Analytical Data
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Gene name
fanC
- Application
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Alternative Names
fanC；FAAP10；MHF2；STRA13；Centromere Protein X
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Species
E.coli
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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
P18103
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Expression Region
23-181aa
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AA Sequence
NTGTINFNGKITSATCTIDPEVNGNRTSTIDLGQAAISGHGTVVDFKLKPAPGSNDCLAKTNARIDWSGSMNSLGFNNTASGNTAAKGYHMTLRATNVGNGSGGANINTSFTTAEYTHTSAIQSFNYSAQLKKDDRAPSNGGYKAGVFTTSASFLVTYM
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Molecular Weight
32.5 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
FanC is a crucial component of the Fanconi Anemia (FA) pathway, a DNA repair mechanism that maintains genomic stability. Fanconi Anemia is a rare genetic disorder characterized by hypersensitivity to DNA cross-linking agents, leading to bone marrow failure, developmental abnormalities, and a heightened risk of cancer. The FanC protein plays an essential role in the monoubiquitination of FANCD2, facilitating the repair of DNA interstrand cross-links. Research into recombinant FanC proteins has gained significance in understanding FA pathology and developing potential therapeutic strategies. By studying the structure and function of FanC, scientists aim to elucidate the molecular mechanisms behind FA, revealing how mutations in the FANCD2 and related genes disrupt normal cellular processes. This research not only deepens our knowledge of the FA pathway but also has implications for cancer therapies, particularly in enhancing the efficacy of chemotherapeutic agents that rely on the integrity of DNA repair mechanisms. Furthermore, recombinant FanC can serve as a valuable tool in diagnostic assays and potential gene therapy approaches, providing hope for targeted treatments in individuals affected by Fanconi Anemia. As such, the study of FanC recombinant proteins is a critical step toward unraveling the complexities of DNA repair and developing targeted interventions for individuals with FA and related disorders.
