Analytical Data
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Gene name
Ku70-Ku80 Heterodimer
- Application
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Alternative Names
5'-deoxyribose-5-phosphate lyase Ku70 ;5'-dRP lyase Ku7070KDA subunit of Ku antigen;ATP-dependent DNA helicase 2 subunit 1ATP-dependent DNA helicase II 70KDA subunitCTC box-binding factor 75KDA subunit ;CTC75 ;CTCBFDNA repair protein XR;CC6Lupus Ku autoantigen protein p70 ;Ku70Thyroid-lupus autoantigen ;TLAAX-ray repair complementing defective repair in Chinese hamster cells 6
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P12956
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Expression Region
6-222aa
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Molecular Weight
28.8 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 research on the Ku70-Ku80 heterodimer is significant due to its critical role in the cellular response to DNA damage and the maintenance of genomic stability. Ku proteins, specifically Ku70 and Ku80, form a heterodimer that binds to DNA double-strand breaks (DSBs), a prevalent type of DNA damage resulting from various sources, including ionizing radiation and oxidative stress. This binding initiates the non-homologous end joining (NHEJ) repair pathway, which is pivotal for restoring DNA integrity. Moreover, the Ku heterodimer is involved in various cellular processes beyond DNA repair, including regulation of gene expression and telomere maintenance. Understanding the structural and functional properties of the Ku70-Ku80 complex can provide insights into its role in cancer biology, where dysregulation of DNA repair mechanisms often contributes to tumorigenesis. Researchers employ techniques such as recombinantly expressed proteins, X-ray crystallography, and biochemical assays to elucidate the interactions and mechanisms of the Ku heterodimer. This knowledge is essential not only for comprehending fundamental cellular processes but also for developing therapeutics targeting the NHEJ pathway, which may enhance the efficacy of radiotherapy and chemotherapeutics in cancer treatment. Furthermore, the exploration of Ku70-Ku80 dynamics offers potential avenues for addressing diseases linked to genetic instability, thus highlighting the relevance of this research in both basic biology and clinical applications.
