首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CCL4L1 |
| Uniprot No | Q8NHW4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24 -92aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMAPMGSDPPTACCFSYTARKLPRNFV VDYYETSSLCSQPAVVFQTKRGKQVCADPSESWVQEYVYDLELN |
| 预测分子量 | 11 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CCL4L1重组蛋白的3篇示例文献(内容为模拟概括，非真实文献)：
---
1. **文献名称**: *Expression and Functional Characterization of Recombinant CCL4L1 in HIV-1 Infection*
**作者**: Smith A, et al.
**摘要**: 本研究通过大肠杆菌系统成功表达并纯化重组CCL4L1蛋白，验证其与CCR5受体的结合能力。实验表明，CCL4L1可竞争性抑制HIV-1病毒颗粒对宿主细胞的入侵，提示其作为抗病毒治疗分子的潜力。
2. **文献名称**: *CCL4L1 Isoforms Exhibit Differential Chemotactic Activity in Inflammatory Diseases*
**作者**: García-Rodríguez M, et al.
**摘要**: 通过哺乳动物细胞表达系统获得两种CCL4L1剪接变体重组蛋白(CCL4L1A和CCL4L1B)。功能实验显示，两者对单核细胞和T细胞的趋化活性存在显著差异，可能与类风湿性关节炎患者个体化病理机制相关。
3. **文献名称**: *Structural Analysis of Recombinant CCL4L1 Reveals Key Residues for Receptor Binding*
**作者**: Tanaka K, et al.
**摘要**: 利用X射线晶体学解析重组CCL4L1的三维结构，发现其N端α螺旋区域的特定氨基酸残基(如Arg18和Lys22)对CCR1/CCR5受体结合至关重要，为设计靶向趋化因子通路的药物提供结构基础。
---
注：以上文献为示例性质，实际研究中请通过PubMed、Web of Science等数据库检索真实文献。
**Background of CCL4L1 Recombinant Protein**
CCL4L1 (C-C motif chemokine ligand 4-like 1) is a variant of the chemokine CCL4. encoded by a gene arising from segmental duplication in the human genome. As a member of the CC chemokine family, CCL4L1 plays a role in immune regulation by recruiting and activating leukocytes through interaction with chemokine receptors, particularly CCR5. Unlike its paralog CCL4. CCL4L1 exhibits genetic polymorphisms and copy number variations across populations, influencing its expression and functional diversity.
The recombinant CCL4L1 protein is engineered *in vitro* using expression systems (e.g., *E. coli* or mammalian cells) to produce a purified, bioactive form. Structurally, it retains conserved chemokine features, including a characteristic fold stabilized by disulfide bonds. Functionally, recombinant CCL4L1 serves as a tool to study chemokine-receptor interactions, immune cell migration, and inflammatory responses. Its role in HIV pathogenesis is of particular interest, as CCR5 is a co-receptor for viral entry, and CCL4L1 may compete with HIV for receptor binding, potentially modulating infection.
Research also links CCL4L1 to autoimmune diseases, cancer, and chronic inflammation, highlighting its dual pro- and anti-inflammatory roles depending on context. Recombinant CCL4L1 enables mechanistic studies to explore these complexities and evaluate therapeutic potential, such as designing CCR5-targeted therapies or immune-modulating agents. However, variability in its natural isoforms and receptor-binding efficiency necessitates careful characterization of recombinant forms for experimental or clinical applications.
In summary, CCL4L1 recombinant protein bridges genetic insights into chemokine evolution with functional studies aimed at understanding immune regulation and developing targeted therapies.
×
