纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CRIM1 |
Uniprot No | Q9NZV1 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-1036aa |
氨基酸序列 | MYLVAGDRGLAGCGHLLVSLLGLLLLLARSGTRALVCLPCDESKCEEPRNCPGSIVQGVCGCCYTCASQRNESCGGTFGIYGTCDRGLRCVIRPPLNGDSLTEYEAGVCEDENWTDDQLLGFKPCNENLIAGCNIINGKCECNTIRTCSNPFEFPSQDMCLSALKRIEEEKPDCSKARCEVQFSPRCPEDSVLIEGYAPPGECCPLPSRCVCNPAGCLRKVCQPGNLNILVSKASGKPGECCDLYECKPVFGVDCRTVECPPVQQTACPPDSYETQVRLTADGCCTLPTRCECLSGLCGFPVCEVGSTPRIVSRGDGTPGKCCDVFECVNDTKPACVFNNVEYYDGDMFRMDNCRFCRCQGGVAICFTAQCGEINCERYYVPEGECCPVCEDPVYPFNNPAGCYANGLILAHGDRWREDDCTFCQCVNGERHCVATVCGQTCTNPVKVPGECCPVCEEPTIITVDPPACGELSNCTLTGKDCINGFKRDHNGCRTCQCINTEELCSERKQGCTLNCPFGFLTDAQNCEICECRPRPKKCRPIICDKYCPLGLLKNKHGCDICRCKKCPELSCSKICPLGFQQDSHGCLICKCREASASAGPPILSGTCLTVDGHHHKNEESWHDGCRECYCLNGREMCALITCPVPACGNPTIHPGQCCPSCADDFVVQKPELSTPSICHAPGGEYFVEGETWNIDSCTQCTCHSGRVLCETEVCPPLLCQNPSRTQDSCCPQCTDQPFRPSLSRNNSVPNYCKNDEGDIFLAAESWKPDVCTSCICIDSVISCFSESCPSVSCERPVLRKGQCCPYCIEDTIPKKVVCHFSGKAYADEERWDLDSCTHCYCLQGQTLCSTVSCPPLPCVEPINVEGSCCPMCPEMYVPEPTNIPIEKTNHRGEVDLEVPLWPTPSENDIVHLPRDMGHLQVDYRDNRLHPSEDSSLDSIASVVVPIIICLSIIIAFLFINQKKQWIPLLCWYRTPTKPSSLNNQLVSVDCKKGTRVQVDSSQRMLRIAEPDARFSGFYSMQKQNHLQADNFYQTV |
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CRIM1重组蛋白的参考文献及其摘要概括(虚构示例,供参考):
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1. **文献名称**: *"CRIM1重组蛋白在TGF-β信号通路中的调控作用"*
**作者**: Hsu, L., & Fan, X.
**摘要**: 本研究通过大肠杆菌表达系统成功纯化CRIM1重组蛋白,发现其通过结合TGF-β受体抑制SMAD蛋白磷酸化,提示CRIM1可能作为TGF-β通路的负调控因子参与细胞分化调控。
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2. **文献名称**: *"CRIM1胞外结构域重组蛋白的晶体结构与功能分析"*
**作者**: Smith, J., & Johnson, R.
**摘要**: 利用X射线衍射解析CRIM1胞外结构域重组蛋白的三维结构,揭示其富含半胱氨酸的结构域通过二硫键形成特异性结合口袋,为靶向CRIM1的分子设计提供结构基础。
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3. **文献名称**: *"CRIM1重组蛋白促进血管内皮细胞迁移的机制研究"*
**作者**: Zhang, Y., et al.
**摘要**: 通过真核表达系统制备CRIM1重组蛋白,发现其通过激活Integrin αVβ3-FAK通路增强血管内皮细胞迁移能力,提示其在血管生成和伤口修复中的潜在应用价值。
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注:以上文献为示例性内容,实际文献需通过PubMed或Web of Science等数据库检索。如需真实文献,建议使用关键词**"CRIM1 recombinant protein"**或**"CRIM1 expression and function"**进行查询。
CRIM1 (Cysteine-Rich Motor Neuron 1) is a transmembrane protein first identified for its role in neuronal development, particularly in motor neurons. It belongs to the CRIM protein family, characterized by multiple cysteine-rich repeat domains and a type I transmembrane structure. These structural features enable CRIM1 to interact with extracellular ligands and intracellular signaling molecules, positioning it as a key regulator of cell-cell communication and developmental processes.
Functionally, CRIM1 is implicated in modulating growth factor signaling pathways, including bone morphogenetic protein (BMP) and Wnt pathways. It acts as a scaffold or adaptor protein, binding to growth factors like BMPs via its cysteine-rich domains and regulating their bioavailability and activity. This interaction influences cellular processes such as differentiation, proliferation, and apoptosis. Studies highlight its critical role in organogenesis, particularly in kidney, eye, and vascular system development, where it helps maintain tissue architecture and signaling precision.
CRIM1 also exhibits context-dependent roles in disease. Reduced CRIM1 expression is linked to cancers (e.g., glioblastoma, colorectal cancer), where it may act as a tumor suppressor by inhibiting oncogenic pathways. Conversely, aberrant CRIM1 overexpression has been associated with fibrosis and chronic kidney disease, suggesting its involvement in extracellular matrix remodeling.
Recombinant CRIM1 protein, produced via heterologous expression systems like mammalian cells or bacteria, retains bioactivity for in vitro studies. It is widely used to elucidate CRIM1's molecular interactions, map binding partners, and explore therapeutic potential. Recent research focuses on leveraging recombinant CRIM1 to develop targeted therapies for developmental disorders and cancer, underscoring its dual role as both a signaling modulator and a disease biomarker.
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