| 纯度 | >80%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PSMB7 |
| Uniprot No | Q99436 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 44-277aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MTTIAGVVYK DGIVLGADTR ATEGMVVADK NCSKIHFISP NIYCCGAGTA ADTDMTTQLI SSNLELHSLS TGRLPRVVTA NRMLKQMLFR YQGYIGAALV LGGVDVTGPH LYSIYPHGST DKLPYVTMGS GSLAAMAVFE DKFRPDMEEE EAKNLVSEAI AAGIFNDLGS GSNIDLCVIS KNKLDFLRPY TVPNKKGTRL GRYRCEKGTT AVLTEKITPL EIEVLEETVQ TMDTS |
| 预测分子量 | 28 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PSMB7重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Expression and Functional Characterization of Recombinant PSMB7 in Proteasome Assembly"*
**作者**：M. Kobayashi et al. (2016)
**摘要**：该研究通过大肠杆菌系统成功表达并纯化了重组PSMB7蛋白，验证了其在26S蛋白酶体组装中的关键作用。实验表明，PSMB7的缺失会导致蛋白酶体活性显著下降，提示其作为潜在药物靶点的可能性。
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2. **文献名称**：*"Structural Insights into PSMB7 Subunit in the Immunoproteasome via Recombinant Protein Crystallography"*
**作者**：H. Li et al. (2019)
**摘要**：作者利用昆虫细胞表达系统制备了重组人源PSMB7蛋白，并通过X射线晶体学解析其高分辨率结构。研究揭示了PSMB7在免疫蛋白酶体中的底物结合特异性，为自身免疫疾病治疗提供结构基础。
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3. **文献名称**：*"PSMB7 Knockdown and Recombinant Protein Rescue in Cancer Cell Models"*
**作者**：J. Park et al. (2020)
**摘要**：本研究通过siRNA敲低PSMB7后，利用重组PSMB7蛋白恢复细胞功能，证实其在多发性骨髓瘤细胞中的促存活作用。重组蛋白的应用为靶向蛋白酶体的抗癌策略提供了实验依据。
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(注：以上文献为示例，实际引用时需核实具体论文信息。)
PSMB7 (Proteasome 20S Subunit Beta 7) is a critical component of the 20S core particle within the 26S proteasome complex, an essential cellular machinery responsible for ubiquitin-mediated protein degradation. As a member of the β-subunit family, PSMB7 contains a catalytically active N-terminal threonine residue that contributes to the chymotrypsin-like proteolytic activity of the proteasome, enabling cleavage of peptide bonds after hydrophobic residues. This subunit plays a vital role in maintaining protein homeostasis, regulating cellular processes such as cell cycle progression, stress response, and immune antigen presentation.
Recombinant PSMB7 protein is engineered through molecular cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. The purified protein retains its structural and functional integrity, allowing researchers to study proteasome assembly, enzymatic mechanisms, and inhibitor interactions *in vitro*. Its recombinant form has become a valuable tool for investigating proteasome-related diseases, including cancer (where proteasome overactivity promotes tumor survival), neurodegenerative disorders (linked to protein aggregation), and autoimmune conditions.
Recent studies also explore PSMB7's potential as a therapeutic target, particularly in developing proteasome inhibitors for multiple myeloma treatment. The recombinant protein facilitates high-throughput drug screening and structural studies using techniques like X-ray crystallography. Additionally, it serves as an antigen in autoimmune disease research, helping characterize autoantibodies in conditions such as anti-proteasome syndrome. With its central role in cellular proteostasis and disease pathogenesis, PSMB7 recombinant protein continues to be a focal point in both basic research and translational biomedical applications.
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