Angiotensin II Type 2 Receptor Recombinant Rabbit Monoclonal Antibody [SN71-03] (ET1611-41)

UNIPROT #

P50052

PROTEIN NAME

Angiotensin II Type 2 Receptor

SYNONYMS

AGTR 2 antibody;Agtr2 antibody;AGTR2_HUMAN antibody;angiotensin II receptor type 2 antibody;Angiotensin II type-2 receptor antibody;Angiotensin receptor 2 antibody;AT 2 antibody;AT2 antibody;ATGR 2 antibody;ATGR2 antibody;MRX 88 antibody;MRX88 antibody;Type 2 angiotensin II receptor antibody;Type-2 angiotensin II receptor antibody

SEQUENCE SIMILARITIES

Belongs to the G-protein coupled receptor 1 family.

TISSUE SPECIFICITY

In adult, highly expressed in myometrium with lower levels in adrenal gland and fallopian tube. Expressed in the cerebellum. Very highly expressed in fetal kidney and intestine.

SUBCELLULAR LOCATION

Cell membrane.

FUNCTION

Angiotensin II (Ang II) is an important physiological effector of blood pressure and volume regulation through vasoconstriction, aldosterone release, sodium uptake and thirst stimulation. Although Ang II interacts with two types of cell surface receptors, AT1 and AT2, most of the major cardiovascular effects seem to be mediated through AT1. Molecular cloning of the AT1 protein has shown it to be a member of the G protein-associated seven transmembrane protein receptor family. Ang II treatment of cells results in activation of several signal transduction pathways as evidenced by tyrosine phosphorylation of several proteins and induction of others. PLCγ is phosphorylated after 30 seconds of treatment with Angiotensin II, indicating this as an early signal transduction event. Ang II treatment also stimulates phosphorylation of Shc, FAK and MAP kinases, and induces MKP-1, indicating stimulation of growth factor pathways. Ang II stimulation through AT1 has been shown to activate the JAK/Stat pathway involving a direct interaction between JAK2 and AT1 as demonstrated by coimmunoprecipitation. The AT1 receptor has no cytoplasmic kinase domain, but is able to function as a substrate for Src kinases and has several putative phosphorylation sites.