MOP ( IHC-grade ), µ-Opioid Receptor Polyclonal Antibody

Overview
- 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).
  
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Properties
- Host
  
  rabbit
  
  Antibody Type
  
  polyclonal
  
  Isotype
  
  IgG
  
  Reactivity
  
  human; mouse; rat
  
  Immunogen
  
  A synthetic peptide with the sequence LENLEAETAPLP which is present in carboxyl-terminal tail of human, mouse and rat MOP
  
  Purification
  
  Antigen affinity chromatography
  
  Formulation
  
  Liquid
  
  Storage
  
  Short-term storage at 4°C and long-term storage at -20°C
  
  Antigen
  
  MOP, OPRM1, µ-Opioid Receptor, Mu Receptor (UniProt:P35372 (human), P42866 (mouse), P33535 (rat))
  
  * This product is intended for research use only.

Applications

Application

WB; ICC; IHC

Application	Dilutions
Western Blot (WB)	1:1000
Immunocytochemistry (ICC)	1:200
Immunohistochemistry (IHC)	1:100

Reference
- Glück L, Loktev A, Moulédous L, Mollereau C, Law PY, Schulz S. Loss of morphine reward and dependence in mice lacking G protein-coupled receptor kinase 5. Biol Psychiatry. 2014 Nov 15;76(10):767-74. doi: 10.1016/j.biopsych.2014.01.021. Epub 2014 Feb 3.
  Illing S, Mann A, Schulz S. Heterologous regulation of agonist-independent μ-opioid receptor phosphorylation by protein kinase C. Br J Pharmacol. 2014 Mar;171(5):1330-40. doi: 10.1111/bph.12546.
  Just S, Illing S, Trester-Zedlitz M, Lau EK, Kotowski SJ, Miess E, Mann A, Doll C, Trinidad JC, Burlingame AL, von Zastrow M, Schulz S. Differentiation of opioid drug effects by hierarchical multi-site phosphorylation. Mol Pharmacol. 2013 Mar;83(3):633-9. doi: 10.1124/mol.112.082875. Epub 2012 Dec 13.
  Doll C, Pöll F, Peuker K, Loktev A, Glück L, Schulz S. Deciphering µ-opioid receptor phosphorylation and dephosphorylation in HEK293 cells. Br J Pharmacol. 2012 Nov;167(6):1259-70. doi: 10.1111/j.1476-5381.2012.02080.x.
  Grecksch G, Just S, Pierstorff C, Imhof AK, Glück L, Doll C, Lupp A, Becker A, Koch T, Stumm R, Höllt V, Schulz S. Analgesic tolerance to high-efficacy agonists but not to morphine is diminished in phosphorylation-deficient S375A μ-opioid receptor knock-in mice. J Neurosci. 2011 Sep 28;31(39):13890-6. doi: 10.1523/JNEUROSCI.2304-11.2011.
  Doll C, Konietzko J, Pöll F, Koch T, Höllt V, Schulz S. Agonist-selective patterns of µ-opioid receptor phosphorylation revealed by phosphosite-specific antibodies. Br J Pharmacol. 2011 Sep;164(2):298-307. doi: 10.1111/j.1476-5381.2011.01382.x. PubMed PMID: 21449911; PubMed Central PMCID: PMC3174411.

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.

MOP ( IHC-grade ), µ-Opioid Receptor Polyclonal Antibody

MOP ( IHC-grade ), µ-Opioid Receptor Polyclonal Antibody

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