| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LAMa5 |
| Uniprot No | O15230 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 3401-3692aa |
| 氨基酸序列 | FVAQMEGLGTRLRAQSRQRSRPGRWHKVSVRWEKNRILLVTDGARAWSQEGPHRQHQGAEHPQPHTLFVGGLPASSHSSKLPVTVGFSGCVKRLRLHGRPLGAPTRMAGVTPCILGPLEAGLFFPGSGGVITLDLPGATLPDVGLELEVRPLAVTGLIFHLGQARTPPYLQLQVTEKQVLLRADDGAGEFSTSVTRPSVLCDGQWHRLAVMKSGNVLRLEVDAQSNHTVGPLLAAAAGAPAPLYLGGLPEPMAVQPWPPAYCGCMRRLAVNRSPVAMTRSVEVHGAVGASGC |
| 预测分子量 | 47.1 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LAMA5(层粘连蛋白α5)重组蛋白研究的示例参考文献(注：以下为模拟示例，实际文献需通过学术数据库检索)：
1. **文献名称**: "Recombinant Laminin-α5 Promotes Epithelial Cell Adhesion in vitro"
**作者**: Smith, J.R., et al.
**摘要**: 研究利用重组LAMA5蛋白构建体外细胞培养模型，证明其能显著增强人角膜上皮细胞的黏附与增殖，为组织工程提供新型基质材料。
2. **文献名称**: "Role of Recombinant LAMA5 in Tumor Extracellular Matrix Remodeling"
**作者**: Chen, L., & Wang, H.
**摘要**: 通过表达重组LAMA5蛋白，揭示其通过整合素信号通路调控肿瘤细胞侵袭能力，为靶向肿瘤微环境的治疗策略提供依据。
3. **文献名称**: "Production and Functional Characterization of Human LAMA5 in HEK293 Cells"
**作者**: Tanaka, K., et al.
**摘要**: 报道在HEK293细胞中高效表达具有生物活性的重组人LAMA5蛋白，并通过体外血管生成实验验证其促进内皮细胞管状结构形成的能力。
4. **文献名称**: "LAMA5 Recombinant Fragments for Neural Regeneration Studies"
**作者**: Müller, S., et al.
**摘要**: 设计并表达LAMA5的功能性片段，证明其在小鼠脊髓损伤模型中可引导神经元轴突定向生长，具有神经修复应用潜力。
---
如需真实文献，建议在 **PubMed** 或 **Web of Science** 中检索关键词："recombinant LAMA5 protein" 或 "laminin alpha 5 recombinant"。部分近期研究可能涉及其在干细胞分化、癌症或再生医学中的应用。
LAMa5 (Laminin alpha-5) is a critical subunit of laminin-511 (α5β1γ1), a trimeric glycoprotein essential for basement membrane formation and cellular interactions. As a key component of the extracellular matrix, laminins mediate cell adhesion, migration, differentiation, and tissue organization through interactions with integrins and other receptors. The alpha-5 chain contains conserved functional domains, including laminin-type epidermal growth factor-like (LE) domains and a globular (G) domain, which facilitate binding to cellular receptors and other matrix components.
Recombinant LAMa5 proteins are engineered using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications and functional integrity. These proteins retain critical bioactive regions while enabling scalable production with high purity and batch-to-batch consistency. Researchers often produce truncated variants focusing on the biologically active G-domain or specific integrin-binding motifs to study targeted interactions.
The development of recombinant LAMa5 has advanced studies in tissue engineering, stem cell biology, and disease modeling. It supports pluripotent stem cell maintenance by mimicking native basement membrane conditions, enabling feeder-free culture systems. In regenerative medicine, LAMa5-enriched matrices show potential for epithelial tissue repair and organoid development. Its role in pathological processes, including cancer metastasis and kidney fibrosis, is also under investigation using recombinant tools to dissect molecular mechanisms.
Commercial availability of recombinant LAMa5 has standardized research applications while reducing reliance on animal-derived extracts like Matrigel. Ongoing optimization focuses on modular protein designs, hybrid biomaterials, and clinical-grade production for therapeutic applications. The protein's versatility in bridging structural support and cellular signaling continues to make it a vital tool for both basic research and translational biomedical studies.
×
