|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||44494 Da|
|Homology||Mouse - identical; human - 15/17 amino acid residues identical.|
|Other Names||Mu-type opioid receptor, M-OR-1, MOR-1, Opioid receptor B, Oprm1, Ror-b|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide CSPAPGSWLNLSHVDGN, corresponding to amino acid residues 22-38 of the rat µ-Opioid receptor (Accession P33535). Extracellular, N-terminus.|
|Peptide Confirmation||Confirmed by amino acid analysis and mass-spectrography.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||25 µl, 50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Endogenous opiates such as endorphins, endomorphins, and enkephalins, as well as opiate drugs (including morphine) exert their effects by binding to opioid receptors. Three "classic" types of opioid receptors have been identified: mu (µ)-opioid (MOP) receptor, delta (δ)-opioid (DOP) receptor, and kappa (κ)-opioid (KOP) receptor.1 Recently, the nociceptin/orphanin FQ (N/OFQ) peptide (NOP) receptor was also described. Despite its significant sequence homology, its pharmacological profile differs greatly from those of the classic µ, δ, and κ receptors.2 The opioid receptors belong to the G protein-coupled receptor (GPCR) superfamily whose members share a common structure of seven putative transmembrane domains, an extracellular amino terminus, a cytoplasmic carboxyl terminus, and a third intracellular loop important for binding G proteins.1 All three receptors mediate opioid-induced analgesia. Supraspinal analgesia is mainly mediated by the µ-receptors, whereas µ-, δ-, and κ-receptors participate in the control of pain at the spinal level. These receptors also mediate the mood-altering properties of opioids.3 Of the opioid receptors, the µ-opioid receptor has been the most extensively studied due to its important role in mediating the actions of morphine and other analgesic agents, as well as other addictive drugs such as heroin.1 The µ-opioid receptors are expressed in the central nervous system (CNS) and in the peripherial nervous system.4 The highest densities are found in the thalamus, caudate putamen, neocortex, amygdala, and other brain regions known to have well established roles in pain and analgesia.5
1. Pan, L. et al. (2005) Neuroscience 133, 209.
3. Matthes, H.W. et al. (1998) J. Neurosci. 18, 7285.
4. Shaqura, M.A. et al. (2004) J. Pharmacol. Exp. Ther. 308, 712.
5. Baraldi, P.G. et al. (2006) Curr. Med. Chem. 13, 3467.
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