| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PCMTD1 |
| Uniprot No | Q96MG8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-220aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMGGAVSAGEDNDDLIDNLKEAQYIRTERVEQAFRAIDRGDYYLEGYR DNAYKDLAWKHGNIHLSAPCIYSEVMEALKLQPGLSFLNLGSGTGYLSTM VGLILGPFGINHGIELHSDVVEYAKEKLESFIKNSDSFDKFEFCEPAFVV GNCLQIASDSHQYDRIYCGAGVQKDHENYMKILLKVGGILVMPIEDQLTQ IMRTGQNTWESKNILAVSFAPLV |
| 预测分子量 | 27 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PCMTD1重组蛋白的3篇参考文献的简要概括(基于假设性文献，实际文献需具体检索验证)：
1. **文献名称**: *Structural and functional characterization of PCMTD1 as a novel methyltransferase*
**作者**: Smith A, et al.
**摘要**: 本研究解析了重组人源PCMTD1蛋白的晶体结构，揭示其甲基转移酶活性结构域，并证明其在体外催化特定底物的甲基化修饰，可能与DNA损伤修复相关。
2. **文献名称**: *PCMTD1 interacts with HSP90 and modulates cellular stress response pathways*
**作者**: Chen L, et al.
**摘要**: 通过重组蛋白互作实验，发现PCMTD1与分子伴侣HSP90直接结合，参与调控细胞应激反应，可能通过蛋白质翻译后修饰影响信号通路稳定性。
3. **文献名称**: *Recombinant PCMTD1 expression in E. coli and its role in oxidative stress resistance*
**作者**: Wang Y, et al.
**摘要**: 报道了PCMTD1重组蛋白在大肠杆菌中的高效表达与纯化方法，并发现其过表达可增强细胞对氧化应激的耐受性，提示其在抗氧化防御中的潜在功能。
注：以上为模拟内容，实际文献需通过PubMed或专业数据库检索。若需具体文献，请提供更详细的研究方向或补充关键词。
PCMTD1 (Protein-L-isoaspartate (D-aspartate) O-methyltransferase domain-containing protein 1) is a less-studied member of the methyltransferase enzyme family, implicated in protein repair and stability. It shares structural homology with protein-L-isoaspartyl methyltransferase (PIMT), a conserved enzyme that recognizes isomerized aspartyl residues (isoAsp) in age-damaged proteins and catalyzes their methylation. This post-translational modification facilitates the restoration of aspartate residues, mitigating protein misfolding and aggregation—processes linked to cellular aging and neurodegenerative disorders. Unlike PIMT, PCMTD1 contains additional N-terminal domains of unclear function, suggesting potential regulatory roles or substrate specificity differences.
The gene encoding PCMTD1 is evolutionarily conserved across eukaryotes, indicating fundamental biological importance. Studies suggest its involvement in stress response pathways, particularly under oxidative or thermal stress, where protein damage is prevalent. PCMTD1 expression is tissue-specific, with higher levels observed in the brain, liver, and testes, hinting at roles in neuroprotection, metabolic regulation, or germ cell development. Dysregulation of PCMTD1 has been tentatively associated with cancers and neurological disorders, though mechanistic insights remain limited.
Recombinant PCMTD1 protein is typically produced in E. coli or mammalian expression systems, often tagged for purification. It serves as a tool to study enzyme kinetics, substrate interactions, and structure-function relationships. Current research focuses on clarifying its physiological substrates, regulatory mechanisms, and potential therapeutic applications, such as targeting protein misfolding diseases or enhancing cellular resilience. Despite progress, PCMTD1’s full functional spectrum and disease relevance await further exploration.
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