Analytical Data
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Gene name
TERF2
- Application
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Alternative Names
TRBF2; TRF2
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Species
Human
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Source
E. coli
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15554-3
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Expression Region
A2-N542
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Protein Length
Partial
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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
TERF2, or Telomeric Repeat-binding Factor 2, is a crucial protein involved in the maintenance of telomeres, the protective structures at the ends of eukaryotic chromosomes. Telomeres play a significant role in cellular aging and stability, with TERF2 being integral to the formation of the shelterin complex that protects telomeres from damage and prevents them from being recognized as double-strand breaks. Research has shown that dysregulation of TERF2 can lead to telomere dysfunction, which is implicated in various diseases, including cancer and age-related disorders. The study of recombinant TERF2 protein has been pivotal in understanding its structural and functional properties, as well as its interactions with other shelterin components. Using techniques such as protein expression systems and purification processes, researchers can analyze the biochemical properties of TERF2, elucidating its role in telomere maintenance and protection. Furthermore, investigating the effects of TERF2 mutations provides insights into the mechanisms behind telomere-related pathologies. The ongoing research on recombinant TERF2 not only enhances our understanding of telomere biology but also holds potential for developing therapeutic strategies aimed at ameliorating diseases associated with telomere dysfunction.
