Analytical Data
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Gene name
aur
- Application
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Alternative Names
aur；AIE2；AIK3；AIRK3；Aurora kinase C
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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
D7UQM5
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Expression Region
1-407aa
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AA Sequence
MTPTGPSHHS MAPKRVLPAA SQSNMYGNIR SASTTSTTAS TSSQALRLLQ NAKTSKNADN RIAHAERQGP PSAHPAAMQK PAARVAPSNE NRPDPAARQH QHQQQLQQQK ATGHDRVLKE SQAGNSTTTT MTSTQSKEAN KWSLANFDIG RPLGKGKFGN VYLAREKKSK FIVALKVLFK SQLQKAKVEH QLRREIEIQS HLRHDHILRL YGYFYDDTRV YLILEYAARG ELYKEMQAQK AGHFDEDRSA VYIYQLAKAL LYCHEKKVIH RDIKPENLLL DLKGDLKIAD FGWSVHAPSS RRATLCGTLD YLPPEMIEGK THDEKVDLWS LGVLCYEFLV GKPPFESQGN TETYRKITKV EFTFPKHVSE GARDLICKLL KHNPSHRLSL EGVIAHAWIQ EKISQRS
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Molecular Weight
45.9 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
AUR (Aurora Kinases) are a family of serine/threonine kinases that play crucial roles in regulating various aspects of cell division, including chromosome alignment, segregation, and cytokinesis. These kinases are vital for maintaining genomic stability, and their dysregulation is often associated with cancer progression and poor prognosis. Researchers have increasingly focused on the development of Aurora kinase inhibitors as potential therapeutic agents due to their overexpression or abnormal activity in various malignancies. The study of recombinant Aurora proteins contributes to our understanding of their structural and functional properties, which is essential for designing targeted therapies. By producing and characterizing AUR recombinant proteins, scientists can investigate their biological functions, identify novel substrates, and elucidate their roles in cell cycle regulation. Furthermore, structural studies provide insights into the mechanisms of kinase activity and can guide the development of specific inhibitors. Overall, understanding the complex biology of Aurora kinases and their potential as drug targets is pivotal in the ongoing battle against cancer, highlighting the importance of recombinant protein research in this field.
