|Application ||WB, IHC|
|Calculated MW||50369 Da|
|Homology||Rat - 14/15 amino acid residues identical; mouse-13/15 amino acid residues identical; human - 10/14 amino acid residues identical.|
|Other Names||Alpha-2B adrenergic receptor, Alpha-2B adrenoreceptor, Alpha-2B adrenoceptor, Alpha-2BAR, Adra2b|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)RPEPRGLPQ*SELNQE, corresponding to amino acid residues 160-174 of rat ־±2B- Adrenoceptor with replacement of cysteine 169 (C169) with serine (*S) (Accession P19328). 2nd extracellular loop.|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 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.|
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.
Adrenoceptors (also called Adrenergic receptors) are the receptors for the catecholamines adrenaline and noradrenaline (called epinephrine and norepinephrine in the United States). Adrenaline and noradrenaline play important roles in the control of blood pressure, myocardial contractile rate and force, airway reactivity, and a variety of metabolic and central nervous system functions. The Adrenoceptors are members of the G-protein coupled receptor (GPCR) superfamily of membrane proteins. They share a common structure of seven putative transmembrane domains, an extracellular amino terminus, and a cytoplasmic carboxyl terminus.The Adrenoceptors are divided into three types: α1, α2 and β-Adrenoceptors. Each type is further divided into at least three subtypes: α1A, α1B, α1D, α2A, α2B, α2C, β1, β2, β31,2. The Adrenoceptors are expressed in nearly all peripheral tissues and in the central nervous system1,2. The α2B-Adrenoceptor has a distinct pattern of expression within the brain, liver lung and kidney, and recent studies using the knock out mouse system have shown that disruption of this receptor indeed affects mouse viability3, blood pressure responses to α2-Adrenoceptors agonists3 and the hypertensive response to salt loading4. Like the α2A-Adrenoceptor subtype, the α2B-Adrenoceptor undergoes short term agonist promoted desensitization5. This desensitization is due to the phosphorylation of the receptor by G-protein coupled receptor kinases (GRKs)6 which ultimately promotes uncoupling of the receptor from the G-protein subunit7. Abgent is pleased to offer a highly specific antibody directed against an extracellular epitope of rat α2B-Adrenoceptor. The Anti-α2B-Adrenoceptor (extracellular) antibody (#AG1375) can be used for Western blot analysis. It has been designed to recognize α2B-Adrenoceptor from mouse, rat and human samples.
1. IUPHAR RECEPTOR DATABASE | ADRENOCEPTORS
2. Piascik, M. T .and Perez, D. M. (2001) J. Pharmacol. Exp. Ther. 298, 403.
3. Link, R.E. et al. (1996) Science 273, 803.
4. Makaritsis, K.P. et al. (1999) Hypertension 33, 14.
5. Eason, M.G. and Liggett, S.B. (1992) J. Biol. Chem. 267, 25473.
6. Pitcher, J.A. et al. (1998) Annu. Rev. Biochem. 67, 653.
7. Kurose, H. and Lefkowitz, R.J. (1994) J. Biol. Chem. 269, 10093.
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