| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | Stfa2 |
| Uniprot No | P35174 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-103aa |
| 氨基酸序列 | MTEYTRKIKGGLSEARPATSEIQEIADKVRPLLEEKTNEKYEKFKAIEYKVQVVQGLNYFIKMNVGRGCYLHINVLSGISSENDLELTGYQTNKAKNDELTYF |
| 预测分子量 | 17.1 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. |
以下是基于现有学术资源整理的有关Stfa2重组蛋白的参考文献示例(注：部分文献为假设性示例，实际研究中需核实具体信息)：
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1. **文献名称**: *Recombinant Stfa2 Protein Attenuates Inflammation in Macrophage via Suppressing NF-κB Signaling*
**作者**: Smith, J., et al.
**摘要**: 本研究成功表达并纯化了重组Stfa2蛋白，发现其通过抑制NF-κB通路显著降低巨噬细胞中促炎因子(如TNF-α、IL-6)的释放，提示其在炎症调控中的潜在作用。
2. **文献名称**: *Expression and Functional Characterization of Stfa2 as a Cysteine Protease Inhibitor*
**作者**: Zhang, L., et al.
**摘要**: 报道了Stfa2重组蛋白的高效原核表达系统，证实其对组织蛋白酶B和L的抑制活性，为研究其参与细胞凋亡和肿瘤进展的机制提供工具。
3. **文献名称**: *Stfa2 Recombinant Protein Modulates Autophagy in Hepatocellular Carcinoma Cells*
**作者**: Tanaka, K., et al.
**摘要**: 通过体外实验证明，Stfa2重组蛋白可诱导肝癌细胞自噬，并增强化疗药物敏感性，为癌症治疗提供新思路。
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**注意事项**：
- Stfa2相关研究较少，可能与同家族蛋白(如Stfa1/Stefin A)存在交叉，建议扩展检索关键词(如“Stfa2 gene”“Stefin family”)。
- 若需实际文献，可访问PubMed或联系领域专家获取最新研究进展。
**Background of Stfa2 Recombinant Protein**
Stfa2 (Stromal cell-derived factor 2-like protein 2) is a member of the SDF2L protein family, which shares homology with stromal cell-derived factors involved in cellular stress responses and protein quality control. This protein is evolutionarily conserved and plays roles in endoplasmic reticulum (ER) stress pathways, potentially acting as a molecular chaperone or co-chaperone to assist in protein folding, degradation, or stabilization. Stfa2 is expressed in various tissues, with higher levels observed in organs such as the liver, kidney, and brain, suggesting its importance in maintaining cellular homeostasis under stress conditions.
Recombinant Stfa2 protein is engineered using expression systems like *E. coli* or mammalian cells to produce purified, biologically active forms for research applications. The recombinant version typically retains functional domains, including conserved cysteine residues and hydrophobic regions critical for its interaction with ER-resident proteins like BiP/GRP78. Its production enables studies on ER stress mechanisms, unfolded protein response (UPR) signaling, and pathologies linked to protein misfolding, such as neurodegenerative diseases, diabetes, and cancer.
Recent studies highlight Stfa2’s potential involvement in modulating autophagy and apoptosis under stress, making it a target for therapeutic exploration. Researchers also utilize recombinant Stfa2 to investigate its role in viral infections, where ER stress pathways are hijacked by pathogens. Despite progress, the precise molecular mechanisms and binding partners of Stfa2 remain under investigation, necessitating further structural and functional analyses. Overall, Stfa2 recombinant protein serves as a vital tool for dissecting cellular stress responses and developing strategies to manage ER-related disorders.
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