| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LN |
| Uniprot No | Q6ZN17 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-250aa |
| 氨基酸序列 | MAEGGASKGG GEEPGKLPEP AEEESQVLRG TGHCKWFNVR MGFGFISMIN REGSPLDIPV DVFVHQSKLF MEGFRSLKEG EPVEFTFKKS SKGLESIRVT GPGGSPCLGS ERRPKGKTLQ KRKPKGDRCY NCGGLDHHAK ECSLPPQPKK CHYCQSIMHM VANCPHKNVA QPPASSQGRQ EAESQPCTST LPREVGGGHG CTSPPFPQEA RAEISERSGR SPQEASSTKS SIAPEEQSKK GPSVQKRKKT |
| 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. |
以下是模拟生成的3篇关于LN(层粘连蛋白)重组蛋白的参考文献示例：
1. **《重组人层粘连蛋白在乳腺癌细胞侵袭中的作用研究》**
作者：Zhang Y, et al.
摘要：本研究通过基因工程技术表达重组人层粘连蛋白(rhLN)，探讨其对乳腺癌细胞侵袭能力的影响。实验发现，rhLN通过激活整合素-ERK信号通路促进癌细胞迁移，为靶向LN的癌症治疗提供理论依据。
2. **《基于重组LN的仿生支架在神经再生中的应用》**
作者：Wang L, et al.
摘要：研究开发了一种负载重组层粘连蛋白的3D打印仿生支架，可显著增强神经干细胞的黏附和轴突延伸。动物实验表明，该材料能加速周围神经损伤修复，具有临床应用潜力。
3. **《高效表达重组层粘连蛋白的毕赤酵母系统优化》**
作者：Kimura T, et al.
摘要：通过密码子优化和发酵条件调控，在毕赤酵母中实现重组LN蛋白的高效分泌表达。获得的蛋白具有天然LN的三维结构活性，为大规模生产用于组织工程的重组LN奠定基础。
注：以上内容为学术场景模拟生成，实际文献需通过PubMed/Web of Science等平台检索。
Laminin (LN) recombinant proteins are engineered versions of naturally occurring laminins, a family of heterotrimeric glycoproteins essential for maintaining the structural and functional integrity of the extracellular matrix (ECM). Native laminins consist of α, β, and γ chains, forming cross-shaped molecules that interact with cell surface receptors (e.g., integrins, dystroglycans) to regulate cell adhesion, migration, differentiation, and tissue organization. Their roles in basement membrane formation and tissue development make them critical in embryogenesis, wound healing, and homeostasis.
The production of LN recombinant proteins emerged to address limitations in isolating native laminins from tissues, which are scarce, heterogenous, and contaminated with other ECM components. Using recombinant DNA technology, specific laminin isoforms (e.g., LN-511. LN-421) are expressed in mammalian cell systems (e.g., HEK293) to ensure proper post-translational modifications and functional domains. This allows large-scale, pure, and customizable laminin production.
LN recombinant proteins have become vital tools in regenerative medicine, cancer research, and stem cell applications. They enhance in vitro cell culture systems by mimicking native ECM environments, supporting pluripotent stem cell maintenance, and guiding tissue-specific differentiation. In therapeutics, they show potential in nerve regeneration, skin grafts, and treating genetic disorders linked to laminin deficiencies (e.g., epidermolysis bullosa). Additionally, their role in tumor metastasis is under investigation, as altered laminin expression correlates with cancer progression.
By enabling precise control over ECM composition, LN recombinant proteins bridge gaps between basic research and clinical translation, offering insights into cell-ECM interactions and advancing bioengineered therapies. Their versatility continues to drive innovations in 3D bioprinting, organoid development, and personalized medicine.
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