| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTMA |
| Uniprot No | P06454 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-110aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMSDAAVDTSSEITTKDLKEKKEVVEEA ENGRDAPANGNANEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGD EDEEAESATGKRAAEDDEDDDVDTKKQKTDEDD |
| 预测分子量 | 15 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PTMA(Prothymosin alpha)重组蛋白的3篇参考文献示例(虚构内容，仅供格式参考)：
1. **《Recombinant Prothymosin Alpha: Expression and Functional Analysis in Cancer Cells》**
- 作者：Smith A, et al.
- 摘要：研究报道了在大肠杆菌中高效表达PTMA重组蛋白的方法，并验证其通过调控凋亡相关通路抑制肿瘤细胞增殖的功能。
2. **《Structural Characterization of Human Prothymosin Alpha and Its Role in Immune Regulation》**
- 作者：Zhang L, et al.
- 摘要：通过核磁共振解析了PTMA重组蛋白的三维结构，并证明其通过增强T细胞活性参与免疫调节，为自身免疫疾病治疗提供理论依据。
3. **《Optimization of Recombinant PTMA Production in Yeast Systems》**
- 作者：Wang Y, et al.
- 摘要：对比酵母与大肠杆菌表达体系，优化毕赤酵母中PTMA重组蛋白的分泌表达条件，显著提高产量及生物活性。
(注：以上文献信息为模拟生成，实际研究中请通过PubMed或Web of Science等数据库检索真实文献。)
**Background of PTMA Recombinant Protein**
Prothymosin alpha (PTMA) is a small, highly acidic nuclear protein initially isolated from the thymus and implicated in immune regulation. With a molecular weight of approximately 12 kDa, PTMA is characterized by its high content of acidic amino acids (glutamic and aspartic acids) and lacks enzymatic activity. It is ubiquitously expressed in mammalian tissues and plays multifunctional roles in cellular processes, including cell proliferation, apoptosis, chromatin remodeling, and immune modulation. Structurally, PTMA lacks a stable tertiary structure under physiological conditions, adopting a disordered conformation that facilitates interactions with diverse molecular partners, such as histones, transcription factors, and nucleic acids.
The recombinant PTMA protein is produced using genetic engineering techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems to ensure proper folding and post-translational modifications. Recombinant PTMA retains the biological activity of its native counterpart and is widely utilized in research to study its mechanisms in cancer biology, viral infection responses, and neurodegenerative diseases. For instance, PTMA has been linked to tumor progression due to its anti-apoptotic properties and interactions with key regulators like p53 and NF-κB. It also exhibits immunostimulatory effects by enhancing T-cell activation and cytokine production.
Recent studies highlight PTMA’s potential as a therapeutic target or biomarker, particularly in oncology. Its dual role in promoting cell survival and modulating immune responses underscores its complexity, necessitating further exploration of its molecular pathways. Advances in recombinant protein technology have enabled large-scale production of PTMA, facilitating both basic research and preclinical investigations into its therapeutic applications.
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