Analytical Data
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Gene name
TTF1
- Application
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Alternative Names
TTF1；Transcription termination factor 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15361
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Expression Region
12-232aa
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AA Sequence
TPVSDKKKKKCSIHKERPQKHSHEIFRDSSLVNEQSQITRRKKRKKDFQHLISSPLKKSRICDETANATSTLKKRKKRRYSALEVDEEAGVTVVLVDKENINNTPKHFRKDVDVVCVDMSIEQKLPRKPKTDKFQVLAKSHAHKSEALHSKVREKKNKKHQRKAASWESQRARDTLPQSESHQEESWLSVGPGGEITELPASAHKNKSKKKKKKSSNREYE
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Molecular Weight
29.6kDa
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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
TTF1, or thyroid transcription factor 1, is a pivotal transcription factor primarily known for its roles in the development and function of the thyroid gland, lungs, and central nervous system. Research into the recombinant forms of TTF1 has gained traction due to its implications in various physiological processes and diseases, including thyroid disorders, lung diseases, and some cancers. The ability to produce TTF1 as a recombinant protein allows researchers to investigate its structural properties, binding interactions, and regulatory mechanisms in detail. Moreover, studying TTF1 in a recombinant context facilitates the exploration of its potential as a therapeutic target or biomarker. Advances in protein engineering and expression systems have made it possible to generate TTF1 in sufficient quantities for functional assays, crystallography, and other biochemical studies. As the understanding of TTF1 expands, its role in gene regulation and cellular pathways continues to be elucidated, promising new insights into its contributions to health and disease.
