Analytical Data
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Gene name
PKBa
- Application
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Alternative Names
PKBa；Non-reducing polyketide synthase pkbA
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Species
E.coli
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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
P54644
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Expression Region
1-444aa
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AA Sequence
MSTAPIKHEG FLTKEGGGFK SWKKRWFILK GGDLSYYKTK GELVPLGVIH LNTSGHIKNS DRKKRVNGFE VQTPSRTYFL CSETEEERAK WIEILINERE LLLNGGKQPK KSEKVGVADF ELLNLVGKGS FGKVIQVRKK DTGEVYAMKV LSKKHIVEHN EVEHTLSERN ILQKINHPFL VNLNYSFQTE DKLYFILDYV NGGELFYHLQ KDKKFTEDRV RYYGAEIVLA LEHLHLSGVI YRDLKPENLL LTNEGHICMT DFGLCKEGLL TPTDKTGTFC GTPEYLAPEV LQGNGYGKQV DWWSFGSLLY EMLTGLPPFY NQDVQEMYRK IMMEKLSFPH FISPDARSLL EQLLERDPEK RLADPNLIKR HPFFRSIDWE QLFQKNIPPP FIPNVKGSAD TSQIDPVFTD EAPSLTMAGE CALNPQQQKD FEGFTYVAES EHLR
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Molecular Weight
51 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
Related Products
Protein Description
The study of PKBa (Protein Kinase B alpha), a key member of the AKT family of serine/threonine kinases, has gained significant attention due to its critical role in various cellular processes, including metabolism, cell survival, and proliferation. Dysregulation of PKBa activity has been implicated in numerous diseases, particularly cancer, where its overactivation can promote tumor growth and resistance to apoptosis. Researchers have focused on understanding the intricate signaling pathways involving PKBa, particularly its activation by phosphoinositide phosphates and growth factors. The development of PKBa recombinant proteins has enabled detailed biochemical and structural studies, facilitating investigations into its mechanism of action and interactions with other cellular proteins. These studies aim to elucidate how PKBa contributes to oncogenic processes and to identify potential therapeutic targets for inhibiting its activity. The recombinant form of PKBa allows for high-yield production and purification, making it a valuable tool for drug screening and the development of PKBa inhibitors, which hold promise for cancer treatment. Overall, the ongoing research on PKBa and its recombinant protein derivatives is crucial for advancing our understanding of cancer biology and developing new therapeutic strategies.
