phospholipase c

PLA2R1 Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus.

Phospholipase C Protein, Clostridium perfringens, Recombinant (His) is expressed in E. coli.

Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Beta-hemolysin is a phospholipase C with specific activity toward sphingomyelins. Has a high specificity for sphingomyelin, hydrolyzes lysophosphatidylcholine at a much lower rate, but has no activity towards phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine. Phospholipase C Protein, S. aureus, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 35.7 kDa and the accession number is P09978.

PLA2R1 Protein, Human, Recombinant (His) is expressed in E. coli.

Hydrolyzes sphingomyelin in addition to phosphatidylcholine. PLC-H Protein, Pseudomonas aeruginosa, Recombinant (His & Myc & SUMO) is expressed in E. coli expression system with N-10xHis-SUMO and C-Myc tag. The predicted molecular weight is 64.3 kDa and the accession number is P06200.

Phospholipase D4 (PLD4) is a newly identified protein expressed in microglia. the expression of PLD4 was located in macrophages in the colon cancer mesenchymal and lymph nodes as shown by immunohistochemical analysis. furthermore, its expression was associated with clinical staging of colon cancer. Then, THP-1 as a cell model induced into TAMs. PLD4 could be involved in the activation process of M1 phenotype macrophages. PLD4 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 51 kDa and the accession number is Q8BG07-1.

The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol. CHRM2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 23.4 kDa and the accession number is P08172.

Major envelope protein that plays a role in the biogenesis of the viral double membrane and in egress of virus from the host cell. Produces the wrapped form of virus that is required for cell-to-cell spread. Acts as a lipase with broad specificity including phospholipase C, phospholipase A, and triacylglycerol lipase activities. Vaccinia virus (strain Western Reserve) OPG057 Protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 49.2 kDa and the accession number is P04021.

Receptor for extracellular adenine nucleotides such as ADP. In platelets, binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and ultimately platelet aggregation. P2Y1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with C-6xHis tag. The predicted molecular weight is 12.4 kDa and the accession number is P47900.

May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids. Since the purified porcine enzyme has very little activity towards hydrogen peroxide or organic hydroperoxides the protective effect is not likely to be exerted by its enzymatic activity. Instead, may protect sperm from premature acrosome reaction in the epididymis by binding to lipid peroxides, which might otherwise interact with phospholipase A2 and induce the acrosome reaction. GPX5 Protein, Pig, Recombinant (E. coli, His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 27.6 kDa and the accession number is O18994.

Parathyroid hormone / parathyroid hormone-related peptide receptor, also known as PTH / PTHrP type I receptor, PTH/PTHr receptor, Parathyroid hormone 1 receptor, PTH1 receptor, PTH1R and PTHR, is a multi-pass membrane protein which belongs to the G-protein coupled receptor 2 family. PTH1R is expressed in most tissues. It is most abundant in kidney, bone and liver. PTH1R is expressed in high levels in bone and kidney and regulates calcium ion homeostasis through activation of adenylate cyclase and phospholipase C. In bone, PTH1R is expressed on the surface of osteoblasts. When the receptor is activated, these cells in turn stimulate osteoclasts to ultimately increase the resorption rate. PTH1R is a receptor for parathyroid hormone and for parathyroid hormone-related peptide. The activity of PTH1R is mediated by G proteins which activate adenylyl cyclase and also a phosphatidylinositol-calcium second messenger system. Defects in PTH1R are the cause of Jansen metaphyseal chondrodysplasia (JMC), chondrodysplasia Blomstrand type (BOCD), enchondromatosis multiple (ENCHOM), Eiken skeletal dysplasia (EISD) and primary failure of tooth eruption (PFE).

DEP1 / PTPRJ (Receptor-type tyrosine-protein phosphatase eta) is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. DEP1 / PTPRJ possesses an extracellular region containing five fibronectin type III repeats, a single transmembrane region, and a single intracytoplasmic catalytic domain, and thus represents a receptor-type PTP. DEP1 / PTPRJ is present in all hematopoietic lineages, and was shown to negatively regulate T cell receptor signaling possibly through interfering with the phosphorylation of Phospholipase C Gamma 1 and Linker for Activation of T Cells. This protein can also dephosphorylate the PDGF beta receptor, and may be involved in UV-induced signal transduction. In stable MCF-7 cell lines, induction of DEP-1 expression inhibited breast cancer cell growth by 5-10-fold. These data describe PTPs expressed and regulated in breast cancer cell lines during differentiation and identify one PTP, DEP-1, that inhibits the growth of breast cancer cells in vitro.

