The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/100 - 1/500. Detects a band of approximately 47 kDa (predicted molecular weight: 47 kDa).
FunctionBeta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
Sequence similaritiesBelongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB2 sub-subfamily.
Post-translational modificationsPalmitoylated; may reduce accessibility of Ser-345 and Ser-346 by anchoring Cys-341 to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation. Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK. Phosphorylated upon DNA damage, probably by ATM or ATR. Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor. Ubiquitinated. Agonist-induced ubiquitination leads to sort internalized receptors to the lysosomes for degradation. Deubiquitination by USP20 and USP33, leads to ADRB2 recycling and resensitization after prolonged agonist stimulation. USP20 and USP33 are constitutively associated and are dissociated immediately after agonist stimulation.
Anti-beta 2 Adrenergic Receptor antibody - Aminoterminal end images
Western blot - beta 2 Adrenergic Receptor antibody - Aminoterminal end (ab71219)
Anti-beta 2 Adrenergic Receptor antibody - Aminoterminal end (ab71219) at 1/440 dilution + HL60 cell line lysates at 35 µg
Predicted band size : 47 kDa Observed band size : 47 kDa
References for Anti-beta 2 Adrenergic Receptor antibody - Aminoterminal end (ab71219)
This product has been referenced in:
O'Leary AP et al. Beta-Adrenoceptor Activation Reduces Both Dermal Microvascular Endothelial Cell Migration Via a cAMP-Dependent Mechanism and Wound Angiogenesis. J Cell PhysiolN/A:N/A (2014).
Read more (PubMed: 24986762) »