Analytical Data
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Gene name
TFIIB
- Application
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Alternative Names
General transcription factor TFIIBS300-II
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q00403
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Expression Region
1-316aa
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Molecular Weight
50.8 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
Related Products
Protein Description
TFIIB, or Transcription Factor IIB, plays a crucial role in the initiation of transcription by RNA polymerase II, acting as a bridge between the polymerase and the promoter region of genes. Given its essential function in transcription regulation, TFIIB has garnered significant attention in the field of molecular biology and biochemistry. Research on recombinant TFIIB proteins has advanced our understanding of the molecular mechanisms underlying gene expression. The ability to produce TFIIB recombinantly has enabled scientists to study its structure, interactions with other transcription factors, and its role in the formation of the pre-initiation complex during transcription. Moreover, investigations into the post-translational modifications of TFIIB, such as phosphorylation and acetylation, reveal how these modifications can affect its function and stability, further emphasizing its regulatory importance. As transcriptional dysregulation is implicated in various diseases, including cancer, insights gained from TFIIB research hold the potential for therapeutic advancements. Overall, the study of recombinant TFIIB proteins not only enhances our foundational knowledge of transcription biology but also opens up new avenues for clinical applications.
