Anti-Mu Opioid Receptor antibody [EPR26293-61] (BSA and Azide free)

Target data

Receptor for endogenous opioids such as beta-endorphin and endomorphin (PubMed : 11060299, PubMed : 15944153, PubMed : 16682964, PubMed : 17384143, PubMed : 17947509, PubMed : 1846076, PubMed : 18558479, PubMed : 21292762, PubMed : 7595566, PubMed : 7678862, PubMed : 8051154, PubMed : 8240812, PubMed : 8393525, PubMed : 9224819, PubMed : 9572309). Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone (PubMed : 11060299, PubMed : 15944153, PubMed : 16682964, PubMed : 17384143, PubMed : 17947509, PubMed : 1846076, PubMed : 18558479, PubMed : 21292762, PubMed : 7595566, PubMed : 7678862, PubMed : 8051154, PubMed : 8240812, PubMed : 8393525, PubMed : 9224819, PubMed : 9572309). Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe (PubMed : 8624732). Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors (PubMed : 16682964, PubMed : 9224819). The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extent to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15 (PubMed : 9224819, PubMed : 9572309). They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B (PubMed : 15944153, PubMed : 21292762, PubMed : 7595566, PubMed : 9572309). Also couples to adenylate cyclase stimulatory G alpha proteins (PubMed : 7595566). The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4. Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization (PubMed : 11060299, PubMed : 17384143, PubMed : 17947509, PubMed : 18558479). Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction. The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins. The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation (PubMed : 11278523, PubMed : 11896051, PubMed : 15944153). Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling. Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling (PubMed : 11060299, PubMed : 17384143, PubMed : 17947509, PubMed : 18558479). Endogenous ligands induce rapid desensitization, endocytosis and recycling. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties (PubMed : 16682964, PubMed : 17384143).