| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TBCB |
| Uniprot No | Q99426 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-244aa |
| 氨基酸序列 | MEVTGVSAPT VTVFISSSLN TFRSEKRYSR SLTIAEFKCK LELLVGSPAS CMELELYGVD DKFYSKLDQE DALLGSYPVD DGCRIHVIDH SGARLGEYED VSRVEKYTIS QEAYDQRQDT VRSFLKRSKL GRYNEEERAQ QEAEAAQRLA EEKAQASSIP VGSRCEVRAA GQSPRRGTVM YVGLTDFKPG YWIGVRYDEP LGKNDGSVNG KRYFECQAKY GAFVKPAVVT VGDFPEEDYG LDEI |
| 预测分子量 | kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于TBCB(Tubulin Folding Cofactor B)重组蛋白的示例参考文献(注：以下内容为模拟示例，非真实文献)：
1. **文献名称**：*Structural and functional analysis of TBCB in tubulin dimer assembly*
**作者**：Martin, R. et al.
**摘要**：本研究利用重组TBCB蛋白，结合X射线晶体学分析其三维结构，揭示了TBCB与β-微管蛋白的相互作用机制，并证明其通过调控微管蛋白折叠参与细胞骨架的动态平衡。
2. **文献名称**：*Recombinant TBCB enhances microtubule stability in neurodegenerative models*
**作者**：Smith, J. & Lee, K.
**摘要**：通过体外表达重组TBCB蛋白，作者发现其能够减少Tau蛋白异常磷酸化引起的微管解聚，在阿尔茨海默病细胞模型中显示出保护微管网络的潜力。
3. **文献名称**：*TBCB knockdown and recombinant rescue in mitotic spindle formation*
**作者**：Yen, H. et al.
**摘要**：利用CRISPR技术敲低TBCB导致细胞分裂异常，而外源性重组TBCB蛋白可恢复纺锤体微管的正常组装，证实了TBCB在有丝分裂中的关键作用。
4. **文献名称**：*High-yield production of recombinant TBCB in E. coli and its biochemical characterization*
**作者**：Garcia, M. et al.
**摘要**：报道了一种高效的大肠杆菌表达系统，用于生产可溶性重组TBCB蛋白，并通过体外微管聚合实验验证其生物活性，为大规模研究提供技术基础。
(注：以上文献为示例，实际引用需查询真实数据库如PubMed、Google Scholar等。)
**Background of TBCB Recombinant Protein**
TBCB (Tubulin Folding Cofactor B) is a critical member of the tubulin-specific chaperone family, which facilitates the proper folding and assembly of α-tubulin into functional heterodimers with β-tubulin. These heterodimers serve as building blocks for microtubules, dynamic cytoskeletal structures essential for cell division, intracellular transport, and maintenance of cell shape. TBCB works in concert with other cofactors (e.g., TBCE, TBCA, and Arl2) to ensure the correct folding and stability of α-tubulin, preventing its aggregation or degradation.
Recombinant TBCB protein is engineered using genetic engineering techniques, where the *TBCB* gene is cloned into expression vectors and produced in host systems like *E. coli*, yeast, or mammalian cells. This allows large-scale production of purified, biologically active TBCB for research and therapeutic applications. Its recombinant form retains the ability to bind and stabilize α-tubulin, making it invaluable for studying microtubule dynamics, neurodevelopmental disorders, and diseases linked to tubulin dysregulation, such as cancer and neurodegenerative conditions.
Research utilizing TBCB recombinant protein has shed light on its role in microtubule-related pathologies. For instance, mutations in tubulin chaperones are associated with microcephaly and motor neuron diseases. Additionally, TBCB is implicated in cancer progression, as altered microtubule stability affects cell division and metastasis. The recombinant protein also serves as a tool for drug screening, particularly for compounds targeting microtubule-modulating pathways.
Despite its utility, producing functional TBCB recombinant protein requires optimization of expression conditions to address solubility and post-translational modification challenges. Advances in structural biology and proteomics continue to refine its applications, positioning TBCB as a pivotal target for both basic research and therapeutic development.
×
