纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | HMGB1 |
Uniprot No | P09429 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-215aa |
氨基酸序列 | MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL SIGDVAKKLG EMWNNTAADD KQPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK SKKKKEEEED EEDEEDEEEE EDEEDEDEEE DDDDE |
预测分子量 | 25 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. |
以下为3篇关于HMGB1重组蛋白的关键文献摘要:
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1. **标题**:HMG-1 as a late mediator of endotoxin lethality in mice
**作者**:Wang, H. et al.
**期刊**:*Science* (1999)
**摘要**:首次提出HMGB1作为脓毒症晚期炎症介质,研究表明重组HMGB1蛋白注射可诱发小鼠全身炎症反应,并证实抗体中和HMGB1可显著提高脓毒症模型存活率。
2. **标题**:Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
**作者**:Scaffidi, P. et al.
**期刊**:*Nature* (2002)
**摘要**:对比细胞凋亡与坏死的HMGB1释放机制,发现坏死细胞主动释放重组HMGB1蛋白至胞外,激活巨噬细胞炎症信号通路,而凋亡细胞保留HMGB1于染色质内。
3. **标题**:High mobility group box protein 1 (HMGB1) as a therapeutic target in neuroinflammation
**作者**:Yang, H. et al.
**期刊**:*Journal of Neuroinflammation* (2020)
**摘要**:利用重组HMGB1蛋白构建小鼠脑损伤模型,证实其通过TLR4/NF-κB通路加剧神经炎症,并验证HMGB1抑制剂Glycyrrhizin可减轻神经退行性病变。
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**备注**:上述文献聚焦HMGB1重组蛋白在炎症模型中的作用机制,涵盖脓毒症、细胞死亡调控及神经疾病领域,可为靶向治疗研究提供参考。
High mobility group box 1 (HMGB1) is a non-histone nuclear protein that plays dual roles in cellular homeostasis and pathological processes. Structurally, it contains two DNA-binding HMG domains and an acidic C-terminal tail. Intracellularly, HMGB1 regulates chromatin architecture, DNA repair, and transcriptional processes. However, when actively secreted by immune cells or passively released during necrosis, extracellular HMGB1 functions as a damage-associated molecular pattern (DAMP) molecule, triggering inflammatory responses through receptor interactions (e.g., TLR4. RAGE) and promoting cytokine production.
Recombinant HMGB1 proteins, typically expressed in bacterial systems like *E. coli*, retain these biological activities and serve as critical tools for studying HMGB1's extracellular signaling mechanisms. Research using recombinant HMGB1 has revealed its involvement in numerous diseases, including sepsis, rheumatoid arthritis, cancer metastasis, and neurodegenerative disorders. It exhibits context-dependent roles—while excessive HMGB1 drives pathological inflammation and tissue damage, controlled release supports tissue repair and immune regulation.
Pharmaceutical interest focuses on developing HMGB1 inhibitors or neutralizing antibodies, with recombinant protein forms enabling drug screening and epitope mapping. Recent studies also explore its paradoxical functions in cancer, where HMGB1 may either promote tumor progression via angiogenesis or enhance chemotherapy efficacy by activating antitumor immunity. Standardized recombinant HMGB1 production remains essential for deciphering its complex biology and therapeutic targeting.
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