Analytical Data
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Gene name
PKIb
- Application
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Alternative Names
PKIB;PRKACN2;cAMP-dependent Protein kinase inhibitor beta
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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
Q9C010
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Expression Region
1-98aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMRTDSSKMTDVESGVANFASSARAGRRNAL PDIQSSAATDGTSDLPLKLEALSVKEDAKEKDEKTTQDQLEKPQNEEK
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Molecular Weight
11 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 PKIb (Protein Kinase B, isoform beta) recombinant proteins has gained significant attention due to their crucial role in cellular signaling pathways, particularly in the regulation of metabolism, cell proliferation, and survival. PKIb, a member of the Akt family of serine/threonine kinases, is activated in response to various growth factors and is pivotal in mediating insulin signaling. The understanding of its biological function is essential, as dysregulation of PKIb has been implicated in various diseases, including cancer and metabolic disorders. Researchers have focused on developing recombinant PKIb proteins to elucidate their specific mechanisms of action and to facilitate structure-function analysis. These recombinant proteins serve as valuable tools for studying phosphorylation events, protein-protein interactions, and cellular responses to therapeutic agents. Furthermore, the production of PKIb recombinant proteins allows for in vitro assays and high-throughput screening of potential inhibitors, which can lead to the development of novel treatments. As a result, the investigation into PKIb recombinant proteins is not only important for basic biological research but also holds promise for clinical applications in combating diseases linked to PKIb dysregulation.
