CNR1 Protein, Rat (Cell-Free, His)

The CNR1 protein is a G-protein-coupled receptor for cannabinoids, including cannabinoids and endocannabinoids such as 2-AG, which mediates diverse effects on food intake, memory, and pain. It regulates mitochondrial respiration and inhibits leptin-induced ROS formation. CNR1 Protein, Rat (Cell-Free, His) is the recombinant rat-derived CNR1 protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of CNR1 Protein, Rat (Cell-Free, His) is 473 a.a., with molecular weight of 58.9 kDa.

The CNR1 protein functions as a G-protein coupled receptor for cannabinoids, including endocannabinoids such as N-arachidonoylethanolamide (anandamide or AEA) and 2-arachidonoylglycerol (2-AG). Mediating various cannabinoid-induced effects, it plays a role in processes such as food intake, memory, gastrointestinal motility, catalepsy, ambulatory activity, anxiety, and chronic pain. Signaling typically involves a reduction in cyclic AMP. In the hypothalamus, CNR1 exhibits a dual effect on mitochondrial respiration, increasing respiration at low doses and decreasing it at high doses. High-dose signaling involves G-protein alpha-i protein activation, subsequent inhibition of mitochondrial soluble adenylate cyclase, a decrease in cyclic AMP concentration, and inhibition of protein kinase A (PKA)-dependent phosphorylation of specific subunits of the mitochondrial electron transport system. In the hypothalamus, it inhibits leptin-induced reactive oxygen species (ROS) formation and mediates cannabinoid-induced increases in SREBF1 and FASN gene expression. In response to cannabinoids, CNR1 drives the release of orexigenic beta-endorphin, promoting food intake. In the hippocampus, it regulates cellular respiration and energy production in response to cannabinoids. Additionally, CNR1 is involved in cannabinoid-dependent processes such as depolarization-induced suppression of inhibition, reduction of excitatory synaptic transmission, inhibition of voltage-gated Ca(2+) channels, induction of leptin production in adipocytes, and reduction of LRP2-mediated leptin clearance in the kidney. In adipose tissue and the liver, CNR1 signaling leads to increased expression of various genes related to lipogenesis and metabolism. Furthermore, CNR1 may modulate energy metabolism and affect inflammation, contributing to processes such as obesity and type-2 diabetes. Notably, hemopressin, a peptide derived from hemoglobin subunit alpha, acts as an antagonist peptide, efficiently blocking CNR1 and subsequent signaling.

Rat

E. coli Cell-free

N-10*His

P20272 (M1-L473)

25248

MKSILDGLADTTFRTITTDLLYVGSNDIQYEDIKGDMASKLGYFPQKFPLTSFRGSPFQEKMTAGDNSPLVPAGDTTNITEFYNKSLSSFKENEENIQCGENFMDMECFMILNPSQQLAIAVLSLTLGTFTVLENLLVLCVILHSRSLRCRPSYHFIGSLAVADLLGSVIFVYSFVDFHVFHRKDSPNVFLFKLGGVTASFTASVGSLFLTAIDRYISIHRPLAYKRIVTRPKAVVAFCLMWTIAIVIAVLPLLGWNCKKLQSVCSDIFPLIDETYLMFWIGVTSVLLLFIVYAYMYILWKAHSHAVRMIQRGTQKSIIIHTSEDGKVQVTRPDQARMDIRLAKTLVLILVVLIICWGPLLAIMVYDVFGKMNKLIKTVFAFCSMLCLLNSTVNPIIYALRSKDLRHAFRSMFPSCEGTAQPLDNSMGDSDCLHKHANNTASMHRAAESCIKSTVKIAKVTMSVSTDTSAEAL

58.9 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.