Analytical Data
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Gene name
RNase A
- Application
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Alternative Names
RNASE1; RNASE; Rnase-A; RNase UpI-1; RIB-1; Ribonuclease,RNase A Family,1(Pancreatic)
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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
P07998
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Expression Region
Lys29~Thr156
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Molecular Weight
18kDa
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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
Ribonuclease A (RNase A) is a well-studied enzyme known for its ability to catalyze the degradation of RNA, making it a valuable tool in biochemistry and molecular biology. As a member of the pancreatic ribonuclease family, RNase A has garnered significant attention due to its implications in various biological processes and its potential therapeutic applications, including anti-cancer and antiviral treatments. The development of recombinant RNase A has enabled researchers to produce the enzyme in a more controlled and efficient manner, allowing for the study of its structure-function relationships and mechanisms of action in detail. Advances in genetic engineering and protein purification techniques have facilitated the production of RNase A with specific mutations or modifications, enhancing its stability, activity, or specificity. Additionally, recombinant RNase A can serve as a model for understanding ribonuclease function and enzyme engineering. As research continues to explore the various applications of RNase A, including its use in targeted RNA interference and as a tool for RNA processing, the enzyme remains a focal point for continued investigation in enzymology, biotechnology, and therapeutic development.
