Rabbit anti-Human ADRA1A Polyclonal Antibody

Uniprot Id

P35348

Target Species

Human

Target Name

ADRA1A

Target Full Name

Alpha-1A adrenergic receptor

Target Function

This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes.

Target Subcellular Location

Nucleus membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Cytoplasm. Membrane, caveola. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes.

Target Protein Families

G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRA1A sub-subfamily

Target Tissue Specificity

Expressed in heart, brain, liver and prostate, but not in kidney, lung, adrenal, aorta and pituitary. Within the prostate, expressed in the apex, base, periurethral and lateral lobe. Isoform 4 is the most abundant isoform expressed in the prostate with hi

Target Research Area

Neuroscience

Target Synonyms

ADRA1A; ADRA1C; Alpha-1A adrenergic receptor; Alpha-1A adrenoreceptor; Alpha-1A adrenoceptor; Alpha-1C adrenergic receptor; Alpha-adrenergic receptor 1c

Target Background

Alpha-1-adrenergic receptors (alpha-1-ARs) are members of the G protein-coupled receptor superfamily. They activate mitogenic responses and regulate growth and proliferation of many cells. There are 3 alpha-1-AR subtypes: alpha-1A, -1B and -1D, all of which signal through the Gq/11 family of G-proteins and different subtypes show different patterns of activation. This gene encodes alpha-1A-adrenergic receptor. Alternative splicing of this gene generates four transcript variants, which encode four different isoforms with distinct C-termini but having similar ligand binding properties.