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Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes (By similarity).. Additionally we are shipping LANCL2 Proteins (4) and many more products for this protein.
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The predicted impairment of regulatory macrophage differentiation by the loss of LANCL2 was simulated based on multiscale linkages between the tissue-level gastric mucosa and the intracellular models. The simulated deletion of LANCL2 resulted in a greater clearance of H. pylori, but also greater IFNgamma responses and damage to the epithelium.
Data show that LANCL2 silencing resulted in a 70% inhibition of the plasma membrane lipid peroxidation induced by abscisic acid (ABA).
Data indicate that lanthionine synthetase C-like 2 (LanCL2) depletion sensitizes cells to apoptosis through down-regulating serine/threonine protein kinase (show PRKACG Antibodies) Akt (show AKT1 Antibodies) phosphorylation.
human recombinant LANCL2 binds abscisic acid (ABA) directly and provide the first demonstration of ABA binding to a mammalian ABA receptor.
Molecular docking studies predict that ABA and other PPAR gamma (show PPARG Antibodies) agonists (e.g., rosiglitazone and pioglitazone) share a binding site on the surface of LANCL2.
Data show that lanthionine synthetase C-like protein (LANCL2) is required for abscisic acid binding on human granulocyte membranes and that LANCL2 is necessary for transduction of the ABA signal into granulocytes and rat insulinoma (show RPS15 Antibodies) cells.
Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes (By similarity).
lanC-like protein 2
, testis-specific adriamycin sensitivity protein
, G protein-coupled receptor 69B
, LanC (bacterial lantibiotic synthetase component C)-like 2