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Syk-induced signals in bone marrow stromal cell lines are mediated by phospholipase C gamma1 (PLCgamma1) in osteogenesis and PLCgamma2 in adipogenesis.
Results show that mice with the mutated Plcg2 gene were less prone to transformation into MALT lymphomas as a result of elevated Treg numbers, and decrease of pro-inflammatory cytokines.
PLCgamma2 in clear cells plays an essential role in luminal expansion of the epididymis during the prepubertal period in mice
platelet activation through GPVI and alphaIIbbeta3 utilizes PLCgamma2 because PLCgamma1 levels are insufficient to support responsiveness, but that PLCgamma1 can restore responsiveness if expressed at levels normally achieved by PLCgamma2.
amarogentin prevents platelet activation through the inhibition of PLC gamma2-PKC cascade and MAPK pathway
PLCgamma2 and protein kinase C are important upstream signals that regulate myelopoiesis through cytokines.
inflammatory osteolysis can be abrogated by treatment with a molecule composed of the tandem SH2 domains of PLCgamma2.
down-regulation of PLCgamma2-beta-catenin pathway occurs in mice and humans and leads to myeloid-derived suppressor cells-mediated tumor expansion.
a novel role of the PLCgamma2-IP(3)-Ca(2+) cascade in the LPS-induced innate immune response pathway where release of intracellular Ca(2+) mediates TLR4 trafficking and subsequent activation of IRF3.
VapB positively regulates RANKL-mediated osteoclastogenesis via PLCgamma2-Ca(2+)-NFAT signaling
PLCgamma2 deficiency impairs Dectin-2-induced NF-kappaB and MAPK activation in response to fungal infection
These results suggest that the Plcg2-mediated pathways play a crucial role in various metabolic and sperm functions, in addition to initiating and maintaining the immune system.
Data indicate a role for PLCgamma2 and Ca(2+) signaling through the modulation of MEK/ERK in IL3/GM-csf stimulated mouse hematopoietic stem/progenitor cells.
Phosphatidylinositol-specific phospholipase C (PLC)-gamma was identified as a partner of the Spry1 and Spry2 proteins.
results demonstrate that the enzymatic activity of PLCgamma2 is tightly regulated to ensure efficient but limited platelet activation at sites of vascular injury
over expression of SH3BP2 in RAW 264.7 cells potentiates sRANKL-stimulated phosphorylation of PLCgamma1 and PLCgamma2.
Integrin alphaIIbbeta3 signaling via Src family kinases and Syk kinase to PLCgamma2 is required for megakaryocyte spreading, migration, and platelet formation.
study demonstrates a critical role for PLCgamma2 in eliciting inflammatory responses by regulating actin dynamics in DCs and positions the PLCgamma2 pathway as a common orchestrator of bone and immune cell functions during arthritis
PLCgamma2 is a critical regulator of the cellular and molecular mechanisms occurring in bone and immune cells during autoimmune inflammation.
The signaling pathway downstream of Syk divides into PLC2- and PI3K-dependent pathways. The activation of these pathways is controlled by the Tec family kinase Btk, which is required for E-selectin-mediated slow rolling.
While BTK/PLCG2 mutations have characteristics suggesting that they can drive ibrutinib resistance, this conclusion remains formally unproven until specific inhibition of such mutations is shown to cause regression of ibrutinib-resistant chronic lymphocytic leukemia . Data suggest that alternative mechanisms of resistance do exist in some patients.
finding that mutations or polymorphisms in two putative calcium-regulated domains of PLCG2 are associated with ibrutinib-resistant CLL adds to the evidence supporting complex regulatory shifts in the PLCG2 protein likely occurring during the development of resistance
The results suggest a new mechanism of PLCgamma activation with unique thermodynamic features and assign a novel regulatory role to its spPH domain.
Data show that protein-altering changes are in PLCG2, ABI3, and TREM2 genes highly expressed in microglia and highlight an immune-related protein-protein interaction network in Alzheimer's disease.
Ocular manifestations of phospholipase-Cgamma2-associated antibody deficiency and immune dysregulation show mutations in the PLC[gamma]2 gene leading to aberrant function of immune cells and overproduction of interleukin-1 [beta] (IL-1[beta]).
R665W and L845F be referred to as allomorphic rather than hypermorphic mutations of PLCG2 Rerouting of the transmembrane signals emanating from BCR and converging on PLCgamma2 through Rac in ibrutinib-resistant CLL cells may provide novel drug treatment strategies to overcome ibrutinib resistance mediated by PLCG2 mutations or to prevent its development in ibrutinib-treated CLL patients.
Data show that phospholipase Cgamma2 (PLCgamma2) is strongly expressed in B cell non-Hodgkin lymphoma and especially in a large subset of Diffuse large B-cell lymphoma (DLBCL).
Characterization of the effect of missense point-mutation at R665W in PLCG2 on signaling mechanisms of ibrutinib resistance in chronic lymphocytic leukemia cells.
PLCG2 missense mutation is a risk factor in the development of steroid sensitive nephrotic syndrome in childhood.
The autoinhibitory C-terminal SH2 domain of phospholipase C-gamma2 stabilizes B cell receptor signalosome assembly.
The relationship between upstream tyrosine kinase SYK and its target, PLCgamma2, is maximally predictive and sufficient to distinguish chronic lymphocytic leukemia from healthy controls.
Single-nucleotide polymorphisms in PLCG2 gene is associated with breast cancer risk after menopausal hormone replacement therapy.
identified three distinct mutations in PLCgamma2 in two patients resistant to ibrutinib
early Ca(2+) fluxing provides feed-forward signal amplification by promoting anchoring of the PLCgamma2 C2 domain to phospho-SLP65.
BANK1 and BLK have roles in B-cell signaling through phospholipase C gamma 2
Associations between treatment response and Lyn, Syk, PLCgamma2 and ERK were not found.
Overexpression of the altered p.Ser707Tyr protein and ex vivo experiments using affected individuals' leukocytes showed clearly enhanced PLCgamma2 activity.
The protein encoded by this gene is a transmembrane signaling enzyme that catalyzes the conversion of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to 1D-myo-inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG), using calcium as a cofactor. IP3 and DAG are second messenger molecules important for transmitting signals from growth factor receptors and immune system receptors across the cell membrane.
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
, 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
, phosphoinositide phospholipase C-gamma-2
, phospholipase C-gamma-2
, phosphoinositide phospholipase C
, phospholipase C-IV
, phosphatidylinositol-specific phospholipase C