; PLC-gamma-1; PLC-II; PLC1; PLC148; Plcg1; PLCG1_HUMAN; PLCgamma1;
Immunogens
- P19174 PLCG1_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRAGERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVTFLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQYFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSSSTELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLWFPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSISMASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCAISIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDLELASLLIKIDIFPAKENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFEDFRISQEHLADHFDSRERRAPRRTRVNGDNRL
PTMs - P19174 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
Phosphorylation | Uniprot | ||
A2 | Acetylation | Uniprot | |
S6 | Phosphorylation | Uniprot | |
K54 | Ubiquitination | Uniprot | |
K68 | Ubiquitination | Uniprot | |
Y93 | Phosphorylation | Uniprot | |
K159 | Ubiquitination | Uniprot | |
K175 | Ubiquitination | Uniprot | |
K178 | Ubiquitination | Uniprot | |
Y186 | Phosphorylation | Uniprot | |
Y210 | Phosphorylation | Uniprot | |
S219 | Phosphorylation | Uniprot | |
K226 | Ubiquitination | Uniprot | |
S236 | Phosphorylation | Uniprot | |
T237 | Phosphorylation | Uniprot | |
Y379 | Phosphorylation | Uniprot | |
K389 | Ubiquitination | Uniprot | |
S412 | Phosphorylation | Uniprot | |
Y428 | Phosphorylation | Uniprot | |
K431 | Ubiquitination | Uniprot | |
K440 | Ubiquitination | Uniprot | |
S451 | Phosphorylation | Uniprot | |
K456 | Ubiquitination | Uniprot | |
K465 | Ubiquitination | Uniprot | |
S470 | Phosphorylation | Uniprot | |
Y472 | Phosphorylation | P00533 (EGFR) | Uniprot |
T477 | Phosphorylation | Uniprot | |
Y481 | Phosphorylation | Uniprot | |
Y496 | Phosphorylation | Uniprot | |
Y506 | Phosphorylation | Uniprot | |
Y509 | Phosphorylation | Uniprot | |
Y518 | Phosphorylation | Uniprot | |
S525 | Phosphorylation | Uniprot | |
S539 | Phosphorylation | Uniprot | |
T542 | Phosphorylation | Uniprot | |
K549 | Ubiquitination | Uniprot | |
K554 | Ubiquitination | Uniprot | |
S582 | Phosphorylation | Uniprot | |
K666 | Ubiquitination | Uniprot | |
Y669 | Phosphorylation | Uniprot | |
Y702 | Phosphorylation | Uniprot | |
K763 | Ubiquitination | Uniprot | |
T766 | Phosphorylation | Uniprot | |
Y771 | Phosphorylation | P43405 (SYK) , P00533 (EGFR) , P00519 (ABL1) , P07948 (LYN) | Uniprot |
Y775 | Phosphorylation | Q08881 (ITK) | Uniprot |
Y783 | Phosphorylation | P43403 (ZAP70) , P43405 (SYK) , Q08881 (ITK) , P07949 (RET) , P00533 (EGFR) , P54764 (EPHA4) | Uniprot |
T791 | Phosphorylation | Uniprot | |
K793 | Ubiquitination | Uniprot | |
K803 | Ubiquitination | Uniprot | |
S815 | Phosphorylation | Uniprot | |
K823 | Ubiquitination | Uniprot | |
Y833 | Phosphorylation | Uniprot | |
Y845 | Phosphorylation | Uniprot | |
K890 | Ubiquitination | Uniprot | |
K941 | Ubiquitination | Uniprot | |
S954 | Phosphorylation | Uniprot | |
Y959 | Phosphorylation | Uniprot | |
Y977 | Phosphorylation | Uniprot | |
S981 | Phosphorylation | Uniprot | |
S982 | Phosphorylation | Uniprot | |
Y991 | Phosphorylation | Uniprot | |
Y1003 | Phosphorylation | P00519 (ABL1) | Uniprot |
C1060 | S-Nitrosylation | Uniprot | |
K1079 | Ubiquitination | Uniprot | |
K1193 | Ubiquitination | Uniprot | |
S1221 | Phosphorylation | Uniprot | |
S1224 | Phosphorylation | Uniprot | |
T1226 | Phosphorylation | Uniprot | |
S1227 | Phosphorylation | Uniprot | |
R1231 | Methylation | Uniprot | |
S1233 | Phosphorylation | Uniprot | |
S1236 | Phosphorylation | Uniprot | |
R1243 | Methylation | Uniprot | |
S1248 | Phosphorylation | P17252 (PRKCA) , P17612 (PRKACA) , P31749 (AKT1) , Q15139 (PRKD1) | Uniprot |
S1251 | Phosphorylation | Uniprot | |
Y1253 | Phosphorylation | P43403 (ZAP70) , P00533 (EGFR) | Uniprot |
S1263 | Phosphorylation | Uniprot | |
S1273 | Phosphorylation | Uniprot | |
R1283 | Methylation | Uniprot |
Research Backgrounds
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 PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration.
Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA (By similarity). Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phosphorylated by activated PDGFRB. The receptor-mediated activation of PLCG1 involves its phosphorylation by tyrosine kinases, in response to ligation of a variety of growth factor receptors and immune system receptors. For instance, SYK phosphorylates and activates PLCG1 in response to ligation of the B-cell receptor. May be dephosphorylated by PTPRJ. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells.
Ubiquitinated by CBLB in activated T-cells.
Cell projection>Lamellipodium. Cell projection>Ruffle.
Note: Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment.
Interacts with AGAP2 via its SH3 domain. Interacts (via SH2 domain) with RET. Interacts with FLT1 (tyrosine-phosphorylated) (By similarity). Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). 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 AXL, FLT4 and KIT. Interacts with RALGPS1. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C (By similarity). Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with SYK; activates PLCG1. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes (By similarity). Interacts with TESPA1; the association is increased with prolonged stimulation of the TCR and may facilitate the assembly of the LAT signalosome.
(Microbial infection) Interacts (via SH3 domain) with HEV ORF3 protein.
The SH3 domain mediates interaction with CLNK (By similarity). The SH3 domain also mediates interaction with RALGPS1.
Research Fields
· Environmental Information Processing > Signal transduction > ErbB signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Ras signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Rap1 signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Calcium signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > NF-kappa B signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > HIF-1 signaling pathway. (View pathway)
· Environmental Information Processing > Signal transduction > Phosphatidylinositol signaling system.
· Environmental Information Processing > Signal transduction > Phospholipase D signaling pathway. (View pathway)
· Human Diseases > Drug resistance: Antineoplastic > EGFR tyrosine kinase inhibitor resistance.
· Human Diseases > Infectious diseases: Bacterial > Vibrio cholerae infection.
· Human Diseases > Infectious diseases: Bacterial > Epithelial cell signaling in Helicobacter pylori infection.
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Human Diseases > Cancers: Overview > Pathways in cancer. (View pathway)
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Human Diseases > Cancers: Overview > MicroRNAs in cancer.
· Human Diseases > Cancers: Specific types > Glioma. (View pathway)
· Human Diseases > Cancers: Specific types > Non-small cell lung cancer. (View pathway)
· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma. (View pathway)
· Human Diseases > Cancers: Overview > Choline metabolism in cancer. (View pathway)
· Metabolism > Carbohydrate metabolism > Inositol phosphate metabolism.
· Metabolism > Global and overview maps > Metabolic pathways.
· Organismal Systems > Development > Axon guidance. (View pathway)
· Organismal Systems > Immune system > Natural killer cell mediated cytotoxicity. (View pathway)
· Organismal Systems > Immune system > Th1 and Th2 cell differentiation. (View pathway)
· Organismal Systems > Immune system > Th17 cell differentiation. (View pathway)
· Organismal Systems > Immune system > T cell receptor signaling pathway. (View pathway)
· Organismal Systems > Immune system > Fc epsilon RI signaling pathway. (View pathway)
· Organismal Systems > Immune system > Fc gamma R-mediated phagocytosis. (View pathway)
· Organismal Systems > Immune system > Leukocyte transendothelial migration. (View pathway)
· Organismal Systems > Nervous system > Neurotrophin signaling pathway. (View pathway)
· Organismal Systems > Sensory system > Inflammatory mediator regulation of TRP channels. (View pathway)
· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway. (View pathway)
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