Analytical Data
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Gene name
RENBP
- Application
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Alternative Names
RBP; RNBP; AGE; N-Acylglucosamine 2-Epimerase; GlcNAc 2-Epimerase; N-Acetyl-D-Glucosamine 2-Epimerase
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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
P51606
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Expression Region
Met1~Gln254
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Molecular Weight
33kDa
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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
RENBP (Reovirus Early Nucleotide Binding Protein) is a crucial protein involved in the life cycle of reoviruses, which are non-enveloped viruses known to infect a wide range of hosts, including humans. The study of RENBP is essential due to its role in viral replication and pathogenesis. Researchers have focused on understanding the molecular mechanisms by which RENBP interacts with viral RNA and host cellular machinery. This involves examining how RENBP facilitates the transcription and translation of viral genes, thus enabling the virus to propagate effectively within host cells. Additionally, RENBP has gained attention in the context of therapeutic developments, as targeting this protein could provide novel strategies for antiviral treatments. The increasing interest in virology, coupled with recent advancements in molecular biology techniques, has propelled RENBP research, making it a significant focal point for understanding viral behavior and developing countermeasures against reovirus infections. Given the potential implications of this research for public health, particularly with respect to emerging viral diseases, continued investigation into RENBP's structure, function, and interactions is imperative.
