Analytical Data
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Gene name
Rnase 3
- Application
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Alternative Names
Rnase-A3; RnaseA3; ECP; RNS3; Ribonuclease,RNase A Family 3; Eosinophil Cationic Protein
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
O35290
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Expression Region
Phe34~Val150
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Molecular Weight
17kDa
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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
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Protein Description
Rnase 3, also known as Dicer, is a crucial ribonuclease enzyme involved in the RNA interference (RNAi) pathway, which plays a pivotal role in the regulation of gene expression and the processing of microRNAs (miRNAs). This enzyme is responsible for the cleavage of double-stranded RNA (dsRNA) into small interfering RNA (siRNA) and miRNA, essential for post-transcriptional gene silencing. The ability of Rnase 3 to modulate gene expression has made it a significant target for therapeutic applications, particularly in cancer and viral infections, where aberrant miRNA levels can contribute to disease progression. Moreover, the study of recombinant Rnase 3 proteins offers insights into its structure-function relationships, enzymatic mechanisms, and potential for biotechnological applications. Understanding the characteristics and functions of Rnase 3 at a molecular level can lead to novel strategies for engineered RNA-based therapies. Researchers have been increasingly focused on developing recombinant Rnase 3 variants with enhanced properties, such as increased stability and specificity, which could improve their utility in research and clinical settings. Therefore, the investigation of Rnase 3 recombinant proteins not only enhances our comprehension of RNA metabolism but also propels the advancement of RNA-targeted therapeutics.
