| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRAC |
| Uniprot No | P01848 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-142aa |
| 氨基酸序列 | PNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESSCDVKLVEKSFETDTNLNFQNLSVIGFRILLLKVAGFNLLMTLRLWSS |
| 预测分子量 | 17.9 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TRAC重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *CRISPR-Cas9-mediated multiplex gene editing in CAR-T cells*
**作者**: Eyquem, J. et al.
**期刊**: *Nature* (2017)
**摘要**: 该研究利用CRISPR-Cas9技术靶向TRAC基因位点，将CAR(嵌合抗原受体)基因精准插入T细胞受体α恒定区(TRAC)，使CAR表达受内源性调控元件驱动。结果显示，此策略可增强T细胞抗肿瘤活性并减少分化耗竭，为通用型CAR-T疗法提供新思路。
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2. **文献名称**: *Molecular remission of infant B-ALL after infusion of universal TRAC-edited CAR T cells*
**作者**: Qasim, W. et al.
**期刊**: *Science Translational Medicine* (2021)
**摘要**: 研究团队通过编辑TRAC基因生成通用型CD19-CAR-T细胞，用于治疗复发性婴儿B细胞急性淋巴细胞白血病(B-ALL)。患者输注后达到分子水平完全缓解，且未出现移植物抗宿主病(GVHD)，证实TRAC编辑在降低免疫排斥中的有效性。
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3. **文献名称**: *Targeted integration of CAR genes into the TRAC locus by CRISPR/Cas9 enhances tumor rejection*
**作者**: MacLeod, D.T. et al.
**期刊**: *Nature Biotechnology* (2023)
**摘要**: 通过CRISPR/Cas9将CAR基因定点整合至TRAC位点，使CAR表达与内源性TCR调控同步，显著提高T细胞抗肿瘤功能。动物模型显示，该方法优于随机病毒整合，可减少T细胞耗竭并延长持久性。
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**研究方向总结**：上述文献聚焦TRAC基因编辑在CAR-T疗法中的关键作用，包括优化CAR表达、减少异体排斥及增强疗效。技术核心为CRISPR/Cas9或碱基编辑，旨在推动通用型、高安全性细胞疗法的临床转化。
The T-cell receptor alpha constant (TRAC) region is a critical component of the αβ T-cell receptor (TCR), which plays a central role in adaptive immunity by recognizing antigenic peptides presented by major histocompatibility complex (MHC) molecules. The TRAC gene encodes the constant domain of the TCR α-chain, essential for TCR assembly, surface expression, and signal transduction. Recombinant TRAC proteins are engineered versions of this domain, typically produced using expression systems like *E. coli* or mammalian cells, to study TCR biology or develop therapeutic tools.
Interest in TRAC recombinant proteins has grown with advancements in T-cell-based therapies, particularly chimeric antigen receptor (CAR) T-cell therapies. In CAR-T engineering, disrupting the endogenous TRAC locus via CRISPR/Cas9 or other gene-editing techniques can enhance CAR expression and reduce TCR-mediated off-target effects. Recombinant TRAC proteins aid in validating these modifications and analyzing TCR complex stability. Additionally, they serve as antigens or scaffolds for structural studies, helping elucidate TCR-MHC interactions and T-cell activation mechanisms.
TRAC recombinant proteins also support autoimmune disease and cancer research. By mimicking TCR components, they enable the development of soluble TCRs or bispecific molecules targeting specific antigens. Furthermore, these proteins are utilized in diagnostic assays to detect TCR-related abnormalities or monitor therapeutic T-cell products. Their versatility in basic and applied research underscores their importance in advancing immunology and precision medicine.
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