Analytical Data
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Gene name
HRNR
- Application
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Alternative Names
S100a18
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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
Q86YZ3
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Expression Region
Glu2685~Gln2850
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Molecular Weight
23kDa
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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
HRNR (Hematopoietic Cell-specific Ribonuclease) is a protein that has gained interest in recent years due to its unique properties and potential therapeutic applications. Initially identified in hematopoietic cells, HRNR is known for its ribonuclease activity, which allows it to selectively degrade RNA molecules. This characteristic positions HRNR as a candidate for applications in RNA-based therapeutics and molecular biology. Furthermore, its role in various cellular functions, including stress response and apoptosis, highlights its significance in understanding cellular mechanisms and disease progression. Researchers have been exploring the recombinant production of HRNR to study its biochemical properties, structure-function relationships, and interactions with other cellular components. The development of recombinant HRNR not only facilitates detailed investigations into its enzymatic activities but also enhances its potential utility in biomedicine, particularly in designing targeted therapies for conditions like cancer and viral infections, where controlling RNA levels can lead to therapeutic advantages. Investigations into HRNR's mechanisms, stability, and efficacy in different contexts continue to shed light on its promises in advancing medical science and therapeutic strategies.
