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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).. 再加上，我们可以发LANCL2 蛋白 (4)和数多这个蛋白质的别的产品。
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Very similar concentrations of lanthionine ketimine (0.5-2.5 nmol/g tissue) were found in LanCL1 knock-out, LanCL1/LanCL2/LanCL3 triple-knock-out and wild type (WT) mouse brains, suggesting that LanCL proteins are not involved in lanthionine biosynthesis.
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).
Site-directed mutagenesis (single mutant R118I, triple mutants R118I/R22I/K362I and R118I/S41A/E46I) and equilibrium binding experiments on the mutated LANCL2 proteins identified a high-affinity ABA-binding site involving R118, with a KD of 2.6nM+/-1.2nM, as determined by surface plasmon resonance.
human LANCL2 is a non-transmembrane G protein-coupled receptor susceptible to hormone-induced nuclear translocation.
Data indicate that lanthionine synthetase C-like 2 (LanCL2) depletion sensitizes cells to apoptosis through down-regulating serine/threonine protein kinase Akt 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 agonists (e.g., rosiglitazone and pioglitazone) share a binding site on the surface of LANCL2.
cDNA cloned and characterized. May play a role as a component of a peptide-modifying complex
Lanthionine synthetase components C-like 2 increases cellular sensitivity to adriamycin by decreasing the expression of P-glycoprotein through a transcription-mediated mechanism.
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 cells.
Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
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