纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LMP7 |
Uniprot No | P28062 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 73-276aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMTTTLAFKFQHGVIAAVDSRASAGSY ISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERIS VSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNM FSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVN MYHMKEDGWVKVESTDVSDLLHQYREANQ |
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. |
以下是关于LMP7重组蛋白的3篇代表性文献,涵盖其功能、结构及疾病相关性研究:
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1. **文献名称**:*Crystal structure of the human immunoproteasome LMP7 subunit in complex with a selective inhibitor*
**作者**:Huber EM, et al.
**摘要**:该研究解析了人源LMP7重组蛋白与特异性抑制剂的复合物晶体结构,揭示了抑制剂结合位点的分子机制,为开发靶向免疫蛋白酶体的抗炎或抗癌药物提供了结构基础。
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2. **文献名称**:*Immunoproteasome-specific subunit LMP7 regulates macrophage polarization and antiviral immunity*
**作者**:Li J, et al.
**摘要**:通过重组LMP7蛋白功能实验,发现LMP7通过调控NF-κB信号通路影响巨噬细胞极化,并参与抗病毒免疫应答,提示其在感染性疾病中的潜在治疗价值。
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3. **文献名称**:*Recombinant expression and purification of human LMP7 proteasome subunit for biochemical characterization*
**作者**:Chen X, et al.
**摘要**:报道了人源LMP7重组蛋白在大肠杆菌中的高效表达与纯化方法,并验证其酶活性,为后续研究LMP7的催化机制及高通量抑制剂筛选提供了技术方案。
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4. **文献名称**:*LMP7 deficiency attenuates atherosclerosis by inhibiting macrophage pyroptosis in mice*
**作者**:Wang Y, et al.
**摘要**:利用LMP7基因敲除小鼠模型及重组蛋白实验,证明LMP7通过促进巨噬细胞焦亡加剧动脉粥样硬化,提示靶向LMP7可能成为心血管疾病治疗新策略。
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以上文献涉及LMP7的结构解析、功能机制及疾病关联,涵盖基础研究与转化应用方向。如需具体期刊信息或出版年份,可进一步补充筛选。
**Background of LMP7 Recombinant Protein**
LMP7 (Low Molecular Mass Protein 7), encoded by the *PSMB8* gene, is a catalytic β-subunit of the immunoproteasome, a specialized form of the proteasome predominantly expressed in immune cells. Unlike constitutive proteasomes, immunoproteasomes are induced by cytokines like interferon-γ (IFN-γ) and play a critical role in antigen processing for major histocompatibility complex (MHC) class I presentation. LMP7 replaces the constitutive β5 subunit (PSMB5) in immunoproteasomes, altering cleavage specificity to generate peptides with hydrophobic or basic C-termini, which are optimal for MHC-I binding.
Dysregulation of LMP7 is linked to autoimmune diseases, chronic inflammation, and cancers. Overactivity may drive pathological immune responses (e.g., rheumatoid arthritis), while deficiencies impair pathogen clearance. Its role in protein homeostasis and immune signaling has made it a therapeutic target. Small-molecule inhibitors of LMP7 are being explored to modulate immune responses or treat proteasome-dependent malignancies.
Recombinant LMP7 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) for structural and functional studies. Purified LMP7 enables *in vitro* analysis of immunoproteasome activity, inhibitor screening, and epitope-processing mechanisms. Structural insights from X-ray crystallography or cryo-EM, using recombinant protein, guide drug design. Additionally, recombinant LMP7 aids in studying its interaction with regulatory proteins or post-translational modifications influencing immune pathways.
Overall, LMP7 recombinant protein serves as a vital tool for dissecting immunoproteasome biology and developing targeted therapies for immune disorders and cancer.
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