| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRY |
| Uniprot No | Q8GV05 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-106aa |
| 氨基酸序列 | MDNTDRRRRR KQHKIALHDS EEVSSIEWEF INMTEQEEDL IFRMYRLVGD RWDLIAGRVP GRQPEEIERY WIMRNSEGFA DKRRQLHSSS HKHTKPHRPR FSIYPS |
| 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篇与TRY重组蛋白相关的参考文献示例(内容为模拟概括，非真实文献)：
1. **《Functional analysis of TRY recombinant protein in Arabidopsis epidermal patterning》**
- 作者：Schellmann, S. et al.
- 摘要：本研究通过重组表达拟南芥TRY蛋白，验证其在表皮细胞分化中的抑制作用，证明TRY通过竞争性结合MYB转录因子调控毛状体发育。
2. **《Optimization of TRY recombinant protein expression in E. coli for structural studies》**
- 作者：Zhang, L. & Wang, H.
- 摘要：报道了TRY重组蛋白在大肠杆菌中的高效可溶性表达策略，并通过纯化与结晶分析其三维结构，为功能机制研究提供基础。
3. **《TRY recombinant protein application in crop trichome engineering》**
- 作者：Kumar, R. et al.
- 摘要：将TRY重组蛋白导入番茄中，显著减少叶片毛状体密度，证实其在作物抗虫性与抗旱性遗传改良中的潜在应用价值。
注：以上文献名为示例性概括，实际研究需参考具体数据库(如PubMed、CNKI)或学术平台。
**Background of TRY Recombinant Protein**
Recombinant TRY proteins are engineered versions of the TRY (TRANSPARENT TESTA YELLOW) protein, originally identified in plants like *Arabidopsis thaliana*. TRY is a key regulatory protein involved in the differentiation of epidermal cells, particularly influencing trichome (plant hair) development and patterning. It functions as a negative regulator, suppressing trichome initiation by interacting with other transcription factors, such as GLABRA1 (GL1), to modulate gene expression networks.
The production of recombinant TRY proteins leverages genetic engineering techniques, where the *TRY* gene is cloned into expression vectors and introduced into host systems (e.g., *E. coli*, yeast, or mammalian cells). This allows large-scale synthesis of the protein under controlled conditions. Recombinant TRY retains its biological activity, enabling researchers to study its structure-function relationships, binding partners, and regulatory mechanisms *in vitro*.
Applications of TRY recombinant proteins span plant biotechnology and synthetic biology. They are used to explore trichome development pathways, which have implications for crop improvement—enhancing pest resistance or stress tolerance by modifying epidermal features. Additionally, TRY serves as a model to study cell fate determination and transcriptional regulation. Challenges in its production include ensuring proper post-translational modifications and solubility, often addressed through codon optimization or fusion tags.
Overall, TRY recombinant proteins provide a versatile tool for dissecting plant developmental biology and advancing agricultural innovations, highlighting the intersection of molecular biology and biotechnological applications.
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