Analytical Data
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Gene name
Gna12
- Application
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Alternative Names
G alpha-12;G-protein subunit alpha-12
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P27600
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Expression Region
1-379aa
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Molecular Weight
51.5 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
Gna12, a member of the G protein α subunit family, plays a pivotal role in various cellular processes by transducing signals from G protein-coupled receptors (GPCRs) to intracellular effectors. Its involvement in key pathways, such as those regulating cell growth, differentiation, and migration, has sparked significant interest in understanding its molecular mechanisms. Recent studies have highlighted Gna12's contribution to oncogenic signaling and cancer progression, as its aberrant activation is often associated with several malignancies. The reconstitution of Gna12 as a recombinant protein allows researchers to investigate its biochemical properties, binding affinities, and interactions with other signaling molecules in controlled environments. Moreover, understanding the structure-function relationship of Gna12 can provide insights into its role in pathophysiological conditions, thereby indicating potential therapeutic targets for interventions. The study of Gna12 as a recombinant protein not only contributes to elucidating the intricacies of GPCR signaling but also enhances our understanding of its implications in diseases like cancer, underscoring the necessity for further investigation into its functional roles and regulatory mechanisms. Overall, characterizing Gna12 through recombinant expression systems paves the way for innovative approaches in drug development and therapeutic strategies related to G protein signaling pathways.
