Analytical Data
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Gene name
SLFN11
- Application
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Alternative Names
SLFN11; Schlafen family member 11; EC 3.6.-.-
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q7Z7L1
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Expression Region
345-901aa
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Molecular Weight
69.6 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
SLFN11 (Sleepy Family Member 11) is a member of the Schlafen gene family known for its roles in cellular stress response and regulation of cell proliferation. Recent studies have highlighted its potential as a tumor suppressor, particularly in the context of various cancers, including breast and ovarian cancers, where its expression correlates with improved patient outcomes. The significance of SLFN11 in DNA repair mechanisms has garnered attention, as it interacts with key proteins involved in the DNA damage response, such as RAD51. Recombination deficiencies, frequently observed in tumors, may be counteracted by SLFN11, providing a potential therapeutic target. Research into SLFN11 recombinant proteins aims to elucidate its structural and functional properties, helping to understand its mechanisms of action at the molecular level. This knowledge could pave the way for novel treatments that exploit SLFN11’s role in enhancing DNA repair processes in chemotherapy-resistant tumors. As researchers develop recombinant forms of SLFN11, they hope to facilitate high-throughput screens for small molecules that can modulate its activity, opening new avenues for cancer therapy and improving patient management in oncological settings.
