Analytical Data
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Gene name
RAD51D
- Application
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Alternative Names
R51H3 RAD51 homolog D RAD51-like protein 3 TRAD
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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
O75771
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Expression Region
1-328aa
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Molecular Weight
62 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
RAD51D is a crucial protein involved in the fundamental process of homologous recombination, a key mechanism for repairing DNA double-strand breaks and ensuring genomic stability. Mutations in the RAD51D gene have been linked to hereditary breast and ovarian cancer, particularly in families with a predisposition to these malignancies. This association highlights the protein's potential role as a tumor suppressor, as its dysfunction can lead to genomic instability and increased cancer risk. Researchers have focused on understanding the biochemical properties and molecular mechanisms of RAD51D, including its interactions with other repair proteins and its regulation during the DNA damage response. Recent studies employing advanced techniques such as cryo-electron microscopy and biochemical assays have revealed insights into the protein's structural dynamics and recruitment to sites of DNA damage. Furthermore, the characterization of RAD51D's role in DNA repair pathways has opened avenues for targeted therapies, especially in cancer types associated with RAD51D mutations. Understanding the implications of RAD51D function in both normal cellular processes and oncogenesis is critical for developing novel strategies in cancer prevention and treatment, making it a significant focus of ongoing genetic and therapeutic research in oncology.
