Analytical Data
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Gene name
GNAI2
- Application
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Alternative Names
Guanine nucleotide-binding protein G(i) subunit alpha-2; Adenylate cyclase-inhibiting G alpha protein; GNAI2
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Species
Mouse
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08752
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Expression Region
G2-F355
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AA Sequence
GCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPQRADDARQLFALSCAAEEQGMLPEDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITQSSLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
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Protein Length
Full Length of Mature Protein
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Molecular Weight
44 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
GNAI2, a member of the G protein alpha subunit family, plays a crucial role in intracellular signaling by participating in the regulation of various pathways, including those involved in cell growth, differentiation, and metabolism. Its dysregulation has been implicated in numerous diseases, including cancer and neurological disorders, making it a significant target for therapeutic research. The study of recombinant GNAI2 proteins is essential to understand their structure-function relationships, signaling mechanisms, and interactions with other cellular proteins. Recent advances in protein engineering and expression systems have enabled the production of high-purity GNAI2 proteins, facilitating detailed biochemical and biophysical analyses. These studies aim to elucidate the molecular mechanisms underlying GNAI2's role in signal transduction pathways, thereby providing insights into its potential as a therapeutic target. As researchers explore the regulatory cascades involving GNAI2, the development of specific inhibitors or modulators could lead to novel treatments for conditions associated with aberrant GNAI2 signaling, highlighting the importance of ongoing research in this area.
