ADRA1B Antibody (Rabbit mAb) [C3A12]

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 - 1:10000 IHC1:500

Application
WB, IHC

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
57 kDa 57 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
ADRA1B Antibody (Rabbit mAb) [C3A12] detects endogenous levels of total ADRA1B protein.

Clone
C3A12

Synonym(s)
Alpha-1B adrenergic receptor, Alpha-1B adrenoreceptor, Alpha-1B adrenoceptor, ADRA1B

Background
Alpha‑1B adrenergic receptor (ADRA1B) is a class A G protein‑coupled receptor of the α1‑adrenoceptor family that couples mainly to Gq/11 proteins and mediates catecholamine‑dependent vasoconstriction, cardiac modulation and central monoaminergic control through phosphatidylinositol–calcium second messenger signaling. The receptor has the typical seven transmembrane helices, extracellular loops that form the orthosteric binding pocket for norepinephrine and epinephrine, and intracellular regions that contact Gq/11 and β‑arrestins; recent high‑resolution crystal and cryo‑EM structures of human α1B bound to the inverse agonist (+)‑cyclazosin reveal the molecular determinants of subtype‑selective ligand recognition, including specific residues in the transmembrane bundle and extracellular vestibule that shape affinity and selectivity for aminergic drugs. Experimental and computational mutagenesis of α1B have identified key residues involved in receptor activation and Gq coupling, and functional studies demonstrate that receptor engagement activates phospholipase C‑β, leading to inositol trisphosphate production, intracellular Ca²⁺ mobilization and smooth muscle contraction in vascular beds, placing ADRA1B as a major contributor to peripheral vasoconstriction and blood pressure regulation. Knockout mouse models lacking α1B show blunted vasoconstrictor responses, altered blood pressure regulation, changes in glucose homeostasis and modified rewarding responses to drugs of abuse, indicating that ADRA1B integrates cardiovascular and metabolic signals with dopaminergic reward circuitry. In the central nervous system, a subset of α1B adrenoceptors innervated primarily by epinephrine has been proposed to form an “EPI–α1 system” that modulates serotonergic, noradrenergic and dopaminergic pathways in parallel; evidence from animal models and clinical data suggests that impairment or inhibition of this α1 system contributes to depressive phenotypes and that restoration of α1B‑mediated signaling by various antidepressants associates with improved behavioral activation, making ADRA1B a candidate target in mood disorders. Human genetic variation in ADRA1B influences vascular responses: a study of ADRA1B polymorphisms and dorsal hand vein constriction demonstrates that specific alleles correlate with interindividual and ethnic differences in adrenergic vasoconstriction, supporting a role for ADRA1B variants in susceptibility to hypertension and other vascular traits. Association analyses also implicate rare ADRA1B haplotypes in attention‑deficit/hyperactivity disorder, within broader noradrenergic gene mapping, reinforcing the contribution of α1B‑mediated norepinephrine signaling to neuropsychiatric disease risk.

Background

Alpha‑1B adrenergic receptor (ADRA1B) is a class A G protein‑coupled receptor of the α1‑adrenoceptor family that couples mainly to Gq/11 proteins and mediates catecholamine‑dependent vasoconstriction, cardiac modulation and central monoaminergic control through phosphatidylinositol–calcium second messenger signaling. The receptor has the typical seven transmembrane helices, extracellular loops that form the orthosteric binding pocket for norepinephrine and epinephrine, and intracellular regions that contact Gq/11 and β‑arrestins; recent high‑resolution crystal and cryo‑EM structures of human α1B bound to the inverse agonist (+)‑cyclazosin reveal the molecular determinants of subtype‑selective ligand recognition, including specific residues in the transmembrane bundle and extracellular vestibule that shape affinity and selectivity for aminergic drugs. Experimental and computational mutagenesis of α1B have identified key residues involved in receptor activation and Gq coupling, and functional studies demonstrate that receptor engagement activates phospholipase C‑β, leading to inositol trisphosphate production, intracellular Ca²⁺ mobilization and smooth muscle contraction in vascular beds, placing ADRA1B as a major contributor to peripheral vasoconstriction and blood pressure regulation. Knockout mouse models lacking α1B show blunted vasoconstrictor responses, altered blood pressure regulation, changes in glucose homeostasis and modified rewarding responses to drugs of abuse, indicating that ADRA1B integrates cardiovascular and metabolic signals with dopaminergic reward circuitry. In the central nervous system, a subset of α1B adrenoceptors innervated primarily by epinephrine has been proposed to form an “EPI–α1 system” that modulates serotonergic, noradrenergic and dopaminergic pathways in parallel; evidence from animal models and clinical data suggests that impairment or inhibition of this α1 system contributes to depressive phenotypes and that restoration of α1B‑mediated signaling by various antidepressants associates with improved behavioral activation, making ADRA1B a candidate target in mood disorders. Human genetic variation in ADRA1B influences vascular responses: a study of ADRA1B polymorphisms and dorsal hand vein constriction demonstrates that specific alleles correlate with interindividual and ethnic differences in adrenergic vasoconstriction, supporting a role for ADRA1B variants in susceptibility to hypertension and other vascular traits. Association analyses also implicate rare ADRA1B haplotypes in attention‑deficit/hyperactivity disorder, within broader noradrenergic gene mapping, reinforcing the contribution of α1B‑mediated norepinephrine signaling to neuropsychiatric disease risk.

References
https://pubmed.ncbi.nlm.nih.gov/35046410/ https://pubmed.ncbi.nlm.nih.gov/12503605/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%