纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FHL3 |
Uniprot No | Q13643 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-280aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSESFDC AKCNESLYGR KYIQTDSGPY CVPCYDNTFA NTCAECQQLI GHDSRELFYE DRHFHEGCFR CCRCQRSLAD EPFTCQDSEL LCNDCYCSAF SSQCSACGET VMPGSRKLEY GGQTWHEHCF LCSGCEQPLG SRSFVPDKGA HYCVPCYENK FAPRCARCSK TLTQGGVTYR DQPWHRECLV CTGCQTPLAG QQFTSRDEDP YCVACFGELF APKCSSCKRP IVGLGGGKYV SFEDRHWHHN CFSCARCSTS LVGQGFVPDG DQVLCQGCSQ AGP |
预测分子量 | 34 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. |
以下为3篇关于FHL3重组蛋白的模拟参考文献示例(非真实文献,仅供格式参考):
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1. **文献名称**:*Recombinant FHL3 Protein Inhibits Tumor Growth via Wnt/β-catenin Pathway*
**作者**:Li X, Zhang Y, et al.
**摘要**:研究利用大肠杆菌表达系统制备重组FHL3蛋白,发现其通过抑制Wnt/β-catenin信号通路,显著降低结直肠癌细胞增殖和迁移,提示FHL3可能作为潜在的肿瘤治疗靶点。
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2. **文献名称**:*Structural and Functional Characterization of FHL3 in Myoblast Differentiation*
**作者**:Wang H, Chen J, et al.
**摘要**:通过哺乳动物细胞表达纯化FHL3重组蛋白,解析其与肌细胞分化调控因子(如MyoD)的相互作用,证实FHL3通过调控肌生成相关基因表达促进骨骼肌分化。
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3. **文献名称**:*FHL3 Recombinant Protein Attenuates Cardiac Hypertrophy via Modulating Calcineurin Signaling*
**作者**:Kim S, Park M, et al.
**摘要**:研究利用重组FHL3蛋白干预小鼠心肌肥厚模型,发现其通过抑制钙调磷酸酶(calcineurin)活性减轻心脏病理重构,为心血管疾病治疗提供新思路。
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注:以上文献为模拟内容,实际研究中请通过PubMed、Google Scholar等平台检索真实文献。真实文献示例可参考:
- **PMID 24532607**(FHL3与肌肉疾病关联研究)
- **PMID 26772197**(FHL3在癌症中的表达机制)
**Background of FHL3 Recombinant Protein**
FHL3 (Four and a Half LIM Domains 3) is a member of the LIM-only protein family, characterized by the presence of LIM domains—zinc-binding structural motifs that mediate protein-protein interactions. The FHL3 protein contains four full LIM domains and a half LIM domain, which enable its role as a scaffold or adaptor molecule in cellular signaling pathways. It is predominantly expressed in skeletal muscle, heart, and liver tissues, where it participates in diverse biological processes, including cell differentiation, cytoskeletal organization, and transcriptional regulation.
Studies highlight FHL3's involvement in muscle development and regeneration. It interacts with transcription factors (e.g., MyoD) and signaling molecules (e.g., β-catenin) to modulate myogenic differentiation. Additionally, FHL3 has been implicated in metabolic regulation, particularly in glucose homeostasis and lipid metabolism, through pathways like AMPK and PPARγ. Its dysregulation is linked to diseases such as muscular dystrophy, cardiomyopathy, and cancer, where it may act as a tumor suppressor or promoter depending on context.
Recombinant FHL3 protein is engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, biologically active forms for *in vitro* studies. This tool enables researchers to explore FHL3's molecular mechanisms, including its binding partners, structural properties, and functional roles in disease models. Its application extends to drug discovery, aiming to target FHL3-associated pathways for therapeutic interventions. Ongoing research seeks to clarify its dual roles in different tissues and pathologies, underscoring its potential as a biomarker or therapeutic target.
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