Analytical Data
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Gene name
RNASE4
- Application
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Alternative Names
RNASE4；RNS4；Ribonuclease 4
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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
P34096
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Expression Region
29-147aa
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AA Sequence
QDGMYQRFLRQHVHPEETGGSDRYCNLMMQRRKMTLYHCKRFNTFIHEDIWNIRSICSTTNIQCKNGKMNCHEGVVKVTDCRDTGSSRAPNCRYRAIASTRRVVIACEGNPQVPVHFDG
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Molecular Weight
15.2 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
RNASE4, a member of the ribonuclease A superfamily, has garnered significant interest in recent years due to its potential roles in various biological processes and therapeutic applications. Initially discovered as an RNase with unique enzymatic properties, RNASE4 exhibits antimicrobial activity and has been implicated in the regulation of immune responses. Studies have shown that RNASE4 can interact with various cellular components, influencing cell proliferation and apoptosis. Furthermore, its expression patterns in different tissues suggest a multifaceted role in both normal physiology and pathological conditions, including cancer. Researchers have focused on the recombinant production of RNASE4, allowing for in-depth studies of its structure-function relationships and facilitating investigations into its potential as a therapeutic agent. The ability to produce RNASE4 in recombinant systems also opens avenues for exploring its enzymatic mechanisms and designing RNASE4-based drugs or biomolecules. As researchers continue to elucidate its functional roles, RNASE4 holds promise for advancements in biomedical research and novel therapeutic strategies.
