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Description
ADRB2 Recombinant Rabbit mAb (S-2418-144)Product Specification Host Rabbit Antigen ADRB2 Synonyms Beta 2 adrenergic receptor; Beta 2 adrenoreceptor (Beta 2 adrenoceptor); ADRB2R; B2AR Immunogen Synthetic Peptide Location Cell membrane Accession P07550 Clone Number S 2418 144 Antibody Type Recombinant mAb Isotype IgG Application WB, IHC P Reactivity Hu, Ms, Rt Positive Sample mouse heart, rat heart Purification Protein A Concentration 0. 5 mg ml Conjugation Unconjugated Physical Appearance
Product Specification
| Host | Rabbit |
| Antigen | ADRB2 |
| Synonyms | Beta-2 adrenergic receptor; Beta-2 adrenoreceptor (Beta-2 adrenoceptor); ADRB2R; B2AR |
| Immunogen | Synthetic Peptide |
| Location | Cell membrane |
| Accession | P07550 |
| Clone Number | S-2418-144 |
| Antibody Type | Recombinant mAb |
| Isotype | IgG |
| Application | WB, IHC-P |
| Reactivity | Hu, Ms, Rt |
| Positive Sample | mouse heart, rat heart |
| Purification | Protein A |
| Concentration | 0.5 mg/ml |
| Conjugation | Unconjugated |
| Physical Appearance | Liquid |
| Storage Buffer | PBS, 40% Glycerol, 0.05% BSA, 0.03% Proclin 300 |
| Stability & Storage | 12 months from date of receipt / reconstitution, -20 °C as supplied |
Dilution
| application | dilution | species |
| WB | 1:1000 | Ms, Rt |
| IHC-P | 1:1000 | Hu, Ms, Rt |
Background
The ADRB2 (β2-adrenergic receptor) is a 413-amino-acid G-protein-coupled receptor embedded in the plasma membrane of airway, vascular, and adipose tissues, where it binds epinephrine and norepinephrine to trigger intracellular signaling cascades via Gs-mediated adenylyl cyclase activation, elevating cAMP and PKA to relax bronchial and vascular smooth muscle, modulate lipolysis, and influence cardiac output; encoded on chromosome 5q31–32, ADRB2 is highly polymorphic—most notably the Arg16Gly and Gln27Glu variants that alter down-regulation and desensitization—making it a pharmacogenomic target for β2-agonists in asthma and COPD therapy, and its structure has been captured in both active and inactive conformations by X-ray crystallography, revealing the molecular basis of agonist efficacy, inverse agonism, and biased signaling exploited in modern drug design.
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