Analytical Data
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Gene name
RNASE10
- Application
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Alternative Names
RNASE9; Inactive ribonuclease-like protein 10
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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
Q5GAN6
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Expression Region
Leu27~Gln216
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Molecular Weight
27kDa
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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
RNASE10 is a member of the ribonuclease A superfamily, which plays a critical role in various biological processes, including RNA metabolism and immune responses. Its unique structure and function have garnered attention in the study of therapeutic applications, particularly in cancer treatment and infectious diseases. Unlike other ribonucleases, RNASE10 exhibits low enzymatic activity, which raises questions about its physiological role and potential as a therapeutic agent. Recent research has focused on the recombinant expression of RNASE10 to better understand its catalytic mechanisms and explore its antitumor properties. By generating recombinant RNASE10, scientists aim to investigate its activity in different biological contexts and identify possible interactions with cell surface receptors. Furthermore, the therapeutic potential of RNASE10 is being explored through its incorporation into drug delivery systems, enhancing the efficacy of existing treatments. As the understanding of RNASE10's function deepens, it may pave the way for novel strategies in targeting RNA-rich tumors and infectious pathogens, thereby contributing to the development of innovative biopharmaceuticals. This line of research highlights the importance of comprehensive studies on reconstituted proteins to unravel their functional roles and therapeutic potential in modern medicine.
