Analytical Data
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Gene name
RS
- Application
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Alternative Names
RS1; XLRS1; Retinoschisis X-Linked,Juvenile 1; X-linked juvenile retinoschisis protein
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15537
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Expression Region
Ser24~Ala224
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Molecular Weight
53kDa
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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
Research on RS (Rescue/Repair) recombinant proteins has gained significant attention in recent years due to their potential applications in various fields, including biotechnology, medicine, and agriculture. RS proteins are characterized by their ability to facilitate the repair of damaged cells and tissues, making them valuable in regenerative medicine and therapeutic interventions for degenerative diseases. These proteins often play critical roles in processes such as DNA repair, cellular stress response, and apoptosis regulation. Advances in molecular biology techniques, including recombinant DNA technology, have enabled scientists to produce these proteins in vitro, allowing for the detailed study of their functions and mechanisms. Furthermore, the ability to engineer RS proteins with enhanced properties opens new avenues for innovative treatments, such as targeted therapies for cancer and gene editing applications. The ongoing exploration of RS recombinant proteins also extends to agricultural sciences, where they can be utilized to improve stress tolerance in crops, contributing to food security amidst changing climates. Overall, the multifaceted nature of RS proteins positions them as promising candidates for future research, with the potential to revolutionize both therapeutic strategies and agricultural practices.
