| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | H295N |
| Uniprot No | A0A1U8JT65 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-313aa |
| 氨基酸序列 | MTSDGATSTPAPRRKPSWRERENNRRRERRRRAIAAKIYTGLRAQGNYNLPKHCDNNEVLKALCSEAGWVVEDDGTTYRKGCKPPPIDIGGSSSKITPFSSQNPSPLSSAFPSPIPSCQVSPSSSSYPSPTRFDANNPSTLLPFLRNAIPSSLPPLRISNSAPVTPPLSSPTSRNPKPLPNWETIAKESMASFNYPFYAVSAPASPTHRHFHAPATIPECDESDTSTVESGQWISFQKFAPSTSQVPTSPTFFKLVKHLPPQNLHNDLGVKDKGRGAEFEFESGHLKPWEGERINDIGMDDLELTLGSGKPQC |
| 预测分子量 | 48.1 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H295N细胞系及其重组蛋白研究的参考文献示例(注意：以下为模拟示例，实际文献需通过学术数据库核实)：
1. **"Regulation of CYP11B1 and CYP11B2 expression in human adrenocortical H295N cells"**
- **作者**: Johansson, M. et al.
- **摘要**: 研究H295N细胞中醛固酮合成酶(CYP11B2)和皮质醇合成酶(CYP11B1)的基因表达调控机制，探讨cAMP信号通路对重组蛋白表达的影响。
2. **"ACTH-mediated steroidogenesis in H295N cells: Role of recombinant StAR protein"**
- **作者**: Christensen, K.L. & Parker, C.R.
- **摘要**: 通过转染重组StAR蛋白(类固醇生成急性调节蛋白)，分析其对H295N细胞中ACTH诱导的类固醇激素合成的促进作用。
3. **"In vitro effects of bisphenol A on recombinant CYP19 expression in H295N cells"**
- **作者**: Karmaus, A.L. et al.
- **摘要**: 评估环境污染物双酚A对H295N细胞中重组芳香酶(CYP19)活性的抑制作用及其对雌激素合成的干扰效应。
4. **"CRISPR/Cas9-engineered H295N cell lines for studying steroidogenic enzyme variants"**
- **作者**: Xiong, Y. et al.
- **摘要**: 利用CRISPR技术构建表达特定重组突变体(如CYP21A2)的H295N细胞系，用于先天性肾上腺增生症的分子机制研究。
**注意**：以上为模拟文献，实际引用时请通过PubMed、Web of Science等平台检索真实文献，并核对作者、标题及摘要内容。
The H295N recombinant protein is derived from the H295R human adrenocortical carcinoma cell line, which serves as a model system for studying adrenal steroidogenesis and endocrine-disrupting chemical effects. Established in the 1990s, H295R cells retain the ability to produce all major adrenal steroid hormones, including cortisol, aldosterone, and sex steroids, making them valuable for toxicological and pharmacological research. The H295N subclone was later developed through genetic modification to enhance experimental reproducibility and specific protein expression capabilities.
Recombinant proteins generated using H295N cells typically involve the insertion of target genes into these steroidogenically active cells, enabling researchers to study enzyme functions (e.g., CYP11B1/B2 in cortisol/aldosterone synthesis), receptor interactions, or signaling pathways under physiologically relevant conditions. This system allows for in vitro investigation of adrenal-specific protein behavior while maintaining native post-translational modification patterns that may be absent in non-adrenal expression systems.
These recombinant proteins find applications in drug discovery for metabolic disorders, hypertension, and adrenal cancers, as well as in environmental toxicology to assess chemical interference with steroidogenic pathways. The H295N platform is particularly useful for creating disease models (e.g., hyperaldosteronism) and screening compounds that modulate steroid hormone production. Its human origin provides distinct advantages over animal-derived models in translational research, offering better prediction of human adrenal responses to pharmaceutical interventions or environmental exposures. Recent advancements have enabled high-throughput applications and CRISPR-engineered variants for precision studies in adrenal protein function and regulation.
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