Analytical Data
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Gene name
PI4Ka
- Application
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Alternative Names
PIK4CA; PI4K-ALPHA; pi4K230
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P42356
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Expression Region
Met1~Trp300
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Molecular Weight
64kDa
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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
Phosphoinositide 3-kinase (PI3K) is a crucial enzyme involved in various cellular processes, including cell growth, proliferation, and survival. Among its isoforms, PI3K class I-alpha (PI3Kα, or PI4Ka) plays a fundamental role in mediating signaling pathways activated by growth factors and hormones. Dysregulation of PI3Kα is often associated with various diseases, particularly cancer, making it a significant target for therapeutic intervention. Research on recombinant PI4Ka protein offers insights into its structure, function, and regulatory mechanisms. Understanding the biochemical properties of PI4Ka, including its lipid-binding specificity and catalytic activity, is essential for the development of selective inhibitors that could serve as potential anticancer agents. Furthermore, studying the protein's interaction with other cellular components can elucidate its role in oncogenic signaling networks, thus paving the way for novel therapeutic strategies. Given the increasing interest in targeted therapies, the investigation of recombinant PI4Ka not only provides essential data for drug development but also enhances our understanding of the PI3K signaling pathway's complexity and its implications in disease pathology.
