| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPF2 |
| Uniprot No | Q9NNZ3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-241aa |
| 氨基酸序列 | MPPLLPLRLCRLWPRNPPSRLLGAAAGQRSRPSTYYELLGVHPGASTEEVKRAFFSKSKELHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRSYDDQLRSGSPPKSPRTTVHDKSAHQTHSSWTPPNAQYWSQFHSVRPQGPQLRQQQHKQNKQVLGYCLLLMLAGMGLHYIAFRKVKQMHLNFMDEKDRIITAFYNEARARARANRGILQQERQRLGQRQPPPSEPTQGPEIVPRGAGP |
| 预测分子量 | 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. |
以下是基于假设的HSPF2重组蛋白研究示例文献(注：HSPF2的命名可能需要进一步确认，建议结合具体领域验证)：
1. **文献名称**: "Recombinant HSPF2 expression in E. coli and its chaperone activity analysis"
**作者**: Kampinga, H.H., et al.
**摘要**: 研究报道了在大肠杆菌系统中高效表达并纯化重组HSPF2蛋白，通过体外实验证实其具有ATP依赖的分子伴侣功能，可协助错误折叠蛋白的再折叠。
2. **文献名称**: "Structural insights into HSPF2's substrate-binding domain by X-ray crystallography"
**作者**: Smith, J., et al.
**摘要**: 利用重组HSPF2蛋白进行晶体结构解析，揭示了其底物结合域的关键氨基酸残基，为靶向HSPF2的药物设计提供了结构基础。
3. **文献名称**: "HSPF2 overexpression inhibits apoptosis in colorectal cancer cells"
**作者**: Chen, B., et al.
**摘要**: 通过体外重组HSPF2蛋白处理结直肠癌细胞，证明其通过抑制线粒体途径减少细胞凋亡，提示其在肿瘤耐药性中的潜在作用。
4. **文献名称**: "Recombinant HSPF2 attenuates neurodegeneration in a Drosophila model"
**作者**: Zhang, Y., et al.
**摘要**: 在果蝇神经退行性疾病模型中，外源性重组HSPF2蛋白显著减少多聚谷氨酰胺蛋白聚集，改善运动功能障碍。
**建议**：实际文献需通过PubMed、Web of Science等平台，以“HSPF2 recombinant protein”或“HSPF2 expression”为关键词检索，并注意核对基因/蛋白命名准确性(如是否指HSF2或HSP90家族成员)。
**Background of HSPA2 (HSP70-2) Recombinant Protein**
HSPA2. a member of the heat shock protein 70 (HSP70) family, is a molecular chaperone critical for cellular stress response and protein homeostasis. While traditionally associated with heat shock, HSPA2 exhibits specialized roles in germ cell development, particularly spermatogenesis, where it ensures proper folding and maturation of proteins essential for sperm formation. Structurally, it contains an N-terminal ATPase domain and a C-terminal substrate-binding domain, enabling ATP-dependent interaction with client proteins to prevent aggregation or assist in refolding.
Recombinant HSPA2 is produced via genetic engineering, often using bacterial (e.g., *E. coli*) or mammalian expression systems, followed by purification to ensure biological activity. Its production enables detailed study of its chaperone functions, mechanisms in stress adaptation, and involvement in pathologies. For instance, HSPA2 dysregulation is linked to male infertility, as mutations or reduced expression impair sperm quality. It also plays dual roles in cancer, acting as a tumor promoter by stabilizing oncoproteins or a suppressor by aiding apoptosis in certain contexts.
In research, recombinant HSPA2 serves as a tool to explore protein-protein interactions, DNA repair pathways, and cellular responses to stressors like heat or toxins. Therapeutically, it holds potential as a biomarker for infertility or cancer prognosis, and HSP70 inhibitors are being investigated for anticancer strategies. However, its pleiotropic roles require careful targeting to avoid off-effects.
Overall, HSPA2 recombinant protein bridges fundamental understanding of chaperone biology with translational applications in reproductive health, oncology, and beyond, highlighting its importance in both cellular resilience and disease mechanisms.
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