Analytical Data
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Gene name
RPA2
- Application
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Alternative Names
Replication factor A protein 2 ;RF-A protein 2Replication protein A 34KDA subunit ;RP-A p34
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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
P15927
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Expression Region
1-267aa
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Molecular Weight
55.9 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
RPA2, a key component of the replication protein A (RPA) complex, plays a crucial role in DNA replication, repair, and cellular response toDNA damage. It is a single-stranded DNA-binding protein that stabilizes unwound DNA during replication and helps initiate repair processes following genotoxic stress. Research into RPA2 has garnered attention due to its involvement in various cellular pathways, including those related to cancer, where abnormal expression or mutations are often observed. Understanding RPA2’s structure and function is essential for elucidating its role in maintaining genomic stability and its potential as a therapeutic target. Recent studies have focused on characterizing RPA2's interactions with other proteins and its post-translational modifications, which can influence its activity and stability. Additionally, the recombinant expression of RPA2 allows for detailed biochemical and structural analyses, providing insights into its mechanism of action. Investigating RPA2 at the molecular level not only enhances our understanding of fundamental cellular processes but also helps identify novel strategies for cancer treatment and prevention, making it a significant subject of ongoing research in molecular biology and medicinal chemistry.
