Analytical Data
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Gene name
TEF
- Application
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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
Q10587
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Expression Region
Gly7~Leu303
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Molecular Weight
44kDa
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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
TEF (Transcription Enhancer Factor) recombinant proteins are crucial in molecular biology research, particularly in the study of gene regulation and transcriptional mechanisms. TEF proteins play significant roles in the expression of genes by interacting with various transcription factors and enhancers, influencing cellular processes such as growth, differentiation, and response to environmental signals. The recombinant production of TEF proteins allows researchers to obtain large quantities of these proteins for in vitro studies, enabling detailed investigations into their structural and functional characteristics. Researchers utilize techniques like recombinant DNA technology to express TEF proteins in host systems, such as bacteria or yeast, which provide a more accessible means of studying their biochemical properties and interactions. These studies contribute to our understanding of complex regulatory networks in the cell, and highlight the potential implications for understanding diseases associated with dysregulated gene expression, such as cancer and genetic disorders. The exploration of TEF recombinant proteins continues to be a vibrant area of research, with applications in therapeutic development and synthetic biology, underscoring the importance of these proteins in both basic and applied sciences.
