The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
In contrast to all other known G protein alpha D/N mutants, the exchange of Asp280 to Asn280 in GGsalphaS does not lead to an inactivation in nucleotide binding.
Mutation of Gln212 to Leu212 inhibits the intrinsic GTPase activity, resulting in a constitutively activated GsalphaS. This mutation also increases the GDP-affinity of GsalphaS.
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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
GTP-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.
Recombinant Rat G protein alpha (mutated Q212 L + D280 N) (ab90410) 使用論文
has not yet been referenced specifically in any publications.