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stimulatory heterotrimeric G-protein, long splice variant of the α-subunit

rat, recombinant, Sf9 insect cells

Cat. No. Amount Price (EUR) Buy / Note
PR-504 1 ml 345,00 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped on dry ice

Storage Conditions: store at -80 °C
avoid freeze/thaw cycles

Shelf Life: 12 months

Molecular Weight: 52 kDa

Accession number: NM_019132

Accession number: NM_019132

Form: Membrane suspension (Supplied in 75 mM Tris-HCl pH 7.4, 12.5 mM MgCl2 and 1 mM EDTA)

GsαL is the long splice variant of the α-subunit of stimulatory heterotrimeric Gs-proteins. It differs from the short splice variant (GsaS) by 15-amino acid insert between the Ras-like domain and the α-helical domain. GsαL activates adenylate cyclase (AC) and possesses a lower GDP-affinity than GsαS (cat.# PR-505). These differences in GDP-affinity have important consequences for receptor/G-protein coupling and AC activation. The exchange of Gln227 to Leu227 inhibits the intrinsic GTPase activity, resulting in a contitutively active Gα, and increases GDP-affinity of Gα.

Selected References:
Graziano et al. (1989) Expression of G in Escherichia coli. Purification and properties of two forms of the protein. J. Biol. Chem. 264:409.
Yu et al. (1998) Interaction of the Xanthine Nucleotide Binding G Mutant with G Protein-coupled Receptors. J. Biol. Chem. 273:30183.
Gille et al. (2003) 2' (3')-O- (N-Methylanthraniloyl)- substituted GTP Analogs: A Novel Class of Potent Competitive Adenylyl Cyclase Inhibitors. J. Biol. Chem. 278:12672.
Gille et al. (2003) GDP Affinity and Order State of the catalytic Site Are Critical for Function of Xanthine Nucleotide-selective Gαs Proteins. J. Biol. Chem. 278:7822.