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The PLCdelta1 negatively regulates autophagy, and PLCdelta1 suppression contributes to the tolerance of CRC cells harboring KRAS mutations to nutrient deprivation and anti-cancer drug treatment.
Phospholipase C delta 1 is both a KLF15-regulated gene and a novel repressor of airway smooth muscle hypertrophy.
High PLC (show HSPG2 Proteins) delta expression is associated with breast cancer.
slow phase of Gi/o-mediated TRPC4 (show TRPC4 Proteins) activation was diminished by inhibiting RhoA (show RHOA Proteins) or enhancing PLCdelta function
Neuropeptide Y (show NPY Proteins) decreased PLCD1 expression in HUVECs.
PLC (show HSPG2 Proteins)-delta1 and TRPV6 (show TRPV6 Proteins) are critical actor of Ca(2 (show CA2 Proteins)+) homeostasis in CF human bronchial epithelial cells.
Ectopic expression of PLCD1 inhibits breast tumor cell proliferation in vivo by inducing apoptosis and suppressed tumor cell migration by regulating cytoskeletal reorganization.
Provide evidence for intramolecular interactions in the PLC (show HSPG2 Proteins)-delta1 PH domain.
Genotyping using microsatellite markers linked the families to the gene PLCD1 on chromosome 3p22.2. Sequence analysis of the gene detected one novel (p.Ser740ArgfsX19) and one previously reported mutation (p.Arg437X).
A novel mutation in the PLCD1 gene, which leads to an aberrant splicing event, underlies autosomal recessive leuconychia.
PLCd1 negatively regulates lipopolysaccharide-induced production of IL-1b (show IL1B Proteins) and Fc gamma receptor (show FCGR1A Proteins)-mediated phagocytosis in macrophages.
Data show that phospholipase C delta1 (PLCD1) transfection can induce the apoptosis of CAPAN-1 and BXPC-3 pancreatic cancer cells, arrest the cell cycle in G0 /G1 phase.
the Ca(2+) dependence of the interaction between PRIP-C2 and Syt1-C2A was attributed to Ca(2+) binding with Syt1-C2A, but not PRIP-C2, using a series of mutants prepared from both C2 domains.
Expression of PLCdelta1 is increased in ALS mouse spinal cord and in neurons from ALS mice. Genetic ablation of this protein in ALS mice significantly increases survival
Identification, characterization and regulatory properties of a novel PLCD1 isoform in mouse.
Plcd1 and Plcd3 (show PLCd3 Proteins) have synergistic effects on the murine hair follicle in specific regions of the body surface.
Loss of phospholipase Cdelta1 from keratinocytes causes features of interleukin-17 (show IL17A Proteins)-associated inflammatory skin diseases.
Results suggest that phospholipase C delta(1) is required for skin stem cell lineage commitment.
the PLC (show HSPG2 Proteins)-delta1 promoter is under the control of NF-kappaB (show NFKB1 Proteins), which mediates the expression of PLC (show HSPG2 Proteins)-delta due to Abeta42
Nuclear translocation of phospholipase C-delta1 is linked to the cell cycle and nuclear phosphatidylinositol 4,5-bisphosphate
This gene encodes a member of the phospholipase C family. Phospholipase C isozymes play critical roles in intracellular signal transduction by catalyzing the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers diacylglycerol (DAG) and inositol triphosphate (IP3). The encoded protein functions as a tumor suppressor in several types of cancer, and mutations in this gene are a cause of hereditary leukonychia. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
, 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1
, phosphoinositide phospholipase C-delta-1
, phospholipase C-III
, PLC-delta 1
, phospholipase C delta 1 Lf
, phospholipase C delta-1
, phospholipase C-delta-1
, Phospholipase C-delta1
, phosphoinositide phospholipase C
, phospholipase C delta 1 long form