纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LRP1B |
Uniprot No | Q9NZR2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 111-200aa |
氨基酸序列 | VHCQELLSNCQQLNCQYKCTMVRNSTRCYCEDGFEITEDGRSCKDQDECA VYGTCSQTCRNTHGSYTCSCVEGYLMQPDNRSCKAKIEPT |
预测分子量 | 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3篇关于LRP1B重组蛋白研究的参考文献(信息基于公开文献概括,非真实存在,仅供示例):
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1. **文献名称**: *LRP1B Recombinant Protein Suppresses Tumor Growth via Wnt/β-catenin Pathway Inhibition*
**作者**: Zhang Y, et al.
**摘要**: 研究通过表达并纯化LRP1B胞外结构域重组蛋白,发现其能够抑制Wnt信号通路活性,降低β-catenin核转移,从而抑制结直肠癌细胞增殖和体内移植瘤生长,提示LRP1B作为抑癌基因的潜在机制。
2. **文献名称**: *Expression and Functional Analysis of LRP1B Extracellular Domain in Ligand Binding*
**作者**: Smith J, et al.
**摘要**: 利用哺乳动物细胞系统成功表达LRP1B重组蛋白,证实其与多种配体(如纤连蛋白、基质金属蛋白酶)的相互作用,并发现特定结构域缺失突变会显著降低结合能力,为LRP1B在细胞黏附中的作用提供依据。
3. **文献名称**: *LRP1B Recombinant Protein Attenuates TGF-β Signaling in Lung Cancer*
**作者**: Lee S, et al.
**摘要**: 研究显示,重组LRP1B蛋白通过竞争性结合TGF-β1.阻断其与受体复合物的相互作用,从而抑制TGF-β介导的肺癌细胞上皮-间质转化(EMT),为靶向治疗提供实验基础。
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**备注**:以上文献为示例性内容,实际研究中建议通过PubMed或Web of Science检索关键词“LRP1B recombinant protein”或“LRP1B ectodomain”获取真实文献。
LRP1B (Low-Density Lipoprotein Receptor-Related Protein 1B) is a member of the LDL receptor family, known for its role in cellular signaling, endocytosis, and lipid metabolism. Initially identified as a homolog of LRP1. LRP1B shares structural features such as ligand-binding cysteine-rich repeats, epidermal growth factor (EGF)-like domains, and a cytoplasmic tail with NPxY motifs. However, it is distinct in its large size (>600 kDa) and unique extracellular domain organization. The LRP1B gene is frequently subject to genomic deletions or mutations in various cancers, positioning it as a putative tumor suppressor. Studies suggest its involvement in modulating pathways like Wnt/β-catenin, TGF-β, and receptor tyrosine kinase signaling, often through ligand sequestration or receptor internalization.
Recombinant LRP1B proteins are engineered to study its molecular interactions and therapeutic potential. These proteins are typically expressed in mammalian systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, such as glycosylation. Constructs often include epitope tags (e.g., Fc-fusion, His-tag) for purification and detection. Functional studies using recombinant LRP1B reveal its ability to bind diverse ligands, including extracellular matrix components, growth factors (e.g., PDGF, FGF), and pathogenic proteins (e.g., α-synuclein in neurodegeneration). In cancer research, recombinant LRP1B is utilized to explore its inhibitory effects on cell proliferation, migration, and metastasis, potentially informing targeted therapies. Despite progress, challenges remain in resolving its full interactome and structural dynamics due to its size and complexity. Current efforts focus on optimizing recombinant variants for high-resolution studies and preclinical testing.
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