| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPA14 |
| Uniprot No | Q0VDF9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-509aa |
| 氨基酸序列 | MAAIGVHLGC TSACVAVYKD GRAGVVANDA GDRVTPAVVA YSENEEIVGL AAKQSRIRNI SNTVMKVKQI LGRSSSDPQA QKYIAESKCL VIEKNGKLRY EIDTGEETKF VNPEDVARLI FSKMKETAHS VLGSDANDVV ITVPFDFGEK QKNALGEAAR AAGFNVLRLI HEPSAALLAY GIGQDSPTGK SNILVFKLGG TSLSLSVMEV NSGIYRVLST NTDDNIGGAH FTETLAQYLA SEFQRSFKHD VRGNARAMMK LTNSAEVAKH SLSTLGSANC FLDSLYEGQD FDCNVSRARF ELLCSPLFNK CIEAIRGLLD QNGFTADDIN KVVLCGGSSR IPKLQQLIKD LFPAVELLNS IPPDEVIPIG AAIEAGILIG KENLLVEDSL MIECSARDIL VKGVDESGAS RFTVLFPSGT PLPARRQHTL QAPGSISSVC LELYESDGKN SAKEETKFAQ VVLQDLDKKE NGLRDILAVL TMKRDGSLHV TCTDQETGKC EAISIEIAS |
| 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HSPA14重组蛋白的3篇模拟参考文献及其摘要概括：
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1. **文献名称**: *"Recombinant HSPA14 enhances cellular protein folding through ATP-dependent mechanisms"*
**作者**: Smith J, et al.
**摘要**: 本研究报道了在大肠杆菌中高效表达并纯化HSPA14重组蛋白的方法，证实其具有ATP酶活性，可通过水解ATP协助错误折叠蛋白的再折叠，揭示了其在细胞应激反应中的分子伴侣功能。
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2. **文献名称**: *"HSPA14 interacts with viral capsid proteins to facilitate enterovirus assembly"*
**作者**: Li X, et al.
**摘要**: 通过重组HSPA14蛋白与肠道病毒蛋白的体外结合实验，发现HSPA14通过与病毒衣壳蛋白结合，促进其正确构象的形成，从而增强病毒颗粒的组装效率，为抗病毒靶点研究提供依据。
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3. **文献名称**: *"Structural insights into HSPA14’s unique substrate-binding domain revealed by cryo-EM"*
**作者**: Gupta R, et al.
**摘要**: 利用重组HSPA14蛋白进行冷冻电镜结构解析，发现其底物结合结构域存在不同于其他HSP70家族成员的特异性疏水口袋，解释了其对特定客户蛋白的选择性识别机制。
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(注：以上文献为模拟示例，实际引用时需检索真实数据库并核实信息。)
HSPA14. a member of the heat shock protein 70 (HSP70) family, is a molecular chaperone involved in protein folding, stress response, and cellular homeostasis. It shares structural and functional similarities with other HSP70 proteins, including an N-terminal ATPase domain and a C-terminal substrate-binding domain. Unlike its cytosolic counterparts (e.g., HSPA8 or HSPA1A), HSPA14 is uniquely localized to the endoplasmic reticulum (ER) and mitochondria, where it participates in organelle-specific protein quality control. Its expression is induced under stress conditions, such as heat shock, oxidative stress, or nutrient deprivation, to mitigate proteotoxic damage.
Recombinant HSPA14 protein is engineered for in vitro studies to explore its biochemical properties and therapeutic potential. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), it retains ATPase activity and substrate-binding capacity, enabling research into its interaction with client proteins or co-chaperones. Studies suggest HSPA14 plays roles in cancer progression, neurodegenerative diseases, and viral infection pathways. For instance, it may regulate ER-associated degradation (ERAD) or modulate mitochondrial function during apoptosis. However, its precise mechanisms remain less characterized compared to other HSP70s, making recombinant HSPA14 a valuable tool for unraveling its unique biological functions.
Current research focuses on its potential as a biomarker or drug target, particularly in diseases linked to protein misfolding. Challenges include optimizing recombinant protein stability and resolving structural details to inform inhibitor design. Further investigation into HSPA14’s role in cellular stress adaptation could advance therapeutic strategies for conditions like cancer or neurodegeneration.
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