Analytical Data
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Gene name
RNASE3
- Application
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Alternative Names
RNASE3;ECP;RNS3;Eosinophil cationic Protein
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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
P12724
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Expression Region
1-160aa
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AA Sequence
MVPKLFTSQICLLLLLGLMGVEGSLHARPPQFTRAQWFAIQHISLNPPRCTIAMRAINNYRWRCKNQNTFLRTTFANVVNVCGNQSIRCPHNRTLNNCHRSRFRVPLLHCDLINPGAQNISNCTYADRPGRRFYVVACDNRDPRDSPRYPVVPVHLDTTI
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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
RNASE3, also known as eosinophil ribonuclease (Eosinophil cationic protein), is a member of the ribonuclease A superfamily and plays a crucial role in the immune response, particularly in allergic reactions and asthma. This protein, predominantly expressed in eosinophils, exhibits potent ribonucleolytic activity and has been implicated in the regulation of inflammation and apoptosis of target cells. Research on RNASE3 has gained considerable interest due to its involvement in various pathological conditions, including asthma, parasitic infections, and certain malignancies. The therapeutic potential of RNASE3 is significant, with studies exploring its use as a biomarker for eosinophilic disorders and its potential application in targeted therapies. Moreover, recombinant RNASE3 proteins are being investigated for their ability to induce apoptosis in cancer cells and modulate immune responses. Understanding the structure-function relationship of RNASE3 through recombinant techniques can provide insights into its biological activity and facilitate the development of novel therapeutic agents. As a result, the study of recombinant RNASE3 not only contributes to basic immunology but also holds promise for translational research in immunotherapy and precision medicine.