Phospholipase D4 (PLD4) is a newly identified protein expressed in microglia. the expression of PLD4 was located in macrophages in the colon cancer mesenchymal and lymph nodes as shown by immunohistochemical analysis. furthermore, its expression was associated with clinical staging of colon cancer. Then, THP-1 as a cell model induced into TAMs. PLD4 could be involved in the activation process of M1 phenotype macrophages. PLD4 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 51.1 kDa and the accession number is Q96BZ4.

Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors in the nucleus. Plays a role in adipose tissue and glucose Homeostasis in a sex-specific manner. Contributes to pulmonary vascular remodeling by accelerating proliferation of pulmonary arterial smooth muscle cells.; In the mitochondria, together with PHB2, forms large ring complexes (prohibitin complexes) in the inner mitochondrial membrane (IMM) and functions as chaperone protein that stabilizes mitochondrial respiratory enzymes and maintains mitochondrial integrity in the IMM, which is required for mitochondrial morphogenesis, neuronal survival, and normal lifespan (Probable). The prohibitin complex, with DNAJC19, regulates cardiolipin remodeling and the protein turnover of OMA1 in a cardiolipin-binding manner. Regulates mitochondrial respiration activity playing a role in cellular aging. The prohibitin complex plays a role of mitophagy receptor involved in targeting mitochondria for autophagic degradation. Involved in mitochondrial-mediated antiviral innate immunity, activates DDX58/RIG-I-mediated signal transduction and production of IFNB1 and proinflammatory cytokine IL6.; In the nucleus, acts as a transcription coregulator, enhances promoter binding by TP53, a transcription factor it activates, but reduces the promoter binding by E2F1, a transcription factor it represses. Interacts with STAT3 to affect IL17 secretion in T-helper Th17 cells.; In the plasma membrane, cooperates with CD86 to mediate CD86-signaling in B lymphocytes that regulates the level of IgG1 produced through the activation of distal signaling intermediates. Upon CD40 engagement, required to activate NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation.; (Microbial infection) In neuronal cells, cell surface-expressed PHB is involved in human enterovirus 71/EV-71 entry into neuronal cells specifically, while membrane-bound mitochondrial PHB associates with the virus replication complex and facilitates viral replication. May serve as a receptor for EV71.

May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids. Since the purified porcine enzyme has very little activity towards hydrogen peroxide or organic hydroperoxides the protective effect is not likely to be exerted by its enzymatic activity. Instead, may protect sperm from premature acrosome reaction in the epididymis by binding to lipid peroxides, which might otherwise interact with phospholipase A2 and induce the acrosome reaction. GPX5 Protein, Pig, Recombinant (His & Myc) is expressed in yeast with N-6xHis and C-Myc tag. The predicted molecular weight is 26.1 kDa and the accession number is O18994.

Serine/threonine-protein kinase D3, also known as Protein kinase C nu type, Protein kinase EPK2, PRKD3, EPK2 and PRKCN, is a cytoplasm and membrane protein that belongs to the protein kinase superfamily, CAMK Ser/Thr protein kinase family and PKD subfamily. PRKD3 / PRKCN contains one PH domain, two phorbol-ester/DAG-type zinc fingers and one protein kinase domain. Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. They also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role. PRKD3 / PRKCN converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in resistance to oxidative stress. PRKD3 / PRKCN is activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains 1 and 2 bind both DAG and phorbol ester with high affinity and mediate translocation to the cell membrane. Autophosphorylation of Ser-735 and phosphorylation of Ser-731 by PKC relieves auto-inhibition by the PH domain. PRKD3 / PRKCN can be activated rapidly by the agonists of G protein-coupled receptors. It resides in both cytoplasm and nucleus, and its nuclear accumulation is found to be dramatically enhanced in response to its activation. PRKD3 / PRKCN can also be activated after B-cell antigen receptor (BCR) engagement, which requires intact phospholipase C gamma and the involvement of other PKC family members.