| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPA12A |
| Uniprot No | O43301 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-675aa |
| 氨基酸序列 | ADKEAGGSD GPRETAPTSA YSSPARSLGD TGITPLSPSH IVNDTDSNVS EQQSFLVVVA VDFGTTSSGY AYSFTKEPEC IHVMRRWEGG DPGVSNQKTP TTILLTPERK FHSFGYAARD FYHDLDPNEA KQWLYLEKFK MKLHTTGDLT MDTDLTAANG KKVKALEIFA YALQYFKEQA LKELSDQAGS EFENSDVRWV ITVPAIWKQP AKQFMRQAAY QAGLASPENS EQLIIALEPE AASIYCRKLR LHQMIELSSK AAVNGYSGSD TVGAGFTQAK EHIRRNRQSR TFLVENVIGE IWSELEEGDK YVVVDSGGGT VDLTVHQIRL PEGHLKELYK ATGGPYGSLG VDYEFEKLLY KIFGEDFIEQ FKIKRPAAWV DLMIAFESRK RAAAPDRTNP LNITLPFSFI DYYKKFRGHS VEHALRKSNV DFVKWSSQGM LRMSPDAMNA LFKPTIDSII EHLRDLFQKP EVSTVKFLFL VGGFAEAPLL QQAVQAAFGD QCRIIIPQDV GLTILKGAVL FGLDPAVIKV RRSPLTYGVG VLNRYVEGKH PPEKLLVKDG TRWCTDVFDK FISADQSVAL GELVKRSYTP AKPSQLVIVI NIYSSEHDNV SFITDPGVKK CGTLRLDLTG TSGTAVPARR EIQTLMQFGD TEIKATAIDI ATSKSVKVGI DFLNY |
| 分子量 | 74.9 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人HSPA12A蛋白的三篇代表性文献的简要总结(文献标题和作者为虚构示例，仅供格式参考)：
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1. **标题**：*Recombinant human HSPA12A attenuates neuronal apoptosis via suppression of mitochondrial dysfunction*
**作者**：Zhang Y, et al.
**摘要**：研究利用大肠杆菌系统成功表达并纯化重组人HSPA12A蛋白，发现其在缺血性脑损伤模型中通过抑制线粒体途径的caspase活化保护神经元凋亡。
2. **标题**：*Expression and functional characterization of HSPA12A in cardiac endothelial cells under oxidative stress*
**作者**：Wang L, et al.
**摘要**：报道了通过哺乳动物细胞系制备重组HSPA12A，并证明其在氧化应激条件下通过调节VEGF信号通路增强内皮细胞存活，提示其在心血管疾病中的潜在治疗价值。
3. **标题**：*Structural insights into HSPA12A’s ATPase domain and its interaction with co-chaperones*
**作者**：Chen X, et al.
**摘要**：通过重组蛋白结晶解析HSPA12A的ATP结合结构域三维结构，揭示了其与HSP40家族分子伴侣相互作用的分子机制，为靶向该蛋白的药物设计提供基础。
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**注**：以上文献及内容为基于HSP家族蛋白的常见研究方向生成的模拟摘要。实际研究中，HSPA12A的相关文献较少，建议通过**PubMed/Google Scholar**用关键词“HSPA12A recombinant”或“HSPA12A function”检索最新研究，或确认目标蛋白是否为**HSPA12B**(研究相对更多)。
Recombinant human HSPA12A (Heat Shock Protein Family A Member 12A) is a less-studied member of the HSP70 protein family, which plays critical roles in cellular stress responses, protein folding, and chaperone-mediated processes. Unlike canonical HSP70 proteins, HSPA12A exhibits distinct structural features, including an extended N-terminal domain and variations in its ATP-binding domain, suggesting specialized functional properties. It is primarily expressed in the brain, testis, and cardiovascular tissues, with emerging evidence linking it to cell survival, anti-apoptotic signaling, and protection against oxidative or hypoxic stress.
Recombinant HSPA12A is typically produced using expression systems like *E. coli* or mammalian cells, followed by purification via affinity chromatography for research applications. Studies highlight its potential involvement in neurodegenerative diseases, ischemic injury, and cancer, where dysregulation of HSPA12A correlates with pathological progression. For instance, its overexpression in endothelial cells promotes angiogenesis, while its suppression may exacerbate neuronal damage. However, its exact molecular mechanisms, including client protein interactions and post-translational modifications, remain poorly understood. Current research focuses on characterizing its role in stress adaptation pathways and evaluating its therapeutic potential as a biomarker or intervention target. Further exploration is needed to clarify its functional divergence from other HSP70 members and its context-dependent roles in health and disease.
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