| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DUSP12 |
| Uniprot No | Q9UNI6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-340aa |
| 氨基酸序列 | MLEAPGPSDGCELSNPSASRVSCAGQMLEVQPGLYFGGAAAVAEPDHLREAGITAVLTVDSEEPSFKAGPGVEDLWRLFVPALDKPETDLLSHLDRCVAFIGQARAEGRAVLVHCHAGVSRSVAIITAFLMKTDQLPFEKAYEKLQILKPEAKMNEGFEWQLKLYQAMGYEVDTSSAIYKQYRLQKVTEKYPELQNLPQELFAVDPTTVSQGLKDEVLYKCRKCRRSLFRSSSILDHREGSGPIAFAHKRMTPSSMLTTGRQAQCTSYFIEPVQWMESALLGVMDGQLLCPKCSAKLGSFNWYGEQCSCGRWITPAFQIHKNRVDEMKILPVLGSQTGKI |
| 分子量 | 63.03 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人DUSP12蛋白的模拟参考文献示例(注：部分文献为假设性描述，实际引用请核实)：
1. **"Expression and Characterization of Recombinant Human DUSP12 in Escherichia coli"**
- 作者：Zhang Y, Liu X, Chen J
- 摘要：研究报道了通过大肠杆菌表达系统成功表达并纯化重组人DUSP12蛋白，分析其体外磷酸酶活性及对MAPK信号通路的调控作用。
2. **"DUSP12 Regulates Cellular Stress Responses via p38 MAPK Dephosphorylation"**
- 作者：Lin Q, Wang H, Santos SD
- 摘要：揭示了重组DUSP12蛋白在细胞氧化应激中的功能，证明其通过特异性去磷酸化p38 MAPK调控细胞凋亡和存活。
3. **"Structural Insights into the Catalytic Mechanism of DUSP12 Phosphatase"**
- 作者：Kim T, Park S, Lee MJ
- 摘要：利用重组人DUSP12蛋白进行晶体结构解析，阐明其催化底物识别及双特异性磷酸酶活性机制。
4. **"DUSP12 as a Potential Therapeutic Target in Hepatocellular Carcinoma"**
- 作者：Wang R, Li F, Zhou Y
- 摘要：通过体外实验发现，重组DUSP12蛋白的高表达抑制肝癌细胞增殖，可能与ERK信号通路失活相关。
建议通过PubMed、Web of Science等平台以“recombinant DUSP12”“DUSP12 phosphatase function”为关键词检索最新文献。
**Background of Recombinant Human DUSP12 Protein**
Dual-specificity phosphatase 12 (DUSP12), also known as YVH1. is a member of the dual-specificity phosphatase (DSP) family, which regulates mitogen-activated protein kinase (MAPK) signaling pathways by dephosphorylating both tyrosine and serine/threonine residues. Unlike classical protein tyrosine phosphatases (PTPs), DSPs exhibit broader substrate specificity. DUSP12 contains an N-terminal domain with potential regulatory roles and a C-terminal catalytic phosphatase domain. It is implicated in diverse cellular processes, including cell cycle progression, stress responses, and apoptosis.
Recombinant human DUSP12 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to ensure high purity and activity for experimental applications. Its production enables mechanistic studies to elucidate DUSP12’s biological functions, particularly its interactions with MAPKs (e.g., ERK, JNK) and other substrates. Research suggests DUSP12 may play roles in cancer, immune regulation, and metabolic diseases, though its precise mechanisms remain under investigation.
Interest in DUSP12 also stems from its unique structural features, such as the zinc-binding domain in the N-terminus, which may influence substrate recognition or protein stability. Additionally, unlike some DSPs, DUSP12 lacks a MAPK-binding docking motif, hinting at distinct regulatory mechanisms. Recombinant DUSP12 is widely used in *in vitro* assays, structural studies, and drug discovery efforts targeting phosphatase-mediated signaling pathways. Its study contributes to understanding DSP family diversity and potential therapeutic applications in diseases linked to aberrant kinase signaling.
(Word count: 247)
×
