| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHMP4B |
| Uniprot No | Q9H444 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-224aa |
| 氨基酸序列 | SVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSIALPSKPAKKKEEEDDDMKELENWAGSM |
| 预测分子量 | 51.8 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CHMP4B重组蛋白的3篇参考文献示例(内容基于已有知识库信息，非真实文献)：
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1. **文献名称**：*Structural insights into CHMP4B polymerization and ESCRT-III disassembly*
**作者**：McCullough J, et al.
**摘要**：本研究通过重组CHMP4B蛋白的体外表达和纯化，结合冷冻电镜技术解析了其在ESCRT-III复合体中的多聚化结构。发现CHMP4B通过螺旋结构域的相互作用形成动态聚合物，并揭示了VPS4 ATP酶介导其解聚的分子机制。
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2. **文献名称**：*CHMP4B mutations disrupt endosomal sorting and cause autosomal dominant cataracts*
**作者**：Shiels A, et al.
**摘要**：研究报道了CHMP4B基因突变与遗传性白内障的关系。通过重组突变体蛋白的功能分析，发现突变导致CHMP4B丧失与ESCRT-III其他组分的结合能力，破坏内吞体膜重塑过程，最终引发晶状体细胞异常凋亡。
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3. **文献名称**：*Reconstitution of CHMP4B-VPS4 complexes in vitro for membrane fission assays*
**作者**：Schöneberg J, et al.
**摘要**：利用重组CHMP4B和VPS4蛋白构建体外膜分裂实验体系，证明CHMP4B在脂质膜表面形成螺旋状聚合物，并通过VPS4的ATP水解活性驱动膜颈收缩，为ESCRT-III介导的膜分离机制提供了直接证据。
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如需真实文献，建议通过PubMed或Google Scholar搜索关键词："CHMP4B recombinant protein"、"CHMP4B ESCRT-III"或结合具体研究方向筛选。
**Background of CHMP4B Recombinant Protein**
CHMP4B (Charged Multivesicular Body Protein 4B) is a key component of the Endosomal Sorting Complex Required for Transport (ESCRT)-III machinery, which plays essential roles in cellular membrane remodeling processes. This protein is involved in critical biological functions, including cytokinesis, multivesicular body (MVB) formation, viral budding, and membrane repair. As part of the ESCRT-III complex, CHMP4B facilitates the scission of membrane necks during these processes, enabling the spatial and temporal regulation of membrane dynamics.
The recombinant CHMP4B protein is produced *in vitro* using genetic engineering techniques, often expressed in bacterial (e.g., *E. coli*) or mammalian cell systems. Recombinant production allows for high purity and controlled modification, making it a valuable tool for studying ESCRT-III assembly, membrane interactions, and its role in diseases. For instance, CHMP4B dysfunction has been linked to cataracts, skin disorders (e.g., keratoderma), and cancer, where aberrant membrane trafficking or cell division may contribute to pathogenesis.
Structurally, CHMP4B contains characteristic “MIT (microtubule interacting and trafficking) interaction motifs” and undergoes conformational changes to polymerize into filaments that drive membrane deformation. Research using recombinant CHMP4B has advanced understanding of its autoinhibited monomeric state and activated oligomeric forms, often studied via cryo-EM or biochemical assays.
Its applications extend to *in vitro* reconstitution experiments, drug screening for ESCRT-related disorders, and exploring viral-host interactions (e.g., HIV-1 budding). By serving as a purified, functional protein, recombinant CHMP4B continues to illuminate fundamental cell biology mechanisms and therapeutic opportunities.
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