Analytical Data
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Gene name
I614N,L616I
- Application
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Alternative Names
Taq polymerase 1
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Species
Thermus aquaticus
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P19821
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Expression Region
293-832aa(I614,L616I)
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Molecular Weight
61.0 kDa
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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
The study of recombinant proteins, particularly I614N and L616I variants, has garnered significant interest in the field of molecular biology and biotechnology due to their potential implications in virology and bioengineering. These specific mutations in viral proteins, often linked to increased viral fitness or altered host interactions, provide valuable insights into the mechanisms of pathogenicity and resistance. The I614N variant has been associated with enhanced viral replication and stability, while L616I may influence the protein's structural conformation and interactions with host factors. Understanding these variants through recombinant protein expression systems enables researchers to elucidate their biological roles and assess their impacts on viral lifecycle and immune evasion. Additionally, characterizing these mutations may contribute to the development of targeted therapeutics and vaccines, as insights into the structure-function relationships of these proteins can reveal new avenues for intervention. Furthermore, the exploration of I614N and L616I mutations is critical in the context of ongoing viral evolution, especially in response to selective pressures from antiviral treatments and host immune responses, making them key subjects for ongoing research in public health and infectious disease management. Thus, the investigation of these recombinant proteins not only deepens our understanding of viral biology but also enhances our capacity to respond to emerging viral threats.
