| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | PMT2 |
| Uniprot No | P31382 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 311-609aa |
| 氨基酸序列 | LLSHSGTGDANMPSLFQARLVGSDVGQGPRDIALGSSVVSIKNQALGGSLLHSHIQTYPDGSNQQQVTCYGYKDANNEWFFNRERGLPSWSENETDIEYLKPGTSYRLVHKSTGRNLHTHPVAAPVSKTQWEVSGYGDNVVGDNKDNWVIEIMDQRGDEDPEKLHTLTTSFRIKNLEMGCYLAQTGNSLPEWGFRQQEVVCMKNPFKRDKRTWWNIETHENERLPPRPEDFQYPKTNFLKDFIHLNLAMMATNNALVPDPDKFDYLASSAWQWPTLNVGLRLCGWGDDNPKYFLLGTPA |
| 预测分子量 | 38.0 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PMT2重组蛋白的3-4条参考文献示例(内容为虚构，仅供格式参考)：
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1. **文献名称**: "Heterologous Expression and Functional Characterization of Pasteurella multocida Toxin PMT2 in Escherichia coli"
**作者**: Wilson, J. et al.
**摘要**: 本研究通过在大肠杆菌中重组表达PMT2蛋白，优化了纯化条件，并验证了其作为脱酰胺酶的活性，证实PMT2通过激活宿主细胞G蛋白信号通路诱导细胞骨架重排。
2. **文献名称**: "Structural Insights into PMT2 Toxin Domain and Its Role in Host Cell Modulation"
**作者**: Zhang, L. et al.
**摘要**: 通过X射线晶体学解析PMT2的C端结构域三维结构，揭示了其与宿主细胞Rho GTPases结合的关键位点，为开发靶向抑制剂提供了理论依据。
3. **文献名称**: "Site-Directed Mutagenesis of PMT2 Reveals Critical Residues for Cytopathic Effects"
**作者**: Müller, R. et al.
**摘要**: 通过点突变技术筛选出PMT2中负责细胞毒性功能的关键氨基酸(如第1165位丝氨酸)，突变后显著降低了对宿主细胞的破坏能力。
4. **文献名称**: "Recombinant PMT2 as a Potential Vaccine Candidate Against Pasteurellosis"
**作者**: Gupta, S. et al.
**摘要**: 评估了重组PMT2蛋白的免疫原性，动物实验表明其可诱导中和抗体，显著降低多杀性巴氏杆菌感染后的死亡率。
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*注：以上文献为示例，实际研究请通过PubMed/Google Scholar等平台检索真实数据。*
PMT2 (Protein O-Mannosyltransferase 2) is a key enzyme involved in post-translational protein modification, particularly O-mannosylation, a conserved glycosylation process critical for protein stability, trafficking, and function. Initially characterized in Saccharomyces cerevisiae, PMT2 belongs to the PMT family (PMT1-7 in yeast) responsible for initiating O-linked carbohydrate attachment to serine/threonine residues of target proteins. This modification is essential for cell wall integrity, stress response, and virulence in pathogenic fungi. In mammals, orthologs like POMT1/POMT2 perform analogous O-mannosylation roles, with defects linked to muscular dystrophies and neuronal disorders.
Recombinant PMT2 proteins are engineered for structural and functional studies, typically expressed in heterologous systems like Escherichia coli or insect cells. The purified enzyme enables biochemical characterization of its mannosyltransferase activity, substrate specificity, and interaction with partner proteins. Research leverages PMT2 recombinant proteins to investigate fungal pathogenesis mechanisms, as PMT family inhibitors are explored as potential antifungal agents. In biomedical contexts, mammalian POMT homolog studies using recombinant PMT2-like proteins contribute to understanding congenital glycosylation defects and developing therapeutic strategies.
Recent advances include cryo-EM structures of PMT complexes, revealing mechanistic insights into catalytic domains and regulatory regions. Such work highlights PMT2's biotechnological relevance in both industrial enzyme engineering and drug discovery pipelines targeting glycosylation pathways.
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