Analytical Data
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Gene name
RNASE11
- Application
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Alternative Names
RNASE11；C14orf6；Probable ribonuclease 11
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Species
Human
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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
Q8TAA1
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Expression Region
17-199aa
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AA Sequence
EASE STMKIIKEEF TDEEMQYDMA KSGQEKQTIE ILMNPILLVK NTSLSMSKDD MSSTLLTFRS LHYNDPKGNS SGNDKECCND MTVWRKVSEA NGSCKWSNNF IRSSTEVMRR VHRAPSCKFV QNPGISCCES LELENTVCQF TTGKQFPRCQ YHSVTSLEKI LTVLTGHSLM SWLVCGSKL
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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
RNASE11, a member of the ribonuclease A superfamily, has garnered attention in recent years due to its potential roles in various biological processes, including RNA metabolism, immune response, and inflammation. Originally discovered in humans, RNASE11 is primarily expressed in the testis and has been implicated in male fertility. Its unique structure and enzymatic properties suggest that it may play a crucial role in the degradation of RNA and regulation of gene expression. Given the increasing interest in ribonucleases for therapeutic applications, researchers are focusing on the recombinant production of RNASE11, which allows for detailed functional studies and characterization of its catalytic mechanisms. Understanding RNASE11's specificity, substrate interactions, and physiological relevance could pave the way for novel treatments targeting RNA-related pathologies, including certain cancers and viral infections. The ability to produce this protein in a recombinantly purified form not only facilitates biochemical analyses but also enhances the potential for developing RNASE11 as a biomarker or therapeutic agent. As research progresses, elucidating the functional significance of RNASE11 may contribute to broader insights into RNA biology and its impact on human health.
