| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | XPO1 |
| Uniprot No | O14980 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1071aa |
| 氨基酸序列 | MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVL THLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCE GIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMVLVQILKQEWPKHWPTFI SDIVGASRTSESPCQNNMVILKLLSEEVFDFSSGQITQVKSKHLKDSMCN EFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTL IYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPL NTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEA LHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHF DVPPRRQLYLPMLFKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDS INLYKNMRETLVYLTHLDYVDTERIMTEKLHNQVNGTEWSWKNLNTLCWA IGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQ YPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFV QVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQ EHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACK AVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRT VKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEV LSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFL LLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTL LQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMF NLVEEGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTG LFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEEREIALRQADEEKH KRQMSVPGIFNPHEIPEEMCD |
| 预测分子量 | 144 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XPO1重组蛋白及相关研究的参考文献概要：
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1. **文献名称**: "Structural basis for leucine-rich nuclear export signal recognition by CRM1"
**作者**: Dong, X., Biswas, A., Süel, K.E., et al.
**摘要**: 本研究解析了CRM1/XPO1与含有富亮氨酸核输出信号(NES)的底物蛋白复合物的晶体结构，揭示了XPO1如何特异性识别并结合NES的分子机制。重组XPO1蛋白的纯化和结构分析为设计靶向核输出通路的抑制剂提供了结构基础。
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2. **文献名称**: "KPT-330. a potent and selective CRM1 inhibitor, exhibits anti-cancer activity through reactivation of tumor suppressor proteins"
**作者**: Etchin, J., Sun, Q., Kentsis, A., et al.
**摘要**: 本文报道了选择性XPO1抑制剂KPT-330(Selinexor)的研发及其抗肿瘤活性。研究利用重组XPO1蛋白验证了药物与靶点的直接结合，并证明其通过阻断肿瘤抑制蛋白(如p53)的核输出，抑制多种癌症细胞增殖。
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3. **文献名称**: "Recombinant expression and functional characterization of human Exportin-1 (XPO1) in yeast"
**作者**: Ossareh-Nazari, B., Gwizdek, C., Dargemont, C.
**摘要**: 作者通过酵母表达系统成功重组表达并纯化了人源XPO1蛋白，验证了其核输出功能。实验证明重组XPO1能够恢复酵母突变株的核质运输缺陷，为体外研究XPO1的生化特性及药物筛选提供了工具。
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如需更具体的文献或访问链接，可提供PMID/DOI进一步检索。
XPO1 (Exportin 1), also known as CRM1 (Chromosome Region Maintenance 1), is a key nuclear transport protein belonging to the karyopherin-β family. It mediates the export of numerous cargo proteins and RNAs from the nucleus to the cytoplasm. XPO1 recognizes specific nuclear export signals (NES) on cargoes, facilitating their transport through nuclear pore complexes via a RanGTP-dependent mechanism. This process is critical for regulating cellular functions such as cell cycle progression, stress response, and tumor suppression.
Dysregulation of XPO1 is implicated in various diseases, particularly cancer. Overexpression of XPO1 is observed in many malignancies, leading to aberrant cytoplasmic localization of tumor suppressor proteins (e.g., p53. p21) and oncogenic RNAs, thereby promoting tumor growth, drug resistance, and metastasis. This makes XPO1 a promising therapeutic target. Small-molecule inhibitors like Selinexor (KPT-330) block XPO1’s cargo-binding domain, restoring nuclear retention of tumor suppressors and inducing cancer cell apoptosis.
Recombinant XPO1 protein is produced using expression systems (e.g., E. coli, mammalian cells) for structural and functional studies. Its recombinant form preserves the native conformation required for binding NES-containing cargoes and RanGTP. Researchers use it to investigate nuclear transport mechanisms, validate inhibitor interactions, and develop diagnostic tools. Structural studies, including cryo-EM and crystallography, have revealed details about its HEAT-repeat architecture and dynamic conformational changes during transport.
Beyond oncology, XPO1 plays roles in viral infections, inflammation, and neurodegenerative diseases. Its recombinant protein aids in exploring these pathways and designing targeted therapies. Ongoing research aims to optimize XPO1 inhibitors for clinical use while minimizing off-target effects, highlighting its dual significance in basic science and translational medicine.
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