Analytical Data
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Gene name
TFPT
- Application
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Alternative Names
Amida; INO80 complex subunit F; INO80F; Protein FB1; TCF3 (E2A) fusion partner (in childhood Leukemia); TCF3 fusion partner; TFPT; TFPT_HUMAN
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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
P0C1Z6
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Expression Region
1-253 aa
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AA Sequence
MELEQREGTM AAVGFEEFSA PPGSELALPP LFGGHILESE LETEVEFVSG GLGGSGLRER DEEEEAARGR RRRQRELNRR KYQALGRRCR EIEQVNERVL NRLHQVQRIT RRLQQERRFL MRVLDSYGDD YRASQFTIVL EDEGSQGTDA PTPGNAENEP PEKETLSPPR RTPAPPEPGS PAPGEGPSGR KRRRVPRDGR RAGNALTPEL APVQIKVEED FGFEADEALD SSWVSRGPDK LLPYPTLASP ASD
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Molecular Weight
28.2 kDa
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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
The research on TFPT (Titanium-Functionalized Protein Technology) recombinant proteins is grounded in the growing need for advanced biomaterials and therapeutic agents in various biomedical applications. TFPT leverages the unique properties of titanium, a biocompatible and corrosion-resistant metal, by incorporating it into protein structures to enhance their stability, functionality, and interaction with biological systems. This innovative approach aims to overcome the limitations of traditional protein-based therapies, such as instability and limited solubility. By utilizing recombinant DNA technology, researchers can produce TFPT in controlled environments, ensuring high purity and consistency. The integration of titanium also opens avenues for targeted drug delivery and improved bioactivity, which is crucial for applications in tissue engineering and regenerative medicine. Furthermore, as the demand for sustainable and efficient production methods grows, TFPT presents a promising solution by potentially reducing the environmental impact associated with conventional protein production processes. Consequently, ongoing research in this area focuses on optimizing the synthesis and functional properties of TFPT recombinant proteins, examining their interactions with cells and tissues, and evaluating their clinical potential across various therapeutic domains.
