纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PAG1 |
Uniprot No | Q9NWQ8 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 38-432aa |
氨基酸序列 | SSCDREKKPRQHSGDHENLMNVPSDKEMFSRSVTSLATDAPASSEQNGALTNGDILSEDSTLTCMQHYEEVQTSASDLLDSQDSTGKPKCHQSRELPRIPPESAVDTMLTARSVDGDQGLGMEGPYEVLKDSSSQENMVEDCLYETVKEIKEVAAAAHLEKGHSGKAKSTSASKELPGPQTEGKAEFAEYASVDRNKKCRQSVNVESILGNSCDPEEEAPPPVPVKLLDENENLQEKEGGEAEESATDTTSETNKRFSSLSYKSREEDPTLTEEEISAMYSSVNKPGQLVNKSGQSLTVPESTYTSIQGDPQRSPSSCNDLYATVKDFEKTPNSTLPPAGRPSEEPEPDYEAIQTLNREEEKATLGTNGHHGLVPKENDYESISDLQQGRDITRL |
预测分子量 | 50.0 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PAG1重组蛋白的3篇参考文献概览:
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1. **文献名称**: *"Expression and Functional Analysis of Recombinant PAG1 in T-Cell Signaling"*
**作者**: Müller et al., 2016
**摘要**: 该研究报道了在大肠杆菌中成功表达并纯化重组人源PAG1蛋白,验证其与Csk激酶的结合能力。通过体外实验证明,重组PAG1可抑制T细胞受体下游信号通路,揭示了其在负向调控免疫反应中的作用机制。
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2. **文献名称**: *"Structural Insights into PAG1-Mediated Signal Regulation via Recombinant Protein Crystallography"*
**作者**: Kimura et al., 2019
**摘要**: 研究团队利用昆虫细胞系统表达重组PAG1蛋白,并通过X射线晶体学解析其三维结构。发现PAG1的磷酸化位点对其招募Csk激酶及调控脂筏微区信号传导至关重要,为靶向PAG1的免疫治疗提供结构基础。
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3. **文献名称**: *"Recombinant PAG1 as a Tool for Studying Lipid Raft Dynamics in Cancer Cells"*
**作者**: Vargas et al., 2021
**摘要**: 通过哺乳动物细胞表达系统制备带有标签的重组PAG1蛋白,并应用于乳腺癌细胞模型。结果表明,外源性PAG1可改变脂筏稳定性,影响EGFR信号通路的激活,提示其在肿瘤微环境中的潜在调控作用。
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注:上述文献为示例性概括,实际引用时需根据真实发表论文调整信息。建议通过PubMed或Web of Science以“PAG1 recombinant protein”为关键词检索最新文献。
PAG1 (Phosphoprotein Associated with Glycosphingolipid-enriched microdomains 1), also known as Csk-binding protein (Cbp), is a transmembrane adaptor protein widely expressed in immune cells, including T cells, B cells, and mast cells. It plays a critical role in regulating signal transduction by acting as a scaffold to recruit signaling molecules within lipid rafts, specialized membrane microdomains enriched in cholesterol and glycosphingolipids. Structurally, PAG1 contains an extracellular N-terminal domain, a single transmembrane helix, and a cytoplasmic tail with multiple tyrosine phosphorylation sites. These sites allow interactions with Src family kinases (SFKs) and their negative regulator, C-terminal Src kinase (CSK), forming a feedback loop to modulate immune receptor signaling.
In resting cells, PAG1 is constitutively phosphorylated and bound to CSK, which suppresses SFK activity. Upon receptor activation (e.g., T-cell receptor or B-cell receptor engagement), PAG1 undergoes dephosphorylation, releasing CSK and enabling SFK activation. This dynamic regulation ensures balanced immune responses, preventing hyperactivation or autoimmunity. Dysregulation of PAG1 has been linked to immune disorders and cancers, where its role as a tumor suppressor or promoter appears context-dependent. For instance, PAG1 downregulation in certain cancers correlates with increased SFK activity and tumor progression.
Recombinant PAG1 proteins are engineered to study these mechanisms, often produced in mammalian or bacterial expression systems. They retain functional domains for phosphorylation and protein interactions, enabling in vitro studies on immune signaling pathways, drug discovery, and structural analyses. Researchers also use PAG1 variants to dissect its regulatory roles in autoimmune diseases, allergies, and cancer immunotherapy. By modulating PAG1-CSK-SFK interactions, recombinant forms provide insights into therapeutic strategies targeting immune checkpoint pathways or oncogenic signaling.
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