| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FHL2 |
| Uniprot No | Q14192 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-279aa |
| 氨基酸序列 | MTERFDCHHCNESLFGKKYILREESPYCVVCFETLFANTCEECGKPIGCD CKDLSYKDRHWHEACFHCSQCRNSLVDKPFAAKEDQLLCTDCYSNEYSSK CQECKKTIMPGTRKMEYKGSSWHETCFICHRCQQPIGTKSFIPKDNQNFC VPCYEKQHAMQCVQCKKPITTGGVTYREQPWHKECFVCTACRKQLSGQRF TARDDFAYCLNCFCDLYAKKCAGCTNPISGLGGTKYISFEERQWHNDCFN CKKCSLSLVGRGFLTERDDILCPDCGKDI |
| 预测分子量 | 56 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FHL2重组蛋白的3篇代表性文献示例(注：以下为模拟示例，具体文献需根据实际数据库检索验证)：
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1. **文献名称**：*Structural insights into the interaction of FHL2 with integrin β1 cytoplasmic domain*
**作者**：Gabriel B, et al.
**摘要**：本研究利用重组表达的FHL2蛋白，结合核磁共振(NMR)技术解析了FHL2与整合素β1胞内结构域的相互作用机制，揭示了其通过LIM结构域介导细胞黏附信号转导的关键位点。
2. **文献名称**：*FHL2 regulates cancer cell proliferation via modulating Wnt/β-catenin signaling*
**作者**：Müller JM, et al.
**摘要**：通过体外表达重组FHL2蛋白，研究发现FHL2作为β-catenin的共激活因子，增强Wnt信号通路活性，从而促进结直肠癌细胞的增殖和迁移，为靶向FHL2的癌症治疗提供依据。
3. **文献名称**：*Recombinant FHL2 inhibits cardiac hypertrophy by blocking calcineurin/NFAT signaling*
**作者**：Puranam RS, et al.
**摘要**：实验通过纯化重组FHL2蛋白，证实其能够结合钙调磷酸酶(calcineurin)，抑制NFAT转录因子的核转位，进而缓解压力负荷诱导的小鼠心肌肥厚，提示FHL2的心脏保护作用。
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**备注**：以上文献信息为基于FHL2功能研究的模拟概括，实际引用时建议通过PubMed、Google Scholar等平台检索最新或特定主题文献，并核对作者及摘要准确性。
**Background of FHL2 Recombinant Protein**
FHL2 (Four and a Half LIM Domain 2) is a member of the LIM-only protein family, characterized by four tandemly repeated LIM domains and a half-LIM motif at the N-terminus. LIM domains are zinc-binding structures that mediate protein-protein interactions, enabling FHL2 to act as a scaffold or adaptor in diverse cellular processes. Initially identified in the 1990s, FHL2 is ubiquitously expressed but shows high abundance in heart, muscle, and reproductive tissues. It interacts with numerous signaling molecules, transcription factors (e.g., β-catenin, androgen receptor), and structural proteins, modulating pathways involved in cell adhesion, proliferation, apoptosis, and mechanotransduction.
FHL2 plays dual roles in disease contexts. It acts as a tumor suppressor or promoter depending on cellular context, contributing to cancers (e.g., breast, prostate) by regulating oncogenic signaling (Wnt/β-catenin, TGF-β) or metastasis-related pathways. It also participates in cardiovascular diseases, fibrosis, and metabolic disorders by influencing extracellular matrix remodeling and stress responses.
Recombinant FHL2 protein is produced via expression systems (e.g., *E. coli*, mammalian cells*) to study its biochemical functions or therapeutic potential. Purification methods (e.g., affinity tags like His or GST) ensure high yield and purity. Researchers use recombinant FHL2 to investigate its interactions, structural dynamics, and roles in disease models. Its therapeutic relevance is emerging, particularly in tissue regeneration and targeted cancer therapies, though challenges remain in understanding its context-dependent mechanisms. Overall, FHL2 recombinant protein serves as a vital tool for deciphering the molecular basis of its multifunctionality in health and disease.
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