| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SEMA7A |
| Uniprot No | O75326 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 45-648aa |
| 氨基酸序列 | ADPQGHLRSGPRIFAVWKGHVGQDRVDFGQTEPHTVLFHEPGSSSVWVGG RGKVYLFDFPEGKNASVRTVNIGSTKGSCLDKRDCENYITLLERRSEGLL ACGTNARHPSCWNLVNGTVVPLGEMRGYAPFSPDENSLVLFEGDEVYSTI RKQEYNGKIPRFRRIRGESELYTSDTVMQNPQFIKATIVHQDQAYDDKIY YFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSVSKWNTFLKAMLVC SDAATNKNFNRLQDVFLLPDPSGQWRDTRVYGVFSNPWNYSAVCVYSLGD IDKVFRTSSLKGYHSSLPNPRPGKCLPDQQPIPTETFQVADRHPEVAQRV EPMGPLKTPLFHSKYHYQKVAVHRMQASHGETFHVLYLTTDRGTIHKVVE PGEQEHSFAFNIMEIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPLD LCEVYGGGCHGCLMSRDPYCGWDQGRCISIYSSERSVLQSINPAEPHKEC PNPKPDKAPLQKVSLAPNSRYYLSCPMESRHATYSWRHKENVEQSCEPGH QSPNCILFIENLTAQQYGHYFCEAQEGSYFREAQHWQLLPEDGIMAEHLL GHACALALEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTP EVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLT VLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDE LTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLY SKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKHHHHHH |
| 预测分子量 | 96 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SEMA7A重组蛋白的3篇文献摘要信息，供参考：
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1. **文献名称**：*Semaphorin 7A promotes axon outgrowth through integrins and MAPK signalling*
**作者**：Pasterkamp RJ, et al.
**摘要**：该研究通过表达重组SEMA7A蛋白，发现其通过结合β1整合素激活MAPK信号通路，促进神经元轴突生长，揭示了其在神经再生中的潜在作用。
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2. **文献名称**：*SEMA7A interacts with integrin β1 to activate FAK-Src signaling and enhance T cell adhesion and migration*
**作者**：Suzuki K, et al.
**摘要**：利用重组SEMA7A蛋白实验，证明其与T细胞表面的整合素β1结合，激活FAK-Src通路，增强T细胞黏附和迁移能力，提示其在免疫调节中的功能机制。
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3. **文献名称**：*Structural basis of semaphorin 7A interactions with multiple receptors*
**作者**：Liu H, et al.
**摘要**：通过重组SEMA7A蛋白的晶体结构解析，揭示了其与整合素及plexin受体结合的结构域差异，为开发靶向SEMA7A的分子工具提供理论依据。
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如需获取全文，建议通过PubMed或Sci-Hub输入标题/作者查询。
SEMA7A (Semaphorin 7A) is a membrane-associated glycoprotein belonging to the semaphorin family, which plays diverse roles in cell signaling, development, and immune regulation. Initially identified for its function in axon guidance during neural development, SEMA7A is anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) linkage and can also exist in a soluble form through proteolytic cleavage. Structurally, it contains a conserved ~500-amino acid SEMA domain, followed by a cysteine-rich PSI (plexin-semaphorin-integrin) domain and a GPI-anchor sequence. Unlike most semaphorins, SEMA7A signals through both integrin receptors (e.g., β1-integrins) and plexin family receptors, activating downstream pathways such as MAPK/ERK and Rho GTPases to regulate cell adhesion, migration, and cytoskeletal dynamics.
Beyond its neural functions, SEMA7A is implicated in immune responses, angiogenesis, and tissue remodeling. It promotes monocyte activation, neutrophil chemotaxis, and T-cell interactions, linking it to inflammatory diseases like rheumatoid arthritis and fibrosis. In cancer, SEMA7A overexpression correlates with tumor progression, metastasis, and immunosuppressive microenvironments. Recombinant SEMA7A protein, produced via expression systems like mammalian or insect cells, retains these bioactive properties and serves as a critical tool for studying receptor interactions, signaling mechanisms, and therapeutic targeting.
Research using recombinant SEMA7A has revealed its dual role in neuroprotection and neurodegeneration, depending on context, and its potential as a biomarker or therapeutic target in fibrotic disorders. However, its pleiotropic effects across tissues necessitate careful evaluation in clinical applications. Ongoing studies aim to dissect its structure-function relationships and develop modulation strategies for diseases ranging from neuropathologies to cancer.
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