首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MSTN |
| Uniprot No | O14793 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-375aa |
| 氨基酸序列 | HHHHHHASNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLR LETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATT ETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVET PTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNW LKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSR RDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEF VFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIP AMVVDRCGCS |
| 预测分子量 | 71 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3篇涉及MSTN重组蛋白研究的文献摘要概览：
1. **文献名称**：*"Expression and purification of biologically active recombinant myostatin in Escherichia coli"*
**作者**：Lee SJ, et al.
**摘要**：研究报道了在大肠杆菌中高效表达并纯化具有生物活性的重组MSTN蛋白，验证其通过抑制成肌细胞增殖调控肌肉生长的功能。
2. **文献名称**：*"Functional characterization of myostatin propeptide in regulating muscle mass through recombinant protein delivery"*
**作者**：Zhu X, et al.
**摘要**：通过重组技术制备MSTN前肽蛋白，证实其通过抑制成熟MSTN活性显著促进小鼠骨骼肌肥大，为肌肉萎缩治疗提供潜在策略。
3. **文献名称**：*"Structural analysis of myostatin and its interaction with follistatin-derived peptides using recombinant protein models"*
**作者**：Walker KS, et al.
**摘要**：利用重组MSTN蛋白解析其与卵泡抑素衍生肽的互作结构，揭示靶向抑制MSTN的分子机制，为设计新型肌肉生长促进剂奠定基础。
注：上述文献为示例性概括，实际引用需根据具体研究内容检索PubMed或Web of Science获取原文信息。
Myostatin (MSTN), also known as growth differentiation factor 8 (GDF-8), is a member of the transforming growth factor-beta (TGF-β) superfamily. It functions as a negative regulator of skeletal muscle growth by inhibiting myoblast proliferation and differentiation. First identified in 1997 through genetic studies in mice, MSTN gained attention due to its role in the "double muscling" phenotype observed in naturally occurring MSTN-deficient livestock and engineered animal models. This discovery highlighted its potential applications in agriculture and biomedicine.
Recombinant MSTN proteins are produced using biotechnological platforms, such as bacterial (E. coli), mammalian, or insect cell expression systems. These proteins typically consist of the mature C-terminal domain (responsible for biological activity) and the propeptide region, which regulates activation through proteolytic cleavage. Structural studies reveal that MSTN forms latent complexes with binding proteins like follistatin or its own prodomain, enabling precise control of its activity.
Research applications of recombinant MSTN span therapeutic development and agricultural innovation. In medicine, MSTN inhibitors are investigated for treating muscle-wasting disorders (e.g., muscular dystrophy, cachexia) and metabolic diseases. Conversely, recombinant MSTN itself could theoretically be used to manage pathological muscle overgrowth. In livestock production, MSTN modulation strategies aim to enhance lean meat yield through genetic or immunological approaches.
Challenges persist in MSTN research, including tissue-specific delivery of therapeutics, balancing muscle growth with cardiovascular safety, and understanding compensatory mechanisms in prolonged MSTN inhibition. Nevertheless, recombinant MSTN proteins remain crucial tools for deciphering muscle biology and developing interventions for human and animal health.
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