| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DLG1 |
| Uniprot No | Q12959 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-90aa |
| 氨基酸序列 | MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALI DIQEFYEVTLLDNPKCIDRSKPSEPIQPVNTWEISSLPSS |
| 预测分子量 | 36 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DLG1重组蛋白的参考文献示例(注：文献为假设性示例，实际引用时请核实真实来源)：
1. **文献名称**: "Recombinant DLG1 PDZ domains suppress hepatitis C virus replication"
**作者**: Müller A, et al.
**摘要**: 本研究利用重组表达的DLG1 PDZ结构域，揭示了其与HCV核心蛋白的相互作用，证明其可通过竞争性结合抑制病毒复制，为抗病毒治疗提供新策略。
2. **文献名称**: "Expression and purification of the DLG1/SAP97 protein for structural analysis"
**作者**: Johnson R, et al.
**摘要**: 开发了一种高效的大肠杆菌表达系统，用于纯化重组DLG1蛋白，并通过X射线晶体学解析其三维结构，为研究其支架蛋白功能奠定基础。
3. **文献名称**: "DLG1 regulates cell polarity through interaction with LKB1 kinase"
**作者**: Tanaka K, et al.
**摘要**: 通过体外结合实验发现，重组DLG1蛋白与LKB1激酶直接互作，调控上皮细胞极性，揭示了DLG1在发育和癌症转移中的潜在作用。
4. **文献名称**: "Recombinant DLG1 rescues synaptic defects in a neuronal model"
**作者**: Chen L, et al.
**摘要**: 在DLG1缺陷的神经元中，外源性重组DLG1蛋白恢复了突触后密度蛋白的聚集，证实其在突触可塑性和神经系统疾病中的关键功能。
**建议**：实际研究中，可通过PubMed或Google Scholar搜索关键词“DLG1 recombinant protein”“SAP97 expression”等获取最新文献。
**Background of DLG1 Recombinant Protein**
DLG1 (Discs Large Homolog 1), also known as SAP97 (Synapse-Associated Protein 97), is a member of the membrane-associated guanylate kinase (MAGUK) family. It plays a critical role in maintaining cell polarity, regulating cell adhesion, and organizing synaptic signaling complexes. Structurally, DLG1 contains multiple protein-protein interaction domains, including three PDZ domains, an SH3 domain, and a catalytically inactive guanylate kinase (GK) domain. These domains enable DLG1 to act as a scaffolding protein, facilitating interactions with transmembrane receptors, cytoskeletal components, and signaling molecules.
DLG1 is widely expressed in epithelial tissues and neurons, where it stabilizes tight junctions, adherens junctions, and postsynaptic densities. In neurons, it participates in synaptic plasticity by anchoring glutamate receptors and modulating neurotransmitter release. Dysregulation of DLG1 has been implicated in various pathological conditions, including cancers, neurological disorders, and cardiovascular diseases. For instance, loss of DLG1 expression disrupts epithelial integrity, promoting tumor invasiveness, while mutations are linked to intellectual disabilities and autism spectrum disorders.
Recombinant DLG1 protein is engineered *in vitro* using expression systems (e.g., bacterial, insect, or mammalian cells) to produce purified, functional forms of the protein for research. It serves as a vital tool for studying DLG1’s interactions, structure-function relationships, and role in disease mechanisms. Tagged versions (e.g., His-tag, GFP-tag) allow efficient purification and visualization in assays. Studies utilizing recombinant DLG1 have advanced understanding of cellular signaling networks, drug target discovery, and therapeutic strategies for DLG1-associated disorders. Its application spans biochemistry, cell biology, and translational research, underscoring its importance in both basic and clinical sciences.
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