Analytical Data
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Gene name
GNAI3
- Application
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Alternative Names
GNAI3;Guanine nucleotide-binding Protein G(i) subunit alpha-3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08754
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Expression Region
2-354aa
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AA Sequence
GCTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVK QMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARA DDARQLFVLAGSAEEGVMTPELAGVIKRLWRDGGVQACFSRSREYQLNDS ASYYLNDLDRISQSNYIPTQQDVLRTRVKTTGIVETHFTFKDLYFKMFDV GGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFD SICNNKWFTETSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAA YIQCQFEDLNRRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKEC GLY
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Molecular Weight
42.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
GNAI3, a member of the G protein alpha subunit family, plays a critical role in various cellular signaling pathways by regulating the activity of downstream effectors in response to G protein-coupled receptor activation. Recent studies have highlighted its involvement in diverse physiological processes such as cell proliferation, differentiation, and metabolism, as well as in pathological conditions including cancer, neurodegenerative diseases, and cardiovascular disorders. The functional dysregulation of GNAI3 has been implicated in tumorigenesis, leading to increasing interest in its potential as a therapeutic target. Furthermore, the development of recombinant GNAI3 proteins has facilitated in-depth investigations of its biochemical properties, interaction dynamics, and functional consequences in cellular contexts. By employing advanced techniques such as site-directed mutagenesis, biophysical characterization, and interaction assays, researchers aim to elucidate the mechanisms by which GNAI3 mediates signal transduction. This research not only contributes to a better understanding of GNAI3's role in health and disease but also paves the way for the identification of novel therapeutic strategies aimed at modulating GNAI3 activity for therapeutic benefit.
