| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TBCA |
| Uniprot No | O75347 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-108aa |
| 氨基酸序列 | ADPRVRQIK IKTGVVKRLV KEKVMYEKEA KQQEEKIEKM RAEDGENYDI KKQAEILQES RMMIPDCQRR LEAAYLDLQR ILENEKDLEE AEEYKEARLV LDSVKLEA |
| 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3篇关于TBCA(微管蛋白伴侣蛋白A)重组蛋白研究的参考文献概览：
1. **文献名称**：Expression and purification of recombinant human tubulin-specific chaperone A (TBCA) in Escherichia coli
**作者**：Lopez-Fanarraga et al.
**摘要**：报道了在大肠杆菌中高效表达人源TBCA重组蛋白的方法，优化了可溶性表达条件，并通过亲和层析纯化获得高纯度蛋白，验证其促进α-微管蛋白正确折叠的功能。
2. **文献名称**：Structural insights into tubulin folding co-chaperones: TBCA and TBCB form a novel heterodimer
**作者**：Serna et al.
**摘要**：解析了TBCA与TBCB重组蛋白的复合物晶体结构，揭示二者协同调控β-微管蛋白折叠的分子机制，为微管组装障碍相关疾病研究提供结构基础。
3. **文献名称**：Functional characterization of plant TBCA homolog in Arabidopsis thaliana
**作者**：Hamada et al.
**摘要**：克隆拟南芥TBCA同源基因并实现重组表达，证明其在植物细胞中同样具有保守的微管蛋白折叠功能，敲除突变体表现出微管组织异常表型。
注：以上为示例性文献框架，实际文献需通过PubMed/Web of Science检索确认。建议使用关键词："TBCA recombinant protein"、"tubulin chaperone expression" 进行精确检索，优先选择近5年发表的分子机制或结构生物学相关研究。
Tubulin-specific chaperone A (TBCA) is a critical component of the tubulin folding pathway, essential for the proper assembly and stability of α- and β-tubulin heterodimers, the building blocks of microtubules. Microtubules are dynamic cytoskeletal structures involved in cell division, intracellular transport, and maintenance of cell shape. Newly synthesized α- and β-tubulin monomers require a series of chaperones, including TBCA, to guide their folding, prevent aggregation, and facilitate heterodimer formation. TBCA specifically interacts with β-tubulin, working in concert with other chaperones (TBCB, TBCC, TBCD, and TBEE) to ensure structural fidelity before tubulin incorporation into microtubules.
Recombinant TBCA protein is produced using genetic engineering techniques, typically through expression in bacterial systems like *E. coli*. This involves cloning the TBCA gene into expression vectors, inducing protein synthesis, and purifying the protein via affinity chromatography. Recombinant production allows researchers to obtain large quantities of highly pure TBCA for functional studies, overcoming limitations of low endogenous concentrations in native tissues.
The availability of recombinant TBCA has advanced research on microtubule biology and associated pathologies. It enables detailed structural analyses (e.g., X-ray crystallography), in vitro reconstitution of tubulin folding pathways, and investigations into diseases linked to tubulin dysregulation, such as neurodegenerative disorders and cancer. Additionally, recombinant TBCA serves as a tool for screening small molecules that modulate tubulin dynamics, with potential therapeutic applications. Its role in maintaining tubulin homeostasis also makes it relevant for studying drug resistance mechanisms in microtubule-targeting chemotherapies.
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