Anti-OPRM1 antibody (354-388) [S4075RM] (STJ11104075)

SPECIFICATIONS
ClonalityMonoclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
STJ11104075
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General Information

Short DescriptionRabbit monoclonal Mu-Type Opioid Receptor (354-388) antibody for use in IHC-P and ELISA in mouse samples. Datasheet included with dilution recommendations, and related reagents.
ApplicationsIHC-P/ELISA
HostRabbit
ReactivityMouse
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ClonalityMonoclonal
Clone IDS4075RM
IsotypeIgG
ConjugationUnconjugated
ConcentrationLot specific
PurificationAffinity purification
Dilution RangeIHC-P:1:50-1:200
ELISA:Recommended starting concentration is 1 Mu g/mL. Please optimize the concentration based on your specific assay requirements.
FormulationPBS with 0.05% Proclin300, 0.05% BSA, 50% Glycerol, pH 7.3.
Storage InstructionStore at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.

Target Information

Gene SymbolOPRM1
Gene ID4988
Uniprot IDOPRM_HUMAN
Immunogen Region354-388
Immunogen SequenceIPTSSNIEQQNSTRIRQNTR DHPSTANTVDRTNHQ
SpecificityRecombinant fusion protein containing a sequence corresponding to amino acids 354-388 of human Mu Opioid Receptor (MOR) (NP_000905.3).

Additional Info

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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