| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ACTH |
| Uniprot No | P63267 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 3-376aa |
| 氨基酸序列 | EEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THNVPIYEGY ALPHAIMRLD LAGRDLTDYL MKILTERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS YELPDGQVIT IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK PEYDEAGPSI VHRKCF |
| 预测分子量 | 41,8 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ACTH重组蛋白的3篇示例文献摘要(注：以下为模拟内容，实际文献需通过学术数据库查询)：
1. **文献名称**：*Expression and Purification of Recombinant Human ACTH in Escherichia coli*
**作者**：Smith J, et al.
**摘要**：该研究利用大肠杆菌表达系统成功表达重组人ACTH，通过优化密码子和诱导条件提高蛋白产量，并采用亲和层析纯化获得高纯度产物，为大规模生产奠定了基础。
2. **文献名称**：*Biological Activity of Recombinant ACTH in Adrenal Cortical Cell Stimulation*
**作者**：Lee H, et al.
**摘要**：研究评估了重组ACTH的体外生物活性，证实其能有效激活肾上腺皮质细胞中皮质醇的合成与分泌，活性与天然ACTH相当，提示其潜在治疗应用价值。
3. **文献名称**：*Comparative Study of Recombinant vs. Natural ACTH in Clinical Therapeutics*
**作者**：Garcia R, et al.
**摘要**：通过临床试验对比重组ACTH与天然提取ACTH的疗效，结果显示重组蛋白在治疗肾上腺功能不全中具有相似疗效，且过敏反应发生率更低，安全性更优。
如需具体文献，建议通过PubMed、Google Scholar等平台以“recombinant ACTH protein”、“synthetic ACTH expression”为关键词检索。
Adrenocorticotropic hormone (ACTH), a 39-amino-acid peptide hormone produced in the anterior pituitary gland, plays a central role in regulating cortisol secretion from the adrenal glands. Its physiological functions are closely tied to the hypothalamic-pituitary-adrenal (HPA) axis, influencing stress responses, metabolism, and immune modulation. Naturally derived ACTH has been used clinically since the 1950s for diagnostic testing of adrenal insufficiency and treating conditions like infantile spasms. However, natural ACTH extracts, typically sourced from animal pituitary glands, face challenges including batch-to-batch variability, potential immunogenicity, and ethical concerns.
The development of recombinant ACTH (rhACTH) emerged to address these limitations. Utilizing genetic engineering techniques, the ACTH gene is inserted into expression systems like Escherichia coli or mammalian cell lines, enabling controlled production of synthetic ACTH with consistent quality. Recombinant technology allows precise modifications, such as creating truncated forms (e.g., the first 24 amino acids) that retain biological activity while improving stability. This approach eliminates reliance on animal sources and reduces contamination risks.
Clinically, rhACTH maintains therapeutic equivalence to natural ACTH in stimulating adrenal cortisol production, making it valuable for diagnosing adrenal disorders like Addison's disease or Cushing's syndrome. Research also explores its anti-inflammatory and immunomodulatory potential in autoimmune diseases. Furthermore, recombinant production supports scalable manufacturing, ensuring better supply stability for rare diseases requiring ACTH therapy. Ongoing studies continue to refine rhACTH formulations for enhanced pharmacokinetics and targeted delivery, reflecting its evolving role in endocrinology and beyond.
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