| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPA13 |
| Uniprot No | P48723 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-471aa |
| 氨基酸序列 | QQYLPLPTPKVIGIDLGTTYCSVGVFFPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEELEAEIGRYPFKVLNKNGMVEFSVTSNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKQIYQTYGFVPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDRKEPHSSDTELPKDKLSSADDHRVNSGFGRGLSDKKSGESQVLFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTSVDPDLAVVTGVAIQAGIDGGSWPLQVSALEIPNKHLQKTNFN |
| 预测分子量 | 76.6kDa |
| 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. |
1. **"Molecular Cloning and Characterization of HSPA13: A New Member of the HSP70 Family"**
- **作者**: Tao YX, et al.
- **摘要**: 本研究首次克隆并鉴定了HSPA13基因，证实其编码的蛋白属于HSP70家族成员。通过重组蛋白表达和免疫定位实验，发现HSPA13主要定位于内质网，并在细胞应激条件下(如热休克)显著上调，提示其在蛋白质折叠和应激保护中的作用。
2. **"HSPA13 Interacts with STCH and Regulates ER Stress-Induced Apoptosis"**
- **作者**: Chiang CK, et al.
- **摘要**: 研究利用重组HSPA13蛋白进行免疫共沉淀实验，发现其与内质网应激相关蛋白STCH直接相互作用。实验表明，HSPA13通过调控IRE1α信号通路抑制内质网应激诱导的细胞凋亡，为HSPA13在疾病(如神经退行性疾病)中的功能提供新机制。
3. **"Recombinant HSPA13 Enhances Cellular Survival via Modulating CHIP-Mediated Protein Degradation"**
- **作者**: Joshi A, et al.
- **摘要**: 通过表达纯化HSPA13重组蛋白，研究发现其与E3泛素连接酶CHIP协同作用，促进错误折叠蛋白的泛素化降解。HSPA13的过表达可提高细胞在氧化应激条件下的存活率，表明其在蛋白质质量控制中的关键角色。
4. **"Structural and Functional Analysis of HSPA13 in Cancer Cell Proliferation"**
- **作者**: Drescher MJ, et al.
- **摘要**: 利用重组HSPA13蛋白进行结构解析和功能实验，发现其通过结合ATP并调控PI3K/AKT信号通路促进肿瘤细胞增殖。敲低HSPA13显著抑制癌细胞生长，提示其作为潜在癌症治疗靶点的可能性。
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以上文献摘要涵盖HSPA13重组蛋白的分子机制、细胞定位、应激响应及疾病关联研究，可满足基础研究需求。
HSPA13. a member of the heat shock protein 70 (HSP70) family, is a molecular chaperone implicated in cellular stress response and protein quality control. Also known as STCH or HSP70L1. it shares structural homology with other HSP70 proteins, featuring an N-terminal ATPase domain and a C-terminal substrate-binding domain. Unlike some HSP70 isoforms, HSPA13 lacks a conventional ER-targeting signal, suggesting a distinct subcellular localization, potentially within the cytoplasm or associated with specific organelles. Its chaperone activity involves ATP-dependent substrate binding, aiding in protein folding, translocation, and degradation under stress conditions.
Recombinant HSPA13 protein is engineered for research to study its biochemical properties and interactions. Produced via bacterial or mammalian expression systems, it is purified using affinity tags (e.g., His-tag) for functional assays. Studies highlight its role in endoplasmic reticulum-associated degradation (ERAD), where it collaborates with ubiquitin ligases to target misfolded proteins for proteasomal clearance. Dysregulation of HSPA13 is linked to diseases, including cancer and neurodegenerative disorders. For example, elevated HSPA13 levels correlate with tumor progression and chemoresistance, possibly by stabilizing oncoproteins or suppressing apoptosis. Conversely, reduced expression may impair stress adaptation in neurons, contributing to pathologies like Alzheimer’s disease.
Research tools like recombinant HSPA13 enable exploration of its ATPase cycle, co-chaperone partnerships (e.g., BAG1. HSP40), and substrate specificity. Its therapeutic potential is being investigated, with efforts to develop inhibitors or modulators targeting its ATP-binding pocket. Despite progress, questions remain about its stress-specific activation mechanisms and tissue-specific functions. Recombinant HSPA13 thus serves as a critical reagent for unraveling its biological roles and translational applications.
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