| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPA9 |
| Uniprot No | P38646 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 47-679aa |
| 氨基酸序列 | ASEA IKGAVVGIDL GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL VGMPAKRQAV TNPNNTFYAT KRLIGRRYDD PEVQKDIKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDSSGPK HLNMKLTRAQ FEGIVTDLIR RTIAPCQKAM QDAEVSKSDI GEVILVGGMT RMPKVQQTVQ DLFGRAPSKA VNPDEAVAIG AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTKLINR NTTIPTKKSQ VFSTAADGQT QVEIKVCQGE REMAGDNKLL GQFTLIGIPP APRGVPQIEV TFDIDANGIV HVSAKDKGTG REQQIVIQSS GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK DQLPADECNK LKEEISKMRE LLARKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE GSGSSGTGEQ KEDQKEEKQ |
| 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. |
以下是关于HSPA9重组蛋白的虚构参考文献示例(注：内容为模拟生成，非真实文献)：
1. **文献名称**：*HSPA9重组蛋白的线粒体定位与凋亡调控机制研究*
**作者**：Zhang L. et al.
**摘要**：本研究通过大肠杆菌表达系统成功获得高纯度HSPA9重组蛋白，证实其通过结合Bcl-2家族蛋白调控线粒体膜通透性，影响细胞凋亡通路，为癌症治疗提供潜在靶点。
2. **文献名称**：*Structural and functional characterization of recombinant HSPA9 in protein folding*
**作者**：Tanaka K. et al.
**摘要**：利用X射线晶体学解析HSPA9重组蛋白的三维结构，揭示其ATP酶结构域与底物结合域的相互作用机制，证明其在新生多肽链折叠中的分子伴侣功能。
3. **文献名称**：*HSPA9重组蛋白抑制神经退行性疾病相关蛋白聚集的体外研究*
**作者**：Wang Y. et al.
**摘要**：通过体外实验发现重组HSPA9蛋白能够有效抑制α-突触核蛋白和tau蛋白的病理性聚集，提示其在阿尔茨海默病和帕金森病中的潜在治疗价值。
4. **文献名称**：*HSPA9重组蛋白与化疗耐药性的相关性分析*
**作者**：Garcia-Ruiz C. et al.
**摘要**：在白血病细胞模型中，过表达重组HSPA9蛋白显著降低阿霉素诱导的细胞凋亡，其机制与线粒体应激通路的抑制相关，提示其可能作为化疗增敏靶点。
(注：以上文献信息为模拟创作，实际引用请查询真实数据库如PubMed)
HSPA9. also known as GRP75 or mortalin, is a member of the heat shock protein 70 (HSP70) family localized primarily in the mitochondria. This multifunctional chaperone plays critical roles in maintaining mitochondrial homeostasis, including facilitating protein import into the mitochondrial matrix, folding nascent polypeptides, and protecting against stress-induced damage. Structurally, it contains an N-terminal ATPase domain that drives conformational changes and a C-terminal substrate-binding domain that interacts with client proteins. HSPA9’s involvement in apoptosis regulation, cellular senescence, and stress response has linked it to various diseases, including cancer, neurodegenerative disorders, and metabolic syndromes.
Recombinant HSPA9 protein is engineered through heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its biochemical properties and therapeutic potential. Its production typically involves cloning the *HSPA9* gene into expression vectors, followed by purification using affinity tags like polyhistidine (His-tag). Researchers utilize recombinant HSPA9 to investigate its interactions with co-chaperones (e.g., TIM44 in mitochondrial protein import), client proteins (e.g., p53 in cancer pathways), and small molecules targeting its ATPase activity. Notably, dysregulation of HSPA9 has been observed in tumor progression, where its overexpression enhances cancer cell survival and chemoresistance, making it a potential biomarker or drug target.
Despite its importance, producing functional recombinant HSPA9 remains challenging due to its ATP-dependent conformational dynamics and susceptibility to aggregation. Recent studies focus on optimizing expression conditions and developing structural models to advance drug discovery. As mitochondrial dysfunction gains attention in aging and complex diseases, recombinant HSPA9 continues to serve as a vital tool for unraveling cellular stress responses and designing targeted therapies.
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