Analytical Data
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Gene name
RNASE3
- 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 90% 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
34kDa
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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
Recombinant RNASE3, also known as eosinophil cationic protein (ECP), has garnered significant attention due to its potential therapeutic applications and its role in immune responses, particularly in allergic diseases and asthma. RNASE3 is primarily produced by eosinophils, a type of white blood cell that plays a crucial role in the body's defense against parasitic infections and in mediating allergic reactions. The protein exhibits ribonucleolytic activity, enabling it to degrade RNA, which is significant for its antimicrobial properties. This characteristic has spurred research into its use as an antiviral agent and in cancer therapy, where targeted RNA degradation could inhibit tumor growth. Moreover, understanding the structure-function relationship of RNASE3 is vital for engineering variants with enhanced activity or specificity. The production of recombinant RNASE3 allows for detailed studies of its biochemical properties and its interactions with other molecules in the immune system. This not only aids in elucidating the mechanisms underlying eosinophil-related pathologies but also facilitates the development of potential therapeutic interventions, providing insights into novel treatments for conditions such as asthma and other allergic diseases. Given the increasing incidence of such conditions globally, RNASE3 represents a promising avenue for future research and development.
