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Syk (show SYK Proteins)-induced signals in bone marrow stromal cell lines are mediated by phospholipase C (show PLC Proteins) gamma1 (PLCgamma1) in osteogenesis and PLCgamma2 (show PLCG2 Proteins) in adipogenesis.
PLCG1, along with ITGA4 (show ITGA4 Proteins) are regulated by miR (show MLXIP Proteins)-30b in clinical samples of coronary artery cells from coronary atherosclerosis patients.
the central biological role of the novel IL-2 (show IL2 Proteins)-R/Lck (show LCK Proteins)/PLCgamma/PKCtheta (show PRKCQ Proteins);/alphaPIX (show ARHGEF6 Proteins)/Rac1/PYGM (show PYGM Proteins) signalling pathway is directly related to the control of fundamental cellular processes such as T cell migration and proliferation.
LAT and phospholipase C-gamma dephosphorylation by SHP-1 inhibits natural killer cell cytototoxicity
Dysregulation of primary PLC (show HSPG2 Proteins) signaling is linked to several brain disorders including epilepsy, schizophrenia, bipolar disorder, Huntington's disease, depression and Alzheimer's disease. (Review)
The products of PLC (show HSPG2 Proteins)-gamma activity mediate the innate immune response by regulating respiratory burst, phagocytosis, cell adhesion, and cell migration. (Review)
1,25(OH)2D3 indirectly modulates the differentiation of Treg/Th17 cells by a ff ;ecting the VDR (show CYP27B1 Proteins)/PLC-gamma1/TGF-beta1pathway. These results indicate that administration 1,25(OH)2D3 supplements may be a beneficial treatment for organ transplantation recipients.
These results suggest that immobilized EGF (show EGF Proteins) increases collective keratinocyte displacement via an increase in single-cell migration persistence resulting from altered EGFR (show EGFR Proteins) trafficking and PLCgamma1 activation.
High PLC (show HSPG2 Proteins) gamma expression is associated with breast cancer.
We show that the decrease in PI(4,5)P2 level under non-stimulated conditions inhibits PTEN activity leading to the aberrant activation of the oncoprotein Akt (show AKT1 Proteins). As well as defining a novel mechanism of Akt (show AKT1 Proteins) phosphorylation with important therapeutic consequences, we also demonstrate that differential expression levels of FGFR2 (show FGFR2 Proteins), Plc11 and Grb2 (show GRB2 Proteins) correlate with patient survival
Findings provide evidence that PLCgamma1 is critical for synaptic function and plasticity and that the loss of PLCgamma1 from the forebrain results in manic-like behavior.
our studies demonstrate that PLCgamma1 is important for pre-TCR mediated signal transduction and pre-T cell development.
Knock-down of PLC-gamma-1 induced foreign body giant cell formation.PLC-gamma-1-deficiency caused a decrease in RUNX1 (show RUNX1 Proteins) and subsequent PU.1 upregulation while subsequent rescue of RUNX1 (show RUNX1 Proteins) in sh-PLC-gamma-1-transfected cells strongly inhibited foreign body giant cell formation.
study shows that PLCgamma1 controls osteoclast numbers via a CSF-1 (show CSF1 Proteins)-dependent DAG/beta-catenin (show CTNNB1 Proteins)/cyclinD1 pathway.
this study shows that PLC-gamma1 contributes to protective activity of LAT (show LAT Proteins) activity in vivo
PLCgamma1 signaling is involved in the formation of neuronal processes for functionally faithful brain development. [review]
FGFR1 (show FGFR1 Proteins)/2 act in concert to recruit and transphosphorylate phospholipase Cgamma1.
platelet activation through GPVI (show GP6 Proteins) and alphaIIbbeta3 utilizes PLCgamma2 (show PLCG2 Proteins) because PLCgamma1 levels are insufficient to support responsiveness, but that PLCgamma1 can restore responsiveness if expressed at levels normally achieved by PLCgamma2 (show PLCG2 Proteins).
foci are polymerized de novo as a result of the T cell receptor (TCR) proximal tyrosine kinase (show TYRO3 Proteins) cascade, and facilitate distal signaling events including PLCgamma1 activation and subsequent cytoplasmic calcium ion elevation
This study is the first to indicate that PLC gamma 1 is expressed in bovine adrenal chromaffin cells and has the potential to be activated.
Tyrosine775 is identified as a new, functionally important phosphorylation site on PLC gamma 1; phosphorylation of both Y775 and Y783 is required for PLC gamma 1 activation as measured by antigen receptor-induced Ca2 (show CA2 Proteins)+ flux, NF-AT (show NFATC3 Proteins) and AP-1 (show JUN Proteins) activation.
PLC-gamma1 is regulated via a novel autoinhibitory mechanism involving its carboxy-terminal Src (show SRC Proteins) homology (SH2C) domain.
The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of receptor-mediated tyrosine kinase activators. For example, when activated by SRC, the encoded protein causes the Ras guanine nucleotide exchange factor RasGRP1 to translocate to the Golgi, where it activates Ras. Also, this protein has been shown to be a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Two transcript variants encoding different isoforms have been found for this gene.
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
, 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
, Phospholipase C-beta1
, phosphoinositide phospholipase C
, phosphoinositide phospholipase C-beta-1
, phospholipase C-I
, phospholipase C-beta-1
, PLC gamma 1
, phospholipase C-gamma-1b
, phospholipase C, gamma 1
, 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
, 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 1
, 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1
, monophosphatidylinositol phosphodiesterase
, phosphatidylinositol phospholipase C
, phosphoinositidase C
, phosphoinositide phospholipase C-gamma-1
, phospholipase C, gamma 1 (formerly subtype 148)
, phospholipase C-148
, phospholipase C-II
, phospholipase C-gamma-1
, triphosphoinositide phosphodiesterase
, cell differentiation and embryonic development