Analytical Data
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Gene name
AKT2
- Application
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Alternative Names
AKT2；RAC-beta serine/threonine-Protein kinase
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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
P31751
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Expression Region
1- 481aa
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AA Sequence
MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLP PLNNFSVAEC QLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREE WMRAIQMVANSLKQRAPGEDPM DYKCGSPSDSSTTEEMEVAVSKARAK VTMNDFDYLKLLGKGTFGKVILVREKATGRYYAM KILRKEVIIAKDEV AHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFH LS RERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKIT DFGLCKEG ISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVM YEMMCGRLPFYNQDHERLFE LILMEEIRFPRTLSPEAKSLLAGLLKKD PKQRLGGGPSDAKEVMEHRFFLSINWQDVVQK KLLPPFKPQVTSEVDT RYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIR E
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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 crucial role in cellular processes such as metabolism, cell proliferation, and survival. This protein is particularly significant in the context of insulin signaling and cancer biology. Alterations in AKT2 expression and activity have been implicated in various metabolic disorders and malignancies, making it a target of interest for therapeutic interventions. The study of recombinant AKT2 protein has gained momentum due to its potential role in elucidating the molecular mechanisms underlying these diseases. Producing AKT2 as a recombinant protein allows researchers to investigate its biochemical properties, interaction with substrates, and the effects of post-translational modifications. Furthermore, understanding the structure-function relationship of AKT2 can provide insight into its regulatory mechanisms and help identify potential small-molecule inhibitors or activators that can modulate its activity. Research into AKT2 also paves the way for novel strategies in developing treatments for conditions like type 2 diabetes and various cancers, where targeting the AKT signaling pathway can yield significant therapeutic benefits. Overall, the exploration of AKT2’s recombinant protein not only enhances our comprehension of its biological functions but also opens avenues for innovative therapeutic approaches in managing related diseases.
