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- Order number: 7TM0319N-IC
- Content: 100 µl
- Host: Rabbit
The µ-Opioid Receptor antibody is directed against the distal end of the carboxyl-terminal tail of mouse, rat and human MOP. It detects selectively the canonical form of MOP and none of the putative splice variants. In can be used to detect total MOP receptors in Western blots independent of phosphorylation. The MOP antibody can also be used to isolate and enrich µ-opioid receptors from brain lysates. It also detects MOP in cultured cells and tissue sections by immunohistochemistry. The MOP antibody has been validated using knockout mice (KO-Validated).
Alternative Names | MOP, OPRM1, µ-Opioid Receptor, Mu Receptor |
IUPHAR Target ID | 319 |
UniProt ID | P35372 (human) P42866 (mouse) P33535 (rat) |
Western Blot (WB) | 1:1000 |
Immunocytochemistry (ICC) | 1:200 |
Immunohistochemistry (IHC) | 1:100 |
Species Reactivity | Human, Mouse, Rat |
Host / Isotype | Rabbit / IgG |
Class | Polyclonal |
Immunogen | A synthetic peptide with the sequence LENLEAETAPLP which is present in carboxyl-terminal tail of human, mouse and rat MOP |
Form | Liquid |
Purification | Antigen affinity chromatography |
Storage buffer | Dulbecco's PBS, pH 7.4, with 150 mM NaCl, 0.02% sodium azide |
Storage conditions | short-term 4°C, long-term -20°C |
Figure 1. Immunohistochemical identification of µ-Opioid Receptor in caudate putamen. Sections were dewaxed, microwaved in citric acid, and incubated with anti-MOP (µ-Opioid Receptor) antibody (7TM0319N-WB) at a dilution of 1:100. Sections were then sequentially treated with biotinylated anti-rabbit IgG and avidin-biotin solution.Color was developed by incubation in 3-amino-9-ethylcarbazole (AEC), and sections were counterstained with hematoxylin. Note, MOP receptors were detected at the rim and as islets in the caudate putamen.
Figure 2. Immunohistochemical identification of µ-Opioid Receptor in spinal cord dorsal horn. Sections were dewaxed, microwaved in citric acid, and incubated with anti-MOP (µ-Opioid Receptor) antibody (7TM0319N-WB) at a dilution of 1:100. Sections were then sequentially treated with biotinylated anti-rabbit IgG and avidin-biotin solution. Sections were then developed in 3,3-diaminobenzidine (DAB)-glucose oxidase and lightly counterstained with hematoxylin. Note, MOP receptors were uniformly detected at the plasma membrane of lung cells.
Figure 3. Immunohistochemical identification of µ-Opioid Receptor in dorsal root ganglia. Sections were dewaxed, microwaved in citric acid, and incubated with anti-MOP (µ-Opioid Receptor) antibody (7TM0319N-WB) at a dilution of 1:100. Sections were then sequentially treated with biotinylated anti-rabbit IgG and avidin-biotin solution. Sections were then developed in 3,3-diaminobenzidine (DAB)-glucose oxidase and lightly counterstained with hematoxylin. Note, MOP receptors were detected predominantly in small- and medium-size cells.
Figure 4. Immunocytochemical identification of µ-Opioid Receptor in HEK293 cells. HEK293 cells stably expressing the complement µ-Opioid Receptor (MOP) were either not exposed or exposed to 10 μM DAMGO ([D-Ala2,N-MePhe4, Gly-ol]-enkephalin) for 30 min and immunocytochemically stained with anti-MOP (µ-Opioid Receptor) antibody (7TM0319N-WB) at a dilution of 1:200. Note, MOP receptors were confined to the plasma membrane in untreated cells (0 min). MOP receptors were seen in perinuclear clusters of vesicles after 30 min DAMGO exposure.
Figure 5. Validation of the µ-Opioid Receptor in transfected HEK293 cells. Native HEK293 cells (MOCK) or HEK293 cells stably expressing the µ-Opioid Receptor (MOP) were lysed and immunoblotted with the phosphorylation-independent anti-MOP antibody (7TM0319N-WB) at a dilution of 1:1000.