Analytical Data
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Gene name
XRCC4
- Application
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Alternative Names
X-ray repair cross-complementing protein 4
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13426
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Expression Region
1-336aa
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Molecular Weight
65.3 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
XRCC4 (X-ray repair cross-complementing protein 4) plays a crucial role in the cellular mechanisms of DNA double-strand break repair, primarily through its function in non-homologous end joining (NHEJ). This process is vital for maintaining genomic stability and preventing mutations that could lead to cancer. Mutations or deficiencies in XRCC4 have been associated with various disorders, including immunodeficiencies and increased cancer susceptibility. Researchers have increasingly focused on XRCC4 due to its involvement in cellular responses to ionizing radiation and its potential as a therapeutic target for enhancing the efficacy of radiation therapy in cancer treatment. The study of XRCC4 recombinant proteins has provided valuable insights into its structural and functional properties, revealing its interaction with other key proteins in the NHEJ pathway, such as DNA ligase IV and the Ku heterodimer. This understanding not only aids in elucidating the fundamental mechanisms of DNA repair but also opens avenues for developing innovative strategies to manipulate this pathway for therapeutic benefits. With advancements in molecular biology techniques, including CRISPR-Cas9 and protein engineering, there is a growing interest in the potential of XRCC4-based therapies, which could enhance DNA repair in various therapeutic contexts or exploit its mechanisms to sensitize cancer cells to treatment. Overall, the research on XRCC4 recombinant proteins continues to be pivotal in advancing our understanding of DNA repair processes and their implications in health and disease.
