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生化/生理作用
PalGly is an endogenous signaling lipid that modulates calcium influx and nitric oxide production.
PalGly is an endogenous signaling lipid that modulates calcium influx and nitric oxide production. PalGly inhibits heat-evoked firing of wide dynamic range (WDR) neurons, activates calcium influx in DRG cells and stimulates NO production. Preliminary studies suggest its signaling mechanism involves GPCR-mediated cation channel activation and a Gαi/o-coupled signaling pathway, which is being further investigated.
特点和优势
This compound is featured on the Nitric Oxide Synthases page of the Handbook of Receptor Classification and Signal Transduction. To browse other handbook pages, click here.
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Krishna Pratap Ravindranathan et al.
Journal of the American Chemical Society, 128(17), 5786-5791 (2006-04-28)
UV-vis absorbance measurements and associated studies of cytochrome P450 BM-3 in complex with N-palmitoylglycine (NPG) indicate that a conformational change occurs in the active site of the complex where the terminal atoms of the ligand move from a site distant
Heather B Bradshaw et al.
Life sciences, 92(8-9), 404-409 (2012-11-28)
Transient receptor potential channels (TRPs) form a large family of ubiquitous non-selective cation channels that function as cellular sensors and in many cases regulate intracellular calcium. Identification of the endogenous ligands that activate these TRP receptors is still under intense
Heather B Bradshaw et al.
Prostaglandins & other lipid mediators, 89(3-4), 131-134 (2009-04-22)
A large and growing family of over 70 endogenous lipids of the basic structure N-acyl amide has been identified during the last 10 years. Only a few of these lipids have been characterized for biological activity, however, those that have
D C Haines et al.
Biochemistry, 40(45), 13456-13465 (2001-11-07)
Cytochrome P450s constitute a superfamily of enzymes that catalyze the oxidation of a vast number of structurally and chemically diverse hydrophobic substrates. Herein, we describe the crystal structure of a complex between the bacterial P450BM-3 and the novel substrate N-palmitoylglycine
Conformational dynamics of substrate in the active site of cytochrome P450 BM-3/NPG complex: insights from NMR order parameters.
Krishna Pratap Ravindranathan et al.
Journal of the American Chemical Society, 129(3), 474-475 (2007-01-18)
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