Anti-OPRM1 antibody (405-455) {Biotin} (STJ501772)

SKU:
STJ501772-100

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Host: Rabbit
Applications: ELISA/IHC/IP/WB
Reactivity: Human/Mouse/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-OPRM1 (405-455) is suitable for use in ELISA, Immunohistochemistry, Immunoprecipitation and Western Blot research applications.
Clonality: Polyclonal
Conjugation: Biotin
Isotype: IgG
Purification: Affinity Purified
Concentration: 0.5 µg/µl
Dilution Range: WB: 1:500
ELISA: 1:10, 000
IP: 1:200
IHC: 1:100
Storage Instruction: Store at-20°C for long term storage. Avoid freeze-thaw cycles.
Gene Symbol: OPRM1
Gene ID: 4988
Uniprot ID: OPRM_HUMAN
Immunogen Region: 405-455
Immunogen: Synthetic peptide taken within amino acid region 405-455 on human Mu-type opiod receptor isoform MOR-1i protein.
Tissue Specificity Expressed in brain. Isoform 16 and isoform 17 are detected in brain.
Post Translational Modifications Phosphorylated. Differentially phosphorylated in basal and agonist-induced conditions. Agonist-mediated phosphorylation modulates receptor internalization. Phosphorylated by GRK2 in a agonist-dependent manner. Phosphorylation at Tyr-168 requires receptor activation, is dependent on non-receptor protein tyrosine kinase Src and results in a decrease in agonist efficacy by reducing G-protein coupling efficiency. Phosphorylated on tyrosine residues.the phosphorylation is involved in agonist-induced G-protein-independent receptor down-regulation. Phosphorylation at Ser-377 is involved in G-protein-dependent but not beta-arrestin-dependent activation of the ERK pathway. Ubiquitinated. A basal ubiquitination seems not to be related to degradation. Ubiquitination is increased upon formation of OPRM1:OPRD1 oligomers leading to proteasomal degradation.the ubiquitination is diminished by RTP4.
Function Receptor for endogenous opioids such as beta-endorphin and endomorphin. Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone. Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe. 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. 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. 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. Also couples to adenylate cyclase stimulatory G alpha proteins. 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. 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. 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. Endogenous ligands induce rapid desensitization, endocytosis and recycling. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties. Isoform 12: Couples to GNAS and is proposed to be involved in excitatory effects. Isoform 16: Does not bind agonists but may act through oligomerization with binding-competent OPRM1 isoforms and reduce their ligand binding activity. Isoform 17: Does not bind agonists but may act through oligomerization with binding-competent OPRM1 isoforms and reduce their ligand binding activity.
Protein Name Mu-Type Opioid Receptor
M-Or-1
Mor-1
Mu Opiate Receptor
Mu Opioid Receptor
Mop
Hmop
Database Links Reactome: R-HSA-111885
Reactome: R-HSA-202040
Reactome: R-HSA-375276
Reactome: R-HSA-418594
Reactome: R-HSA-6785807
Reactome: R-HSA-9022699
Cellular Localisation Cell Membrane
Multi-Pass Membrane Protein
Cell Projection
Axon
Perikaryon
Dendrite
Endosome
Is Rapidly Internalized After Agonist Binding
Isoform 12: Cytoplasm
Alternative Antibody Names Anti-Mu-Type Opioid Receptor antibody
Anti-M-Or-1 antibody
Anti-Mor-1 antibody
Anti-Mu Opiate Receptor antibody
Anti-Mu Opioid Receptor antibody
Anti-Mop antibody
Anti-Hmop antibody
Anti-OPRM1 antibody
Anti-MOR1 antibody

Information sourced from Uniprot.org

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