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sPLA2 (show PLA2G2A Proteins)-IB was correlated with the level of proteinuria in membranous nephropathy patients suggesting to be a potential biomarker for monitoring disease severity and therapeutic effects of both primary membranous nephropathy and secondary membranous nephropathy.
The sPLA2 (show PLA2G2A Proteins) IB-PLA2R (show PLA2R1 Proteins) interaction stimulated podocyte apoptosis through activating ERK1/2 and cPLA2alpha (show PLA2G4A Proteins) and through increasing the podocyte AA content
TNF-alpha (show TNF Proteins)-induced cPLA2 (show PLA2G4A Proteins) expression and PGE2 release were mediated through a Jak2 (show JAK2 Proteins)/PDGFR (show PDGFRB Proteins)/PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins)/p42/p44 (show PSMC6 Proteins) MAPK (show MAPK3 Proteins)/Elk-1 (show ELK1 Proteins) pathway in human lung epithelial cells.
stimulation of three isoforms of PLA2 by thapsigargin liberates free AA that, in turn, induces capacitative calcium influx in human T-cells
results indicate a selective sorting of a cell-derived cPLA2 (show PLA2G4A Proteins) during human cytomegalovirus maturation, which is further required for infectivity
Group IB phospholipase A2 (PLA2G1B) stimulates leukotriene B4 (LTB4 (show PTGR1 Proteins)) production in the absence of cytochalasin B in human neutrophils.
Here, we report sPLA2 (show PLA2G2A Proteins)-IB in rat and human brain as well as in neurons in primary culture. The distribution of sPLA2 (show PLA2G2A Proteins)-IB seems to be mainly neuronal, with the highest abundance occurring in the cerebral cortex and hippocampus.
a critical regulatory role of arachidonate reacylation that limits leukotriene biosynthesis in concert with 5-lipoxygenase (show ALOX5 Proteins) and cytosolic phospholipase A (show HRASLS Proteins)(2)alpha activation
Results describe the structural basis for bile salt inhibition of pancreatic phospholipase A2.
MMP-2 (show MMP2 Proteins)/9 production is regulated by sPLA2 (show PLA2G2A Proteins)-IB acting as a receptor ligand to activate cPLA2 (show PLA2G4A Proteins)
Equilibrium unfolding of porcine pancreatic phospholipase A2 was monitored using multiple approaches. An unusually broad unfolding transition at remarkably high denaturant concentration was observed.
Porcine group IB secretory phospholipase A2 (PLA2G1B) stimulates the expression and secretion of CXC chemokine (show CXCL12 Proteins) ligand 8 (show CCL8 Proteins) (CXCL8 (show IL8 Proteins)) in human neutrophils without affecting other proinflammatory cytokines.
Porcine pancreatic PLA(2) shows a long lag (show STMN1 Proteins) phase of several hours during which the enzyme binds to the bilayer surface, but only 5+/-3% of the lipids react before the onset of rapid hydrolysis.
Results show that the decylsulfate epitope for the successive E i (#) complexes increasingly resembles the micellar complex formed by the binding of PLA2 to preformed micelles.
An increased sPLA(2 (show PLA2G2A Proteins)) activity and a reduced inhibition may play an important role in the pathogenesis of ischemia-reperfusion injury of non-heart-beating donor liver grafts.
Interfacial activation of pig pancreatic IB phospholipase A (show HRASLS Proteins)(2) (PLA2) is modeled in terms of the three discrete premicellar complexes (E(i)(#), i = 1, 2, or 3) consecutively formed by the cooperative binding of a monodisperse amphiphile to the i-face
Phospholipase A2 isoforms are differentially regulated; they selectively participate in retinal signaling in an experimental model of age-related macular degeneration.
results suggest the hydrophobic surfactant protein, SP-B, protects alveolar surfactant phospholiopids from hydrolysis mediated by multiple sPLA(2 (show PLA2G2A Proteins)) in both vesicles (alveolar subphase) and monomolecular films (air-liquid interface)
crystal structure of the triple mutant pancreatic phospholipase A2 with calcium.
NMR characterization of a unique low-barrier hydrogen bond between an active site residue from the enzyme and a bound inhibitor: the complex between secreted phospholipase A (show HRASLS Proteins)(2) (sPLA(2 (show PLA2G2A Proteins)), from bovine pancreas) and a transition-state analog inhibitor HK32
The final protein model consists of 123 amino-acid residues, two calcium ions, one chloride ion, 243 water molecules and six 2 (show SIX2 Proteins)-methyl-2,4-pentanediol molecules.
The crystal structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 complexed with an organic molecule, p-methoxybenzoic acid (anisic acid), is reported.
The quadruple mutant of phospholipase A2 has monoclinic or trigonal crystal structures and results suggested evidence for the involvement of the second calcium and surface loop in interfacial binding.
Pla2g1b inactivation suppressed diet-induced body weight gain and reduced diabetes and atherosclerosis in LDL receptor (show LDLR Proteins)-deficient mice.
inhibition of Pla2g1b protects against diet-induced hyperlipidemia
Lysophospholipids produced by Pla2g1b hydrolysis suppress hepatic fat utilization and down-regulate energy expenditure, preventing metabolically beneficial adaptation to a high-fat diet exposure in promoting diet-induced obesity and type 2 diabetes.
sPLA2IB has a role in promoting MMP-2 (show MMP2 Proteins) mediated cell migration via the phosphatidylinositol 3-kinase and Akt (show AKT1 Proteins) pathway
Elevating plasma lysophospholipid levels in Pla2g1b deficient mice via intraperitoneal injection resulted in glucose intolerance.
pro-inflammatory effects of Ps. aeruginosa involve release of an sPLA2 of epithelial origin that, in part, via distinct signalling molecules, transactivates the ABCA1 gene, leading to export of phospholipid.
The results indicate that PLA2 activity in equine endometrium changes with the stage of the oestrous cycle and thus may be influenced by systemic hormone concentrations.
During pregnancy, PLA2 expression may be sufficient to initiate the cascade for prostaglandin f2alpha secretion and does not play a direct role in maternal recognition of pregnancy.
Phospholipase A2 (EC 18.104.22.168) catalyzes the release of fatty acids from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals. Sequences of pancreatic PLA2 enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Other forms of PLA2 have been isolated from brain, liver, lung, spleen, intestine, macrophages, leukocytes, erythrocytes, inflammatory exudates, chondrocytes, and platelets (Seilhamer et al., 1986
, phospholipase A2
, allergen Api m 1
, allergen Api m I
, phosphatidylcholine 2-acylhydrolase
, phosphatidylcholine 2-acylhydrolase 1B
, group IB phospholipase A2
, group IB secretory phospholipase A(2)
, phospholipase A2, major isoenzyme
, Group IB phospholipase A2
, Phosphatidylcholine 2-acylhydrolase 1B
, phospholipase A2, group IB, pancreas
, phospholipase A2 group IB
, phospholipase A2, group 1B
, cytosolic phospholipase A2
, phospholipase A2 group IVA
, phospholipase A2, group IB (pancreas)