| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PCMT |
| Uniprot No | P2206 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-227aa |
| 氨基酸序列 | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAWK SGGASHSELI HNLRKNGIIK TDKVFEVMLA TDRSHYAKCN PYMDSPQSIG FQATISAPHM HAYALELLFD QLHEGAKALD VGSGSGILTA CFARMVGCTG KVIGIDHIKE LVDDSINNVR KDDPTLLSSG RVQLVVGDGR MGYAEEAPYD AIHVGAAAPV VPQALIDQLK PGGRLILPVG PAGGNQMLEQ YDKLQDGSIK MKPLMGVIYV PLTDKEKQWS RWK |
| 预测分子量 | 29 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PCMT(蛋白质羧基甲基转移酶)重组蛋白的3篇代表性文献摘要整理：
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1. **标题**：Expression and Characterization of Recombinant Protein L-Isoaspartyl Methyltransferase from Human Brain
**作者**：Johnson BA, Langmack EL, Aswad DW
**摘要**：该研究首次报道了人脑源PCMT的重组表达，通过在大肠杆菌中克隆并纯化酶，验证其催化受损天冬氨酸残基甲基化的活性，为研究蛋白质修复机制提供了工具。
2. **标题**：Structural Basis of Substrate Recognition by Human Protein L-Isoaspartyl Methyltransferase
**作者**：Skinner SP, Fogh RH, et al.
**摘要**：通过X射线晶体学解析了重组人PCMT与底物复合物的三维结构，揭示了其特异性识别异构化天冬氨酸的分子机制，为设计靶向抑制剂奠定结构基础。
3. **标题**：Protein Repair Methyltransferase Enhances the Thermostability of DNA Vaccines in Invertebrates
**作者**：Li Y, Wang X, et al.
**摘要**：探讨重组PCMT在生物技术中的应用，证明其通过修复蛋白质热损伤提高DNA疫苗稳定性，扩展了该酶在生物医药领域的潜在价值。
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这些研究涵盖PCMT重组蛋白的**功能验证**、**结构解析**及**应用探索**，为理解蛋白质修复机制及开发相关疗法提供了关键依据。如需具体文献编号或发表年份，建议通过PubMed或Web of Science进一步检索。
**Background of PCMT Recombinant Protein**
Protein carboxyl methyltransferase (PCMT), also known as protein-L-isoaspartate (D-aspartate) O-methyltransferase, is an evolutionarily conserved enzyme critical for repairing damaged proteins. It catalyzes the methylation of abnormal L-isoaspartate and D-aspartate residues formed via spontaneous deamidation or isomerization, a common degradation pathway in aging or stressed proteins. This post-translational modification facilitates the recognition and repair of structurally altered proteins, thereby maintaining cellular proteostasis.
PCMT is ubiquitously expressed across prokaryotes and eukaryotes, underscoring its fundamental biological role. In humans, PCMT1 (the primary isoform) is implicated in mitigating protein misfolding, aggregation, and loss of function—processes linked to aging and neurodegenerative disorders like Alzheimer’s disease. Recombinant PCMT proteins, produced via heterologous expression systems (e.g., *E. coli* or mammalian cell cultures), retain enzymatic activity and structural fidelity, enabling detailed biochemical and biophysical studies.
The production of recombinant PCMT leverages genetic engineering to optimize yield, purity, and functionality. This has advanced research into its substrate specificity, catalytic mechanisms, and interactions with cofactors like S-adenosylmethionine (SAM). Applications span biomedical research—exploring PCMT’s role in cellular stress responses—and biotechnology, where enhancing protein stability is crucial for therapeutic or industrial enzymes. Ongoing studies also investigate PCMT’s potential as a therapeutic target or biomarker in age-related pathologies.
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