| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DSP |
| Uniprot No | P15924 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 78-300aa |
| 氨基酸序列 | CSDCLMRAELIVQPELKYGDGIQLTRSRELDECFAQANDQMEILDSLIREMRQMGQPCDAYQKRLLQLQEQMRALYKAISVPRVRRASSKGGGGYTCQSGSGWDEFTKHVTSECLGWMRQQRAEMDMVAWGVDLASVEQHINSHRGIHNSIGDYRWQLDKIKADLREKSAIYQLEEEYENLLKASFERMDHLRQLQNIIQATSREIMWINDCEEEELLYDWSD |
| 预测分子量 | 42.1 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DSP(双特异性磷酸酶)重组蛋白的3篇参考文献示例，内容为虚构概括，仅供参考：
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1. **文献名称**：*Expression and Purification of Recombinant DSP-1 in E. coli for Functional Studies*
**作者**：Smith J. et al.
**摘要**：研究利用大肠杆菌系统高效表达DSP-1重组蛋白，优化了诱导条件和纯化流程，获得高活性蛋白，并验证其在MAPK信号通路中的去磷酸化功能。
2. **文献名称**：*Structural Insights into DSP-2 Catalytic Mechanism via Crystallography*
**作者**：Chen L. et al.
**摘要**：通过X射线晶体学解析DSP-2重组蛋白的三维结构，揭示了其底物结合口袋的构象变化，为设计特异性抑制剂提供了结构基础。
3. **文献名称**：*High-Yield Production of DSP-3 in Yeast for Therapeutic Applications*
**作者**：Wang Y. et al.
**摘要**：开发了一种基于毕赤酵母的重组DSP-3表达系统，实现大规模生产，并证明其在细胞炎症模型中的潜在治疗作用。
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(注：以上文献为模拟生成，实际文献需通过学术数据库检索。)
**Background of DSP Recombinant Proteins**
Desmoplakin (DSP) is a critical component of desmosomes, specialized intercellular junctions that maintain tissue integrity by anchoring intermediate filaments to the plasma membrane in epithelial and cardiac cells. As a member of the plakin protein family, DSP plays a pivotal role in cell-cell adhesion, mechanical stability, and signal transduction. Mutations in the *DSP* gene are linked to severe disorders, including arrhythmogenic cardiomyopathy (ACM) and skin fragility syndromes, highlighting its biological significance.
Recombinant DSP proteins are engineered versions of the native protein, produced via heterologous expression systems (e.g., bacterial, mammalian, or insect cells). These proteins retain functional domains, such as the N-terminal plakin domain for cytoskeletal interactions and the C-terminal rod domain for dimerization, enabling researchers to study DSP’s structure-function relationships *in vitro*.
The development of DSP recombinant proteins addresses challenges in studying endogenous DSP, which is large (>260 kDa), difficult to purify, and low in abundance. Recombinant technology allows scalable production, post-translational modifications (e.g., phosphorylation), and customization (e.g., tagging for detection). Applications span mechanistic studies of desmosome assembly, disease modeling (e.g., ACM-associated mutations), and drug screening for therapies targeting cell adhesion defects.
Furthermore, DSP recombinant proteins serve as antigens for antibody development, aiding diagnostics for DSP-related pathologies. Their use in structural biology (e.g., cryo-EM) has advanced understanding of desmosomal architecture. As research shifts toward personalized medicine, recombinant DSP tools are vital for exploring genotype-phenotype correlations and potential gene therapies.
In summary, DSP recombinant proteins are indispensable for dissecting desmosome biology, elucidating disease mechanisms, and developing targeted interventions, bridging gaps between basic research and clinical translation.
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