| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | INHA |
| Uniprot No | P05111 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-366aa |
| 氨基酸序列 | CQGLELARELVLAKVRALFLDALGPPAVTREGGDPGVRRLPRRHALGGFT HRGSEPEEEEDVSQAILFPATDASCEDKSAARGLAQEAEEGLFRYMFRPS QHTRSRQVTSAQLWFHTGLDRQGTAASNSSEPLLGLLALSPGGPVAVPMS LGHAPPHWAVLHLATSALSLLTHPVLVLLLRCPLCTCSARPEATPFLVAH TRTRPPSGGERARRSTPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALN ISFQELGWERWIVYPPSFIFHYCHGGCGLHIPPNLSLPVPGAPPTPAQPY SLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI |
| 预测分子量 | 38 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INHA(抑制素α亚基)重组蛋白研究的3篇示例文献(注：文献信息为模拟示例，仅供参考)：
1. **文献名称**: "Expression and purification of recombinant human inhibin α subunit in Escherichia coli"
**作者**: Smith J, et al.
**摘要**: 研究报道了通过原核表达系统(大肠杆菌)成功表达人源INHA重组蛋白，并优化了纯化条件，获得高纯度蛋白。通过Western blot和体外活性实验验证了其与抑制素β亚基的结合能力。
2. **文献名称**: "Functional characterization of recombinant inhibin A in ovarian granulosa cells"
**作者**: Chen L, et al.
**摘要**: 利用哺乳动物细胞表达系统制备重组INHA蛋白，证明其可显著抑制FSH诱导的小鼠卵巢颗粒细胞增殖，并通过SMAD信号通路调控细胞功能，为生殖内分泌研究提供工具。
3. **文献名称**: "Role of recombinant inhibin α in a PCOS rat model"
**作者**: Wang Y, et al.
**摘要**: 研究通过注射重组INHA蛋白干预多囊卵巢综合征(PCOS)大鼠模型，发现其可改善激素紊乱和卵泡发育异常，提示INHA在生殖疾病治疗中的潜在应用价值。
(注：以上文献为示例性内容，实际研究需参考具体数据库如PubMed、ScienceDirect等检索。)
**Background of INHA Recombinant Protein**
INHA (Inhibin Alpha Subunit) recombinant protein is derived from the alpha subunit of inhibin, a glycoprotein hormone involved in regulating reproductive physiology. Inhibin, primarily produced in the gonads, consists of an α-subunit (INHA) and one of two β-subunits (βA or βB), forming inhibin A or B. It plays a critical role in negative feedback regulation of follicle-stimulating hormone (FSH) secretion from the pituitary gland, thereby influencing gametogenesis and steroidogenesis.
The development of recombinant INHA emerged from the need to study inhibin’s biological functions and its dysregulation in diseases. Traditional methods of isolating inhibin from biological fluids were inefficient due to low abundance. Advances in genetic engineering in the 1980s–1990s enabled the production of recombinant INHA using expression systems like *E. coli*, yeast, or mammalian cells (e.g., CHO). Mammalian systems are preferred for generating properly folded, post-translationally modified proteins, crucial for functional studies.
Recombinant INHA has been instrumental in reproductive research, including elucidating its role in ovarian follicle development, spermatogenesis, and feedback mechanisms in the hypothalamic-pituitary-gonadal axis. It also has diagnostic and therapeutic applications. For instance, it serves as an antigen in immunoassays to measure inhibin levels, aiding in monitoring ovarian reserves or diagnosing granulosa cell tumors. Additionally, recombinant INHA is explored in fertility treatments and as a target for neutralizing antibodies in cancers overexpressing inhibin alpha.
Recent studies highlight its potential in regenerative medicine and disease modeling, such as using INHA-knockout models to study reproductive disorders. Challenges remain in optimizing production yield and bioactivity, but ongoing advancements in protein engineering continue to expand its research and clinical utility.
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