| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SEMA4G |
| Uniprot No | Q9NTN9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-127aa |
| 氨基酸序列 | MGSMSPPSAWPCVLDGPETRQDLCQPPKPCVHSHAHMEECLSAGLQCPHP HLLLVHSCFIPASGLGVPSQLPHPIWSSSPASCGDLFVKSLGTGQPGEVR LHHSPPLPSCVALVNQPPHSPWSFSRV |
| 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. |
以下是关于SEMA4G重组蛋白的3篇模拟参考文献及其摘要概括(注：文献为示例性虚构，实际文献需通过学术数据库查询)：
1. **文献名称**: *"SEMA4G Recombinant Protein Suppresses Hepatocellular Carcinoma Metastasis via ERK Signaling Pathway"*
**作者**: Zhang Y, et al. (2020)
**摘要**: 研究利用重组SEMA4G蛋白体外处理肝癌细胞，发现其通过抑制ERK磷酸化降低细胞迁移和侵袭能力，提示SEMA4G在肝癌治疗中的潜在靶点作用。
2. **文献名称**: *"SEMA4G Acts as a Novel HIV-1 Entry Cofactor by Binding to Viral Envelope Glycoproteins"*
**作者**: Smith JL, et al. (2018)
**摘要**: 通过重组SEMA4G蛋白与HIV-1包膜蛋白的互作实验，证实SEMA4G促进病毒与宿主细胞膜融合，阻断其功能可显著抑制HIV感染，为抗病毒治疗提供新策略。
3. **文献名称**: *"Recombinant SEMA4G Modulates Axon Guidance by Competing with Endogenous Semaphorins"*
**作者**: Li X, et al. (2022)
**摘要**: 在神经元模型中发现，外源性重组SEMA4G蛋白通过竞争性结合神经纤毛蛋白(Neuropilin-1)，逆转SEMA3A介导的轴突导向抑制，揭示了其在神经发育中的双向调节机制。
如需真实文献，建议检索PubMed/Google Scholar关键词：**SEMA4G recombinant protein**、**SEMA4G function** 或 **SEMA4G signaling**。
SEMA4G (Semaphorin-4G) is a member of the semaphorin protein family, a group of signaling molecules initially identified for their roles in axonal guidance during neuronal development. Semaphorins are characterized by a conserved ~500-amino acid Sema domain, which mediates receptor binding and biological activity. Over time, research has expanded their known functions to include immune regulation, angiogenesis, and tumor progression. SEMA4G, a transmembrane class IV semaphorin, is distinguished by its immunoglobulin-like domain and cytoplasmic tail, which facilitate interactions with cell surface receptors like plexins and neuropilins.
The biological significance of SEMA4G remains under active investigation. Studies suggest its involvement in modulating immune responses, particularly in T-cell activation and dendritic cell function. Additionally, SEMA4G has been implicated in vascular development and cancer metastasis, where it may influence cell adhesion, migration, and microenvironment signaling. Dysregulation of semaphorins, including SEMA4G, has been linked to pathological conditions such as autoimmune disorders, cardiovascular diseases, and tumor invasiveness.
Recombinant SEMA4G protein is engineered using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications. This involves cloning the SEMA4G gene into expression vectors, followed by transfection, protein purification (often via affinity tags like His or Fc), and functional validation. The recombinant form enables precise study of SEMA4G’s structure-function relationships, receptor interactions, and downstream signaling pathways in vitro and in vivo. It also serves as a critical tool for developing therapeutic antibodies or inhibitors targeting SEMA4G-related diseases.
Current research focuses on elucidating SEMA4G’s dual roles in immune homeostasis and cancer biology, aiming to harness its therapeutic potential while addressing challenges in specificity and off-target effects. Its recombinant form accelerates translational studies, bridging mechanistic insights to clinical applications.
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