Analytical Data
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Gene name
TFAM
- Application
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Alternative Names
MtTF1; TCF6; TCF6L2; mtTFA; Mitochondrial transcription factor 1; Transcription factor 6-like 2
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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 95% as determined by SDS-PAGE.
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Uniprot
Q00059
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Expression Region
Ser43~Cys246
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Molecular Weight
30kDa
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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
Transcription Factor A (TFAM) is a nuclear-encoded mitochondrial protein that plays a crucial role in mitochondrial DNA (mtDNA) transcription and replication. It is pivotal for maintaining mitochondrial function, which is essential for cellular energy production through oxidative phosphorylation. TFAM binds to mtDNA, facilitating the compaction of the mitochondrial genome and regulating its transcription. Research has shown that alterations in TFAM expression are linked to various mitochondrial disorders and age-related diseases, including Alzheimer's and Parkinson's disease. Moreover, the relationship between TFAM and mitochondrial biogenesis highlights its importance in metabolic diseases, as TFAM influences the production of new mitochondria in response to cellular energy demands. Recent studies have also explored TFAM's potential as a therapeutic target for enhancing mitochondrial function in aging and metabolic dysfunction. The emergence of TFAM reconstitution experiments using recombinantly produced proteins has provided insights into its mechanism of action and its role in the pathophysiology of mitochondrial diseases. Therefore, understanding TFAM’s structure and function through recombinant protein studies is crucial for elucidating its contributions to mitochondrial health and developing innovative therapeutic strategies.
