Analytical Data
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Gene name
ARSF
- Application
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Alternative Names
ASF
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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
P54793
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Expression Region
His23~Asp300
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Molecular Weight
35kDa
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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
The study of ARSF (Asparagine-Rich Protein with Similarity to FIC) recombinant proteins has gained attention due to their potential roles in various biological processes and disease mechanisms. ARSF proteins are implicated in cellular stress responses and have been linked to the regulation of essential cellular functions such as apoptosis, cell proliferation, and differentiation. Understanding the structure and function of ARSF recombinant proteins can provide insights into their specific biological activities and interactions within the cellular environment. Moreover, alterations in ARSF levels have been associated with several pathologies, including cancer, making them a valuable target for therapeutic strategies. The advancement of recombinant DNA technology allows for the production of these proteins in a controlled manner, facilitating detailed biochemical and functional studies. This research not only enhances our understanding of ARSF’s biological roles but also opens up new avenues for the development of novel diagnostic and therapeutic applications in diseases where ARSF dysfunction is a contributing factor. Through the exploration of ARSF recombinant proteins, scientists aim to unravel the intricate relationships between these proteins and cellular health, potentially leading to groundbreaking discoveries in the field of molecular medicine and biotechnology.
