Analytical Data
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Gene name
RPAIN
- Application
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Alternative Names
RPAIN;RIP;RPA-interacting Protein
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Species
Human
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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
Q86UA6-6
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Expression Region
1-106aa
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AA Sequence
GSSHHHHHH SSGLVPRGSH MGSMAESLRS PRRSLYKLVG SPPWKEAFRQ RCLERMRNSR DRLLNRYRQA GSSGPGNSQN SFLVQEVMEE EWNALQSVEN CPEDLAQLEE LIDMAVLEEI QQELINQGL
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Molecular Weight
15 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
RPAIN, or Replication Protein A-Interacting Protein, has garnered attention in the field of molecular biology due to its critical role in cellular processes such as DNA replication, repair, and cell cycle regulation. It is known to interact with the replication protein A (RPA), which is essential for maintaining genomic stability. Dysfunction in the RPAIN protein has been linked to various diseases, including cancer, highlighting its potential as a biomarker for disease progression or a target for therapeutic interventions. Recent studies have focused on elucidating the structural and functional aspects of RPAIN, exploring how its interactions with RPA and other cellular factors influence DNA metabolic processes. Understanding the molecular mechanisms of RPAIN could provide insights into the intricate web of signaling pathways involved in DNA repair and cell cycle control. Given the increasing importance of precision medicine, RPAIN’s role in disease mechanisms makes it a significant subject for ongoing research aimed at developing targeted therapies and advancing our knowledge of tumor biology and cell proliferation dynamics.
