| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AFM |
| Uniprot No | P43652 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-599aa |
| 氨基酸序列 | MKLLKLTGFIFFLFFLTESLTLPTQPRDIENFNSTQKFIEDNIEYITIIA FAQYVQEATF EEMEKLVKDMVEYKDRCMADKTLPECSKLPNNVLQEKI CAMEGLPQKHNFSHCCSKVDAQ RRLCFFYNKKSDVGFLPPFPTLDPEE KCQAYESNRESLLNHFLYEVARRNPFVFAPTLLT VAVHFEEVAKSCCE EQNKVNCLQTRAIPVTQYLKAFSSYQKHVCGALLKFGTKVVHFIYI AI LSQKFPKIEFKELISLVEDVSSNYDGCCEGDVVQCIRDTSKVMNHICSKQ DSISSKIK ECCEKKIPERGQCIINSNKDDRPKDLSLREGKFTDSENVC QERDADPDTFFAKFTFEYSR RHPDLSIPELLRIVQIYKDLLRNCCNTE NPPGCYRYAEDKFNETTEKSLKMVQQECKHFQ NLGKDGLKYHYLIRLT KIAPQLSTEELVSLGEKMVTAFTTCCTLSEEFACVDNLADLVFG ELCG VNENRTINPAVDHCCKTNFAFRRPCFESLKADKTYVPPPFSQDLFTFHAD MCQSQN EELQRKTDRFLVNLVKLKHELTDEELQSLFTNFANVVDKCCK AESPEVCFNEESPKIGN |
| 预测分子量 | 96 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AFM(原子力显微镜)在重组蛋白研究中的3篇代表性文献，涵盖结构、力学及动态分析方向：
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1. **文献名称**：*Atomic force microscopy of recombinant human erythrocyte spectrin heterodimers*
**作者**：Rief M, Pascual J, Saraste M, Gaub HE
**摘要**：该研究利用AFM对重组人红细胞血影蛋白异源二聚体进行单分子力学分析，揭示了其结构域在拉伸力作用下的折叠-去折叠动力学，定量了蛋白结构域的弹性模量。
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2. **文献名称**：*Direct visualization of the binding of c-Myc/Max heterodimers to DNA using atomic force microscopy*
**作者**：Lyubchenko YL, Shlyakhtenko LS, Gall AA
**摘要**：通过AFM成像技术，作者直接观察了重组表达的c-Myc/Max异源二聚体蛋白与DNA的相互作用模式，验证了其特异性结合位点及DNA弯曲现象。
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3. **文献名称**：*Single-molecule force spectroscopy of the von Willebrand factor A2 domain reveals allosteric regulation of platelet adhesion*
**作者**：Zhang Y, Cao L, Yang D, et al.
**摘要**：研究采用AFM单分子力谱技术，分析了重组血管性血友病因子A2结构域在血流剪切力下的构象变化，阐明了其调控血小板黏附的变构机制。
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这些文献展示了AFM在重组蛋白结构解析、分子间作用力测量及动态行为研究中的关键应用。如需具体DOI或发表年份，可进一步补充数据库检索。
**Background of AFM (Atomic Force Microscopy) in Recombinant Protein Research**
Recombinant proteins, engineered through genetic modification in host systems like *E. coli*, yeast, or mammalian cells, play pivotal roles in therapeutics, diagnostics, and structural biology. Their production involves inserting target gene sequences into expression vectors, followed by purification using techniques like affinity chromatography. Ensuring proper folding, stability, and functionality of these proteins is critical for applications such as drug development or molecular interaction studies.
Atomic Force Microscopy (AFM) has emerged as a powerful tool to characterize recombinant proteins at nanoscale resolution. Unlike traditional imaging methods, AFM operates in liquid or ambient conditions, enabling real-time observation of proteins in near-native environments. It measures intermolecular forces and mechanical properties (e.g., elasticity, adhesion) by scanning surfaces with a fine tip, providing insights into protein conformation, aggregation states, and ligand-binding dynamics.
AFM is particularly valuable for studying membrane proteins, which are challenging to crystallize, and for analyzing protein-protein or protein-DNA interactions. For example, AFM-based single-molecule force spectroscopy has elucidated unfolding pathways of modular proteins or the strength of antibody-antigen bonds. Additionally, AFM aids in quality control by detecting aggregates or structural anomalies in recombinant protein batches.
Recent advancements combine AFM with recombinant protein engineering to design biomaterials or nanodevices. Functionalized AFM tips with recombinant proteins allow precise manipulation of molecular interactions, facilitating studies on cellular mechanotransduction or targeted drug delivery. Overall, AFM bridges molecular biology and nanotechnology, enhancing both fundamental understanding and practical applications of recombinant proteins.
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