| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FST |
| Uniprot No | P19883 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-344aa |
| 氨基酸序列 | G NCWLRQAKNG RCQVLYKTEL SKEECCSTGR LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGRCKKTCRD VFCPGSSTCV VDQTNNAYCV TCNRICPEPA SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI KAKSCEDIQC TGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA ACSSGVLLEV KHSGSCNSIS EDTEEEEEDE DQDYSFPISS ILEW |
| 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. |
以下是基于FST(卵泡抑素)重组蛋白研究的示例参考文献(注：以下为模拟示例，非真实文献)：
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1. **《Expression and Purification of Recombinant Human Follistatin in E. coli》**
*作者：Zhang L, et al.*
摘要：研究报道了通过大肠杆菌表达系统高效表达人源FST重组蛋白，优化了纯化工艺，并通过体外实验验证其抑制激活素A活性的功能，为大规模生产提供参考。
2. **《Recombinant Follistatin Enhances Muscle Regeneration in Murine Dystrophy Models》**
*作者：Smith JR, et al.*
摘要：利用哺乳动物细胞表达系统制备FST重组蛋白，证明其在肌营养不良小鼠模型中能显著促进肌肉修复并减少纤维化，提示其治疗肌肉退行性疾病的潜力。
3. **《Functional Characterization of FST-288 Isoform in Ovarian Follicle Development》**
*作者：Wang Y, et al.*
摘要：通过昆虫细胞表达体系获得FST-288亚型重组蛋白，研究发现其通过调控卵泡颗粒细胞增殖影响卵巢发育，为生殖功能障碍治疗提供新靶点。
4. **《A Novel PEGylated Follistatin Variant Improves Metabolic Parameters in Obese Mice》**
*作者：Tanaka K, et al.*
摘要：开发了一种聚乙二醇修饰的长效FST重组蛋白变体，证实其可通过调节脂肪代谢和胰岛素敏感性改善肥胖小鼠的代谢异常，具有临床应用前景。
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提示：实际研究中需通过学术数据库(如PubMed、Web of Science)检索具体文献，并关注近年发表的成果以获取最新进展。
Follistatin (FST), a glycoprotein initially isolated from ovarian follicular fluid in the 1980s, is a key regulatory protein involved in modulating cellular processes through interactions with members of the transforming growth factor-beta (TGF-β) superfamily. It acts primarily as a binding antagonist for activins, myostatin, and specific bone morphogenetic proteins (BMPs), effectively neutralizing their biological activity by preventing receptor engagement. This inhibitory mechanism positions FST as a critical player in tissue development, muscle growth, and metabolic homeostasis. Structurally, FST contains multiple isoforms generated via alternative splicing, with a conserved domain responsible for high-affinity ligand binding.
The recombinant form of FST (rhFST) is produced using genetic engineering techniques, often expressed in mammalian or bacterial systems for research or therapeutic purposes. Its ability to block myostatin—a negative regulator of muscle mass—has spurred interest in treating muscle-wasting disorders such as muscular dystrophy. Preclinical studies demonstrate that rhFST enhances muscle regeneration and reduces fibrosis, while also showing potential in metabolic disorders by improving insulin sensitivity. In reproductive biology, FST’s role in regulating activin-mediated folliculogenesis and steroidogenesis highlights its relevance in fertility research.
Current investigations extend to its anti-inflammatory properties and applications in tissue repair, including cardiac and bone regeneration. Despite promising outcomes in animal models, clinical translation remains limited, with challenges in optimizing delivery methods and minimizing off-target effects. Ongoing research aims to refine rhFST’s therapeutic window, exploring fusion proteins or targeted delivery systems to enhance efficacy. As a multifunctional modulator of TGF-β signaling, FST continues to be a focal point for understanding complex cellular interactions and developing novel biologics.
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