Analytical Data
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Gene name
TINF2
- Application
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Alternative Names
TINF2;TIN2;TERF1-interacting nuclear factor 2
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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
Q9BSI4
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Expression Region
2-451aa
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AA Sequence
ATPLVAGPA ALRFAAAASW QVVRGRCVEH FPRVLEFLRS LRAVAPGLVR YRHHERLCMG LKAKVVVELI LQGRPWAQVL KALNHHFPES GPIVRDPKAT KQDLRKILEA QETFYQQVKQ LSEAPVDLAS KLQELEQEYG EPFLAAMEKL LFEYLCQLEK ALPTPQAQQL QDVLSWMQPG VSITSSLAWR QYGVDMGWLL PECSVTDSVN LAEPMEQNPP QQQRLALHNP LPKAKPGTHL PQGPSSRTHP EPLAGRHFNL APLGRRRVQS QWASTRGGHK ERPTVMLFPF RNLGSPTQVI SKPESKEEHA IYTADLAMGT RAASTGKSKS PCQTLGGRAL KENPVDLPAT EQKENCLDCY MDPLRLSLLP PRARKPVCPP SLCSSVITIG DLVLDSDEEE NGQGEGKESL ENYQKTKFDT LIPTLCEYLP PSGHGAIPVS SCDCRDSSRP L
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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
TINF2, or Telomerase Interacting Protein 2, is a crucial component of the telomere complex, playing a vital role in maintaining telomere stability and integrity. Telomeres, the protective caps at the ends of chromosomes, are essential for genomic stability, and their dysfunction is associated with aging, cancer, and various genetic disorders. Research into TINF2 has gained momentum due to its involvement in disorders like dyskeratosis congenita, which is characterized by premature aging and increased cancer risk linked to telomere shortening. Recent studies have highlighted the interaction of TINF2 with other telomeric proteins and telomerase, suggesting its significant role in telomere length regulation and cellular lifespan. Understanding the structural and functional properties of TINF2 through recombinant protein studies is pivotal for elucidating its mechanism of action within the telomere complex. This research aims not only to clarify the molecular underpinnings of telomere maintenance but also to explore potential therapeutic targets for age-related diseases and cancer, where telomere dysfunction is a critical factor. As such, the study of TINF2 recombinant proteins opens avenues for developing strategies to manipulate telomere biology, with promising implications for improving healthspan and providing novel insights into tumorigenesis.











