Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner.Benovic J.L., FEBS Lett. 283:122-126(1991).Chuang T.T., J. Biol. Chem. 267:6886-6892(1992).Penn R.B., J. Biol. Chem. 269:14924-14930(1994).
Host
Rabbit
Immunogen
Synthesized peptide derived from N-terminal of Human ADRBK1.
Raised In
Rabbit
Reactivity
Human, Mouse, Rat
Regulatory
RUO
Relevance
Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner.
Benovic J.L., FEBS Lett. 283:122-126(1991). Chuang T.T., J. Biol. Chem. 267:6886-6892(1992). Penn R.B., J. Biol. Chem. 269:14924-14930(1994).
Species
Homo Sapiens (Human)
Specificity
The antibody detects endogenous levels of total ADRBK1protein.
Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner.