| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MSN |
| Uniprot No | P26038 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-577aa |
| 氨基酸序列 | PKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKGFSTWLK LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI EVQQMKAQAR EEKHQKQMER AMLENEKKKR EMAEKEKEKI EREKEELMER LKQIEEQTKK AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLALE MAELTARISQ LEMARQKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEQ DEQDENGAEA SADLRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM |
| 预测分子量 | 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MSN(Moesin)重组蛋白的模拟参考文献示例(注：文献为虚构示例，建议通过学术数据库检索真实文献)：
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1. **文献名称**: *Expression and Purification of Recombinant Moesin (MSN) for Structural Studies*
**作者**: Smith J, et al.
**摘要**: 本研究报道了通过大肠杆菌表达系统高效表达和纯化重组MSN蛋白的方法，并利用X射线晶体学解析其结构，揭示其与细胞骨架相互作用的分子机制。
2. **文献名称**: *Functional Analysis of Recombinant MSN Protein in Cancer Cell Migration*
**作者**: Lee S, et al.
**摘要**: 通过体外重组MSN蛋白实验，证明其在调节肿瘤细胞迁移中的关键作用，并发现MSN磷酸化状态影响Rho GTPase信号通路活性。
3. **文献名称**: *Recombinant MSN Fusion Protein as a Targeted Drug Delivery Carrier*
**作者**: Patel R, et al.
**摘要**: 开发了一种基于重组MSN的融合蛋白载体，可特异性结合肿瘤细胞表面受体，显著提高化疗药物的靶向递送效率并减少脱靶毒性。
4. **文献名称**: *Role of Recombinant MSN in Immune Response Modulation*
**作者**: Wang Q, et al.
**摘要**: 利用昆虫细胞表达系统获得高纯度重组MSN蛋白，研究发现其通过调控T细胞膜稳定性参与免疫抑制过程，为自身免疫疾病治疗提供新思路。
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**提示**：实际研究中建议通过PubMed、Web of Science等平台，以“recombinant Moesin protein”“MSN protein purification”等关键词检索近期文献。
MSN (Moesin) recombinant protein is a key component in studying cellular structure, signaling, and disease mechanisms. Moesin, a member of the ERM (Ezrin, Radixin, Moesin) protein family, acts as a scaffolding protein that links the plasma membrane to the cytoskeleton. It plays critical roles in maintaining cell shape, adhesion, motility, and membrane organization by interacting with actin filaments and transmembrane proteins. Structurally, Moesin contains an N-terminal FERM domain for membrane binding and a C-terminal actin-binding domain, with a regulatory α-helical region in between.
Recombinant MSN proteins are engineered using expression systems like *E. coli* or mammalian cells to produce purified, functional Moesin for research. These proteins retain post-translational modifications when expressed in eukaryotic systems, enhancing their biological relevance. Researchers utilize MSN recombinant proteins to investigate cytoskeletal dynamics, cell polarization, and signaling pathways involving Rho GTPases. Dysregulation of Moesin is implicated in cancer metastasis, immune cell activation, and viral pathogenesis (e.g., HIV entry via membrane ruffling).
In cancer studies, MSN overexpression correlates with invasive phenotypes, making it a potential therapeutic target. Its role in immune responses includes regulating T-cell receptor signaling and leukocyte migration. Recombinant Moesin also aids in structural biology, enabling crystallographic studies to map interaction sites. Production of MSN variants (e.g., phosphorylation-mimetic mutants) helps dissect activation mechanisms. Challenges include maintaining protein stability and mimicking native phosphorylation states. Overall, MSN recombinant proteins serve as indispensable tools for decoding cellular mechanics and disease pathways.
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