Analytical Data
-
基因名
TFPT
- Application
-
别名
Amida; INO80 complex subunit F; INO80F; Protein FB1; TCF3 (E2A) fusion partner (in childhood Leukemia); TCF3 fusion partner; TFPT; TFPT_HUMAN
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P0C1Z6
-
表达区间
1-253 aa
-
氨基酸序列
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
-
分子量
28.2 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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.
