The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
GTP-binding possesses a highly conserved aspartate residue in the NKXD motif that is critical for high-affinity interaction with GTP. In almost all GTP-binding proteins so far, the D/N-mutation switches base-specifity from guanine to xanthine.
Whereas the exchange of Asp295 to Asn295 leads to inactive mutants of Galpha-subunits, an additional Q/L-mutation in the catalytic site (Gln227 to Leu227) rescues protein function and induces xanthine nucleotide-specifity.
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Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Guanine nucleotide binding protein G(s) alpha subunit
Guanine nucleotide binding protein G(s) subunit alpha isoforms XLas
guanine nucleotide regulatory protein
Neuroendocrine secretory protein
RelevanceGTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.
Cellular localizationCell Membrane
References for Recombinant Rat G protein alpha (mutated L227 + N295) (ab90406)
has not yet been referenced specifically in any publications.
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