|Application ||WB, IHC, ICC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||36512 Da|
|Homology||Mouse, rat, bovine, canis and pig - identical.|
|Other Names||Adenosine receptor A1, ADORA1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)KKVSASSGDPQKYYGKE, corresponding to amino acid residues 213-229 of human A1AR (Accession P30542). 3rd intracellular loop.|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Application Details||Western blot analysis (WB): - Mouse muscle, brain and spinal cord lysates (1:5000) (see Garcia, N. et al. (2013) in Product Citations). Immunohistochemistry (IH): - Mouse plastic-embedded muscle sections (1:100) (see Garcia, N. et al. (2013) in Product Citations).|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.85 mg/ml.|
|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.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Adenosine is an endogenous nucleoside generated locally in tissues under conditions of hypoxia, ischemia, or inflammation. It modulates a variety of physiological functions in many tissues including brain and heart.1,2It exerts its action via four specific adenosine receptors (also named P1 purinergic receptors): A1-Adenosine Receptor (A1AR), A2A-Adenosine Receptor (A2AAR), A2B-Adenosine Receptor (A2BAR), and A3-Adenosine Receptor (A3AR). All are integral membrane proteins and members of the G Protein-Coupled Receptor superfamily. They share a common structure of seven putative transmembrane domains, an extracellular amino terminus, a cytoplasmic carboxyl terminus, and a third intracellular loop that is important in binding G proteins.1-3 The various adenosine receptors can be distinguished on the basis of their differential selectivity for adenosine analogs.1-3 A1AR is widely distributed and has been well characterized. High expression of A1AR is found in brain (mainly in the cortex, cerebellum, and hippocampus), dorsal horn of the spinal cord, adrenal gland, and atria, and to a lower extent in several other tissues including adipose tissue, colon, and kidney.2,4 A1AR modulates the activity of several ion channels. Activation of A1AR (by adenosine, its major agonist) inhibits N-type Ca2+ channels via a voltage-dependent, pertussis toxin (PTX)-sensitive pathway in neurons of the rat major pelvic ganglia (MPG).5 Since A1AR is the most prominent adenosine receptor in adipocytes, it has become a natural target for research on obesity, which is a major health problem.6,7 A possible role in cell proliferation and carcinogenesis has also been suggested for A1AR.8-10
1. Okusa, M.D. (2002) Am. J. Physiol. 282, F10.
2. Nakata, H. (1989) J. Biol. Chem. 264, 16545.
3. Linden, J. (1991) FASEB J. 5, 2668.
4. Park, K-S. et al. (2001) J. Pharmacol. Exp. Therap. 299, 501.
5. Rice, A.M. et al. (2000) Endocrinology 141, 1442.
6. LaNoue, K.F. and Martin, L.F. (1994) FASEB J. 8, 72.
7. Synowitz, M. et al. (2006) Cancer Res. 66, 8550.
8. Lelievre, V. et al. (1998) Eur. J. Pharmacol. 341, 289.
9. Khoo, H.E. et al. (1996) Cancer Lett. 106, 17.
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