Analytical Data
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Gene name
TRF1
- Application
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Alternative Names
TRF; PIN2; TRBF1; TRF1; hTRF1-AS; t-TRF1; NIMA-interacting protein 2; TTAGGG repeat-binding factor 1; Telomeric protein Pin2/TRF1
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P54274
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Expression Region
Ile148~Lys428
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Molecular Weight
60kDa
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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
TRF1, or Telomeric Repeat-binding Factor 1, plays a crucial role in telomere maintenance and cellular aging. It is a key component of the shelterin complex, which protects telomeres from being recognized as sites of DNA damage and regulates telomere length by influencing telomerase activity and DNA replication processes. Research into TRF1 has gained momentum due to its implications in aging, cancer biology, and genomic stability. Dysregulation of TRF1 expression can lead to telomere dysfunction, contributing to the onset of various diseases, notably certain types of cancer where telomeres become critically short. Studies have focused on understanding the molecular mechanisms of TRF1's interactions with other shelterin components and its role in chromatin organization. The recombinant expression of TRF1 in various model systems has advanced our knowledge of its structure-function relationship and potential as a therapeutic target. Investigating TRF1's multidimensional role in telomere biology not only enhances our understanding of cellular senescence but also opens avenues for novel treatments that could harness telomere dynamics in cancer and age-related diseases. Overall, the study of TRF1 represents a critical intersection of molecular biology, oncology, and aging research, with promising implications for both fundamental biology and clinical applications.
