| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPA12B |
| Uniprot No | Q96MM6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-686aa |
| 氨基酸序列 | MLAVPEMGLQ GLYIGSSPER SPVPSPPGSP RTQESCGIAP LTPSQSPKPE VRAPQQASFS VVVAIDFGTT SSGYAFSFAS DPEAIHMMRK WEGGDPGVAH QKTPTCLLLT PEGAFHSFGY TARDYYHDLD PEEARDWLYF EKFKMKIHSA TDLTLKTQLE AVNGKTMPAL EVFAHALRFF REHALQELRE QSPSLPEKDT VRWVLTVPAI WKQPAKQFMR EAAYLAGLVS RENAEQLLIA LEPEAASVYC RKLRLHQLLD LSGRAPGGGR LGERRSIDSS FRQAREQLRR SRHSRTFLVE SGVGELWAEM QAGDRYVVAD CGGGTVDLTV HQLEQPHGTL KELYKASGGP YGAVGVDLAF EQLLCRIFGE DFIATFKRQR PAAWVDLTIA FEARKRTAGP HRAGALNISL PFSFIDFYRK QRGHNVETAL RRSSVNFVKW SSQGMLRMSC EAMNELFQPT VSGIIQHIEA LLARPEVQGV KLLFLVGGFA ESAVLQHAVQ AALGARGLRV VVPHDVGLTI LKGAVLFGQA PGVVRVRRSP LTYGVGVLNR FVPGRHPPEK LLVRDGRRWC TDVFERFVAA EQSVALGEEV RRSYCPARPG QRRVLINLYC CAAEDARFIT DPGVRKCGAL SLELEPADCG QDTAGAPPGR REIRAAMQFG DTEIKVTAVD VSTNRSVRAS IDFLSN |
| 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HSPA12B重组蛋白的3篇代表性文献的简要信息(注：文献为示例性概括，具体内容请以实际文献为准)：
1. **文献名称**：*HSPA12B attenuates cardiac dysfunction and mitochondrial dysfunction in doxorubicin-induced cardiomyopathy*
**作者**：Li Y, et al.
**摘要**：本研究通过重组HSPA12B蛋白在小鼠模型中验证其心脏保护作用，发现其通过抑制线粒体凋亡通路(如降低Bax/Bcl-2比例)减轻阿霉素诱导的心肌病，提示其在治疗化疗相关心脏毒性中的潜力。
2. **文献名称**：*Recombinant HSPA12B suppresses hepatic inflammation via modulating TLR4/NF-κB signaling in alcoholic liver disease*
**作者**：Wang H, et al.
**摘要**：文章报道重组HSPA12B蛋白通过抑制TLR4/NF-κB通路减少酒精性肝病中的炎症反应，并在体外肝细胞实验中证实其降低IL-6和TNF-α表达的能力，为肝脏疾病的治疗提供新靶点。
3. **文献名称**：*HSPA12B promotes angiogenesis through activating ERK1/2 signaling and enhancing VEGF expression*
**作者**：Liu Q, et al.
**摘要**：研究利用重组HSPA12B蛋白处理内皮细胞，发现其通过激活ERK1/2通路显著上调VEGF表达，促进血管新生，提示其在缺血性组织修复中的潜在应用价值。
4. **文献名称**：*Efficient prokaryotic expression and purification of human HSPA12B for structural studies*
**作者**：Zhang R, et al.
**摘要**：本文优化了HSPA12B重组蛋白在原核系统中的表达条件(如诱导温度、IPTG浓度)，并通过镍柱亲和层析获得高纯度蛋白，为后续结构解析(如X射线晶体学)奠定基础。
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**注**：以上内容基于领域内常见研究方向模拟生成，实际文献需通过PubMed、Web of Science等平台检索确认。
HSPA12B (Heat Shock Protein Family A Member 12B) is a relatively understudied member of the heat shock protein 70 (HSP70) family, which plays critical roles in cellular stress responses, protein folding, and apoptosis regulation. Unlike canonical HSP70s, HSPA12B exhibits distinct structural features and tissue-specific expression patterns, with higher abundance in endothelial cells, the brain, and cardiovascular tissues. It contains a conserved N-terminal ATPase domain and a C-terminal substrate-binding domain but lacks certain motifs found in traditional HSP70s, suggesting unique functional mechanisms.
Research indicates HSPA12B is involved in maintaining endothelial cell homeostasis, modulating inflammation, and promoting cell survival under stress conditions. It has been linked to protective roles in cardiovascular diseases, such as ischemia-reperfusion injury and atherosclerosis, by enhancing autophagy and suppressing oxidative stress. Its expression is upregulated in response to hypoxia and inflammatory cytokines, implying adaptive roles in pathological environments.
Recombinant HSPA12B protein is typically produced using bacterial or mammalian expression systems to enable functional studies. Purification often involves affinity chromatography tags (e.g., His-tag) followed by refolding steps to ensure proper conformation. This engineered protein serves as a tool to investigate HSPA12B's interactions with client proteins, its ATPase activity, and its therapeutic potential in diseases involving endothelial dysfunction or protein misfolding. Challenges remain in elucidating its precise molecular targets and signaling pathways, highlighting the need for further structural and mechanistic studies. Current applications span basic research, drug discovery, and biomarker development for conditions like neurodegenerative disorders and cardiovascular pathologies.
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