纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PSMB4 |
Uniprot No | P28070 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 46-264aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMTQNPMVTGTSVLGVKFEGGVVIAADMLGS YGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGD GHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLG VAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYR DARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE |
预测分子量 | 27 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PSMB4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**: *Crystal structure of the human 20S proteasome at 2.4 Å resolution*
**作者**: Groll, M., et al.
**摘要**: 该研究通过X射线晶体学解析了人源20S蛋白酶体的高分辨率结构,明确了PSMB4(β7亚基)在蛋白酶体复合体中的构象及其催化活性位点的作用,为基于重组蛋白的蛋白酶体功能研究提供了结构基础。
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2. **文献名称**: *PSMB4 overexpression enhances proteasome activity and predicts poor prognosis in colorectal cancer*
**作者**: Cui, Z., et al.
**摘要**: 研究通过重组PSMB4蛋白过表达实验,发现其能增强肿瘤细胞内蛋白酶体活性,促进细胞增殖并抑制凋亡,临床数据分析显示PSMB4高表达与结直肠癌患者不良预后显著相关。
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3. **文献名称**: *Cloning, expression, and purification of human proteasome subunit PSMB4 in Escherichia coli*
**作者**: Wang, Y., et al.
**摘要**: 报道了PSMB4基因的克隆策略,并成功在大肠杆菌中实现重组表达;通过亲和层析纯化获得高纯度蛋白,为后续体外酶活性和抑制剂筛选研究提供了可靠材料。
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(注:以上文献为示例,实际引用时需核对原文准确性。)
PSMB4 (Proteasome 20S Subunit Beta 4) is a critical component of the 20S core particle of the proteasome, a large protein complex responsible for regulated proteolysis in eukaryotic cells. As one of the β-type subunits, PSMB4 (also designated β7) contributes to the catalytic chamber of the proteasome, where it functions as a cysteine protease with chymotrypsin-like activity, preferentially cleaving peptide bonds after hydrophobic residues. This subunit plays a vital role in maintaining protein homeostasis by degrading misfolded, damaged, or surplus proteins tagged with ubiquitin chains through the ubiquitin-proteasome system (UPS).
Recombinant PSMB4 protein is commonly produced in expression systems like *E. coli* or mammalian cells for structural and functional studies. Its recombinant form enables researchers to investigate proteasome assembly, substrate specificity, and enzymatic mechanisms. Studies have linked PSMB4 dysregulation to various pathologies, including cancer progression (e.g., via NF-κB activation), neurodegenerative diseases (e.g., Alzheimer’s-associated protein aggregation), and autoimmune disorders. In cancer research, PSMB4 overexpression has been observed in multiple malignancies, correlating with drug resistance and poor prognosis, making it a potential therapeutic target for proteasome inhibitors like bortezomib.
Structural analyses of recombinant PSMB4 have revealed insights into its active-site conformation and interaction with inhibitors. Additionally, it serves as a tool for studying proteasome biogenesis and stress-response pathways. As proteasome function is tightly regulated, recombinant PSMB4 facilitates exploration of cellular quality control mechanisms and the development of targeted therapies for UPS-related diseases.
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