Analytical Data
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Gene name
AKT2
- Application
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Alternative Names
AKT2; PKBBETA; PRKB-B; RAC-BETA; RAC-Beta Serine/Threonine-Protein Kinase; V-Akt Murine Thymoma Viral Oncogene Homolog 2
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P31751
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Expression Region
Lys142~Ile412
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Molecular Weight
38kDa
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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
Related Products
Protein Description
AKT2, a member of the AKT family of serine/threonine kinases, plays a critical role in various cellular processes, including metabolism, growth, proliferation, and survival. It is activated in response to insulin and growth factors, making it integral to signaling pathways that regulate glucose homeostasis and cellular response to stress. Dysregulation of AKT2 has been associated with several diseases, particularly type 2 diabetes and various cancers, highlighting its potential as a therapeutic target. Understanding the structure and function of AKT2 is essential for developing targeted treatments. The study of recombinant AKT2 protein allows researchers to explore its biochemistry, interaction with other molecules, and regulatory mechanisms. This can pave the way for novel strategies to manipulate AKT2 activity in disease contexts. Advances in protein engineering and expression systems have enabled the production of active AKT2, facilitating further investigations into its role in cell signaling and its implications in metabolic diseases and tumor biology. Overall, the research into AKT2 recombinant protein serves as a foundation for future therapeutic developments aimed at correcting the imbalances associated with its dysfunction.
