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Recombinant Human MOAP1 protein

  • 中文名: 调控因子1(MOAP1)重组蛋白
  • 别    名: MOAP1;PNMA4;Modulator of apoptosis 1
货号: PA1000-1994
Price: ¥询价
数量:
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产品详情

纯度>85%SDS-PAGE.
种属Human
靶点MOAP1
Uniprot NoQ96BY2
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-351aa
氨基酸序列MTLRLLEDWCRGMDMNPRKALLIAGISQSCSVAEIEEALQAGLAPLGEYR LLGRMFRRDENRKVALVGLTAETSHALVPKEIPGKGGIWRVIFKPPDPDN TFLSRLNEFLAGEGMTVGEL SRALGHENGSLDPEQGMIPEMWAPMLAQ ALEALQPALQCLKYKKLRVFSGRESPEPGEEEFGRWMFHTTQMIKAWQVP DVEKRRRLLESLRGPALDVIRVLKINNPLITVDECLQALEEVFGVTDNPR ELQVKYLTTYQKDEEKLSAYVLRLEPLLQKLVQRGAIERDAVNQARLDQV IAGAVHKTIRRELNLPEDGPAPGFLQLLVLIKDYEAAEEEEALLQAILEG NFT
预测分子量42 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.

参考文献

以下是关于MOAP1重组蛋白的3篇文献示例(注:文献信息为模拟示例,实际需根据具体文献调整):

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1. **文献名称**:*MOAP1 Recombinant Protein Induces Bax-dependent Apoptosis in Colorectal Cancer Cells*

**作者**:Chen L. et al.

**摘要**:研究报道了通过大肠杆菌表达系统成功制备重组MOAP1蛋白,并发现其通过激活Bax蛋白促进结直肠癌细胞凋亡。实验验证了重组蛋白的体外促凋亡活性及与线粒体途径的关联。

2. **文献名称**:*Expression and Functional Characterization of Human MOAP1 in a Mammalian Cell System*

**作者**:Wang Y. et al.

**摘要**:作者利用哺乳动物细胞表达体系制备了带有His标签的重组MOAP1蛋白,通过亲和层析纯化后,证实其能够增强化疗药物诱导的肿瘤细胞凋亡,提示其在联合治疗中的潜在应用价值。

3. **文献名称**:*Structural Insights into MOAP1 Interaction with Bcl-2 Family Proteins*

**作者**:Kumar S. et al.

**摘要**:该研究通过重组MOAP1蛋白的晶体结构解析,揭示了其与Bcl-2家族蛋白(如Bax)的关键结合域,为设计靶向MOAP1凋亡通路的抗癌药物提供了结构基础。

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**说明**:以上文献为模拟内容,实际研究中建议通过PubMed、Web of Science或Google Scholar检索关键词“MOAP1 recombinant protein”或结合具体研究领域筛选文献。

背景信息

MOAP1 (Modulator of Apoptosis 1), also known as MAP-1. is a mitochondrial protein implicated in the intrinsic pathway of apoptosis. Initially identified as a Bax-associated protein, it plays a regulatory role in programmed cell death by interacting with components of the Bcl-2 family. MOAP1 promotes Bax activation, facilitating mitochondrial outer membrane permeabilization (MOMP) and subsequent cytochrome c release, which triggers caspase activation and apoptosis. Its activity is tightly linked to the tumor suppressor RASSF1A (Ras association domain family 1A), forming a complex that enhances pro-apoptotic signaling under stress conditions. This interaction highlights MOAP1's role in bridging upstream stress signals to downstream mitochondrial apoptosis machinery.

Structurally, MOAP1 contains a BH3-like domain critical for its interaction with Bax, though it is not classified as a traditional Bcl-2 family member. Studies suggest MOAP1 functions in both p53-dependent and -independent apoptotic pathways, making it a versatile mediator of cell fate. Dysregulation of MOAP1 has been associated with cancer progression, where reduced expression correlates with chemotherapy resistance and poor prognosis, emphasizing its potential as a therapeutic target.

Recombinant MOAP1 protein is typically produced in bacterial (e.g., E. coli) or mammalian expression systems, often fused with tags (e.g., His-tag) for purification via affinity chromatography. This engineered protein enables in vitro studies to dissect MOAP1's molecular interactions, structural features, and functional domains. Researchers utilize recombinant MOAP1 to investigate its binding kinetics with Bax, Bcl-2 proteins, and RASSF1A, as well as its role in reconstituting apoptotic pathways in cell-free systems. Additionally, it serves as a tool for screening small molecules that modulate MOAP1 activity, with implications for developing pro-apoptotic therapies in oncology. Ongoing research explores its involvement in neurodegenerative diseases and ischemic injury, broadening its biomedical relevance.

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