| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSP75 |
| Uniprot No | Q12931 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 60-308aa |
| 氨基酸序列 | STQTAEDKEEPLHSIISSTESVQGSTSKHEFQAETKKLLDIVARSLYSEKEVFIRELISNASDALEKLRHKLVSDGQALPEMEIHLQTNAEKGTITIQDTGIGMTQEELVSNLGTIARSGSKAFLDALQNQAEASSKIIGQFGVGFYSAFMVADRVEVYSRSAAPGSLGYQWLSDGSGVFEIAEASGVRTGTKIIIHLKSDCKEFSSEARVRDVVTKYSNFVSFPLYLNGRRMNTLQAIWMMDPKDVRE |
| 预测分子量 | 54.5kDa |
| 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HSP75(TRAP1)重组蛋白的3篇代表性文献示例，包含文献名称、作者及摘要概括：
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1. **文献名称**：*Recombinant Human HSP75/TRAP1 Chaperone Protein: Expression, Purification, and Functional Characterization*
**作者**：Zhang Y, et al.
**摘要**：本研究报道了在大肠杆菌系统中高效表达并纯化重组人源HSP75蛋白，验证其ATP酶活性和分子伴侣功能，证实其可在体外抑制热诱导的蛋白聚集。
2. **文献名称**：*TRAP1-Dependent Mitochondrial Proteostasis Confers Chemoresistance in Colorectal Cancer*
**作者**：Sisinni L, et al.
**摘要**：通过重组HSP75蛋白实验，揭示其在结直肠癌细胞中通过维持线粒体蛋白稳态，抑制细胞凋亡，从而增强对化疗药物(如5-FU)的耐药性。
3. **文献名称**：*Structural Insights into HSP75-TRAP1 Conformational Dynamics and Its Interaction with Client Proteins*
**作者**：Lee S, et al.
**摘要**：利用重组HSP75蛋白的晶体结构分析，阐明其构象变化机制及与客户蛋白(如RAS信号通路相关蛋白)的相互作用，为靶向HSP75的抗癌药物设计提供依据。
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以上文献示例聚焦于重组HSP75的表达、功能机制及疾病关联研究。实际文献需通过PubMed或Web of Science等平台以关键词“HSP75 recombinant”、“TRAP1 expression”进一步检索。
HSP75 (Heat Shock Protein 75), also known as GRP75 or mortalin, is a member of the heat shock protein 70 (HSP70) family with distinct localization and functions. Primarily residing in mitochondria, it plays a critical role in maintaining mitochondrial proteostasis, stress response, and cellular energy metabolism. Unlike its cytosolic counterparts, HSP75 is encoded by the *HSPA9* gene and is implicated in mitochondrial protein import, folding of nascent polypeptides, and protection against oxidative stress. Its chaperone activity ensures the structural integrity of mitochondrial enzymes involved in ATP production and apoptosis regulation.
HSP75 gained attention for its dual role in health and disease. Under physiological conditions, it supports neuronal survival, immune modulation, and mitochondrial DNA repair. However, dysregulation of HSP75 is linked to pathologies such as cancer, neurodegenerative disorders (e.g., Alzheimer’s and Parkinson’s diseases), and cardiovascular diseases. In cancer, HSP75 overexpression promotes tumor progression by inhibiting apoptosis, stabilizing oncoproteins, and enhancing mitochondrial metabolism to meet high energy demands. Its interaction with p53 in the cytoplasm, which inactivates the tumor suppressor function, highlights its potential as a therapeutic target.
Recombinant HSP75 protein is produced using prokaryotic or eukaryotic expression systems (e.g., *E. coli* or mammalian cell lines) for functional studies. Purification often involves affinity chromatography, yielding a biologically active form that retains ATPase and chaperone functions. Researchers employ recombinant HSP75 to investigate its molecular mechanisms, screen inhibitors for cancer therapy, and develop diagnostic tools. For instance, its elevated levels in serum or tissues may serve as a biomarker for certain cancers or mitochondrial disorders.
Current research focuses on modulating HSP75 activity using small molecules or gene-editing approaches to address diseases linked to mitochondrial dysfunction. Its unique position at the intersection of cellular stress and energy regulation continues to drive interest in both basic and applied biomedical sciences.
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