Analytical Data
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Gene name
AURKA
- Application
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Alternative Names
AIK; ARK1; AURA; AURORA2; BTAK; STK15; STK6; STK7; Aurora/IPL1-related kinase 1; Breast tumor-amplified kinase; Serine/threonine-protein kinase 6
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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
O14965
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Expression Region
Met1~Val218
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Molecular Weight
55kDa
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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
Aurora A kinase (AURKA) is a crucial mitotic serine/threonine kinase that plays a significant role in cell division, particularly in processes such as spindle assembly, centrosome maturation, and chromosome alignment. Aberrant regulation of AURKA has been implicated in various cancers, making it a valuable target for therapeutic interventions. The study of recombinant AURKA protein has become increasingly important for understanding its molecular mechanisms and functions. By producing AURKA in a recombinant form, researchers can investigate its biochemical properties, post-translational modifications, and interactions with other proteins in a controlled environment. This enables the elucidation of AURKA’s role in tumorigenesis and its potential as a drug target. Furthermore, recombinant AURKA is utilized in high-throughput screening assays for identifying small-molecule inhibitors that could serve as novel cancer therapies. The ongoing research on AURKA not only contributes to the basic understanding of cell cycle regulation but also paves the way for the development of targeted treatments, highlighting its dual significance in both fundamental biology and clinical applications.
