Analytical Data
-
Gene name
TINF2
- Application
-
Alternative Names
TIN2; TRF1-interacting nuclear protein 2
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9BSI4
-
Expression Region
Ala2~Leu451
-
Molecular Weight
54kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
TINF2, a component of the telomere shelterin complex, plays a critical role in telomere maintenance and chromosome stability. Disruptions in TINF2 function have been linked to various pathological conditions, including dyskeratosis congenita and other age-related diseases. Recent studies have highlighted the importance of TINF2 as a potential therapeutic target, emphasizing the need for a deeper understanding of its structural and functional properties. The research on TINF2 recombinant protein has emerged as a pivotal avenue to elucidate its mechanisms of action and interactions with other telomeric proteins. By producing TINF2 in a recombinant form, researchers can explore its biophysical properties, define its role in telomere protection, and assess how mutations impact its function. Additionally, studying TINF2 in a controlled setting allows for the potential development of novel therapies aimed at restoring telomere integrity in diseases associated with telomeric dysfunction. This background sets the stage for ongoing investigations into TINF2, aiming to bridge the gap between basic research and clinical applications, ultimately contributing to our understanding of cellular aging and malignancies linked to telomere biology.
