| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DUSP13 |
| Uniprot No | Q9UII6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-198aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMDSLQK QDLRRPKIHG AVQASPYQPP TLASLQRLLW VRQAATLNHI DEVWPSLFLG DAYAARDKSK LIQLGITHVV NAAAGKFQVD TGAKFYRGMS LEYYGIEADD NPFFDLSVYF LPVARYIRAA LSVPQGRVLV HCAMGVSRSA TLVLAFLMIC ENMTLVEAIQ TVQAHRNICP NSGFLRQLQV LDNRLGRETG RF |
| 预测分子量 | 25 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DUSP13重组蛋白的3篇参考文献摘要概括：
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1. **文献名称**：*"Characterization of the Dual Specificity Phosphatase DUSP13B and Its Role in Apoptosis"*
**作者**：Li Y, et al.
**摘要**：通过原核系统表达重组DUSP13B蛋白，发现其通过去磷酸化调控p38 MAPK信号通路，抑制细胞凋亡，揭示其在应激反应中的潜在功能。
2. **文献名称**：*"Recombinant DUSP13 Catalytic Domain: Structural and Functional Analysis"*
**作者**：Chen X, et al.
**摘要**：解析DUSP13催化结构域的重组蛋白晶体结构，证实其底物特异性依赖于保守的活性位点残基，为设计靶向抑制剂提供结构基础。
3. **文献名称**：*"DUSP13 Regulates Skeletal Muscle Development via ERK Signaling in Transgenic Mice"*
**作者**：Wang H, et al.
**摘要**：利用重组DUSP13蛋白进行体外实验，结合转基因模型证明其通过负调控ERK磷酸化参与肌肉分化，提示其在发育疾病中的治疗价值。
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注：以上文献为模拟概括，实际研究需通过数据库(PubMed、Web of Science)检索具体论文。建议补充关键词"DUSP13 recombinant protein expression/function"进一步筛选。
DUSP13 (Dual Specificity Phosphatase 13), also known as MDSP or TMDP, is a member of the dual-specificity phosphatase family, which regulates mitogen-activated protein kinase (MAPK) signaling pathways by dephosphorylating both phosphotyrosine and phosphoserine/phosphothreonine residues. It belongs to the atypical DUSP subfamily due to its unique structural features, including a conserved C-terminal catalytic phosphatase domain and a divergent N-terminal region lacking MAPK-binding motifs found in typical MAPK phosphatases (MKPs).
DUSP13 exists in two splice variants: DUSP13A (expressed predominantly in skeletal muscle and heart) and DUSP13B (testis-specific). Its recombinant form is typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems to study its enzymatic activity, substrate specificity, and interactions. Recombinant DUSP13 exhibits selectivity toward stress-activated MAPKs, particularly p38 and JNK, implicating its role in cellular stress responses, apoptosis, and muscle differentiation.
Research highlights its involvement in pathophysiological contexts, such as cancer, metabolic disorders, and inflammation. For instance, DUSP13 overexpression in certain cancers modulates chemoresistance by altering MAPK-driven survival pathways. Structural studies using recombinant DUSP13 have revealed insights into its catalytic mechanism and regulatory regions, enabling the design of mutants (e.g., catalytically inactive Cys-to-Ser variants) for functional assays.
Recombinant DUSP13 is also explored for therapeutic targeting, as small-molecule inhibitors or activators could fine-tune MAPK signaling in diseases with dysregulated stress responses. Further studies aim to clarify its tissue-specific roles and post-translational modifications, leveraging recombinant protein tools to advance mechanistic and translational discoveries.
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