| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GULP1 |
| Uniprot No | Q9UBP9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-304aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMNRAFSR KKDKTWMHTP EALSKHFIPY NAKFLGSTEV EQPKGTEVVR DAVRKLKFAR HIKKSEGQKI PKVELQISIY GVKILEPKTK EVQHNCQLHR ISFCADDKTD KRIFTFICKD SESNKHLCYV FDSEKCAEEI TLTIGQAFDL AYRKFLESGG KDVETRKQIA GLQKRIQDLE TENMELKNKV QDLENQLRIT QVSAPPAGSM TPKSPSTDIF DMIPFSPISH QSSMPTRNGT QPPPVPSRST EIKRDLFGAE PFDPFNCGAA DFPPDIQSKL DEMQEGFKMG LTLEGTVFCL DPLDSRC |
| 预测分子量 | 37 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GULP1重组蛋白的3篇参考文献示例(注：文献为假设性示例，实际研究中请根据具体论文调整)：
1. **文献名称**：*Structural and Functional Analysis of GULP1 in Apoptotic Engulfment*
**作者**：Smith A, et al.
**摘要**：本研究通过重组表达GULP1蛋白，解析其磷酸酪氨酸结合结构域(PTB)的结构，并证明其在凋亡细胞吞噬过程中与下游信号适配体的相互作用机制。
2. **文献名称**：*GULP1 Recombinant Protein Enhances TGF-β Signaling via Smad2/3 Activation*
**作者**：Lee J, et al.
**摘要**：利用昆虫细胞系统表达GULP1重组蛋白，发现其通过调控TGF-β受体稳定性促进Smad2/3磷酸化，为癌症治疗提供潜在靶点。
3. **文献名称**：*Expression Optimization and Functional Characterization of Human GULP1 in E. coli*
**作者**：Zhang Y, et al.
**摘要**：优化GULP1重组蛋白在大肠杆菌中的可溶性表达条件，验证其与低密度脂蛋白受体家族(LRP1/2)的结合活性，揭示其在胆固醇代谢中的作用。
如需具体文献，建议在PubMed或Web of Science中检索关键词 **"GULP1 recombinant protein"** 或 **"GULP1 expression and function"**。
GULP1 (engulfment adaptor PTB domain-containing protein 1) is a cytosolic adaptor protein involved in cellular engulfment processes, apoptotic cell clearance, and intracellular signaling pathways. Initially identified for its role in phagocytosis, GULP1 interacts with receptors such as LRP1 (low-density lipoprotein receptor-related protein 1) and participates in the internalization of apoptotic cells, pathogens, and cellular debris. Structurally, it contains a phosphotyrosine-binding (PTB) domain that mediates protein-protein interactions, facilitating connections with signaling molecules and membrane receptors. This domain enables GULP1 to act as a scaffold, coordinating downstream effectors in pathways like TGF-β signaling and cholesterol homeostasis.
Research highlights GULP1's regulatory functions in neurobiology and disease. In the nervous system, it modulates synaptic pruning and neuronal survival by influencing engulfment mechanisms. Dysregulation of GULP1 has been implicated in neurodegenerative disorders, including Alzheimer's disease, where impaired clearance of amyloid-β aggregates correlates with disrupted phagocytic activity. Additionally, GULP1 interacts with autophagy-related proteins, linking it to cellular quality control processes. In cancer, GULP1 exhibits context-dependent roles, acting as a tumor suppressor by promoting apoptosis in some contexts or supporting tumor progression through immune evasion in others.
Recombinant GULP1 protein, produced via bacterial or mammalian expression systems, is widely used to study its molecular interactions, structural dynamics, and therapeutic potential. Studies leveraging recombinant GULP1 have clarified its binding partners, post-translational modifications, and functional domains. Ongoing research explores its application in modulating engulfment pathways for treating inflammatory diseases, neurodegeneration, and cancer. The protein's dual role in homeostasis and pathology underscores its biological significance and highlights its potential as a therapeutic target.
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