Analytical Data
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Gene name
AUR1
- Application
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Alternative Names
AUR1；Serine/threonine-Protein kinase Aurora-1
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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
P36107
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Expression Region
313-401aa
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AA Sequence
TKYTHLPIVDTSLFCRWSYTSIEKYDISKSDPLAADSNDIESVPLSNLELDFDLNMTDEPSVSPSLFDGSTSVSRSSATSITSLGVKRA
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Molecular Weight
26.7 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
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Protein Description
The study of AUR1 recombinant protein is predicated on its pivotal role in the cell cycle regulation, particularly during mitosis. AUR1, or Aurora Kinase A, is a serine/threonine kinase that is crucial for various processes such as centrosome maturation, spindle assembly, and chromosome alignment. Its dysregulation has been linked to numerous cancers, making it a target for potential therapeutic interventions. Researchers focus on the recombination of AUR1 to better understand its structure-function relationship, to identify its interaction partners, and to elucidate its mechanisms of action within the cell. The recombinant protein allows for detailed biochemical assays, structural analyses, and the development of inhibitors that could aid in cancer treatment. By harnessing techniques such as molecular cloning and protein expression systems, scientists can produce AUR1 in ample quantities, facilitating a deeper understanding of its biological significance and offering insights into potential drug development strategies aimed at targeting aberrant AUR1 activity in tumorigenesis. This ongoing research is vital for unraveling the complex molecular underpinnings of cancer and improving therapeutic outcomes.
