This product is an active protein and may elicit a biological response in vivo, handle with caution.
RelevanceADRB2 is activated by the catecholamine epinephrine and couples to the G-protein Gs to mediate adeylate cyclase activation. ADRB2 is found in numerous tissues and cell types including vascular and bronchial smooth muscle cells, leukocytes and liver. ADRB2 mediates smooth muscle relaxation, inhibition of leukocyte function and activation of glycogenolysis. GaaS is the short splice variant of the alpha; subunit of the heterotrimeric G-protein Gs. Gs activates the effector adenylate cyclase. GaaS differs from the long splice variant (GsaL) by the absence of a 15-amino acid insert between the ras-like domain and the a-helical domain. GaaS possesses a higher GDP-affinity than GaaL. GTP-binding proteins possess a highly conserved aspartate residue in the NKXD motif that is critical for high-affinity interaction with GTP. In small GTP-binding proteins, the D/N-mutation switches base-specifity from guanine to xanthine. In contrast to all other known Ga D/N mutants, the exchange of Asp280 to Asn280 in GaaS does not lead to an inactivation in nucleotide binding. The D/N mutant is a Gaa with specificity for XTP and XppNHp relative to GTP and GppNHp respectively. However, the mutant is not specific for XTPgS relative to GTPgS probably because of conformational alterations in the catalytic site by the g-thiophosphate.
References for Recombinant human ADRB2 and GiaaS Asn280 fusion protein (ab90334)
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