| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Erap1 |
| Uniprot No | Q9NZ08 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-941aa |
| 氨基酸序列 | MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDGVKGMDGFCSRSQHSSSSSHWHQEGVDVKTMMNTWTLQKGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERM |
| 预测分子量 | 107,2 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ERAP1重组蛋白的3篇参考文献，按文献名称、作者及摘要概括整理：
---
1. **文献名称**: "The role of endoplasmic reticulum aminopeptidase 1 in antigen processing"
**作者**: Saric, T., et al.
**摘要**: 该研究首次证实ERAP1在内质网中对MHC I类分子结合的抗原前体进行氨基末端修剪，调控抗原呈递。重组ERAP1蛋白体外实验显示其选择性剪切特定长度多肽，影响T细胞识别。
---
2. **文献名称**: "Genetic and functional characterization of ERAP1 polymorphisms in autoimmune diseases"
**作者**: Yan, J., et al.
**摘要**: 通过分析ERAP1基因多态性与强直性脊柱炎等疾病的关联，发现特定突变(如rs30187)影响重组ERAP1酶活性，导致抗原肽修剪异常，从而改变MHC I呈递并触发自身免疫反应。
---
3. **文献名称**: "Structural basis for antigenic peptide trimming by ERAP1"
**作者**: Kochan, G., et al.
**摘要**: 利用重组ERAP1蛋白的晶体结构解析，揭示其底物结合域的动态构象变化机制，阐明其如何根据多肽长度选择性切割，为设计ERAP1抑制剂治疗自身免疫病提供结构依据。
---
如需更多文献或特定研究方向(如重组蛋白纯化方法)，可进一步补充说明。
ERAP1 (Endoplasmic Reticulum Aminopeptidase 1) is a multifunctional enzyme belonging to the M1 zinc metallopeptidase family, primarily involved in antigen processing and immune regulation. Located in the endoplasmic reticulum, it trims precursor peptides to optimal lengths (typically 8-10 residues) for loading onto MHC class I molecules, a critical step in adaptive immunity. By shaping the peptide repertoire presented to CD8+ T cells, ERAP1 influences immune surveillance against pathogens and cancerous cells while maintaining self-tolerance.
Beyond its canonical role, ERAP1 exhibits dual enzymatic activities: aminopeptidase and endopeptidase, with substrate specificity modulated by cellular redox conditions. Structurally, it contains four domains: a catalytic domain, a bridging domain, and two β-sheet domains, with its C-terminal domain playing key roles in substrate binding and allosteric regulation.
Genetic studies have linked ERAP1 polymorphisms to autoimmune diseases (e.g., ankylosing spondylitis, psoriasis arthritis) and cancer progression. Certain variants alter enzymatic activity or substrate preference, affecting antigen presentation efficiency and inflammatory responses. Notably, ERAP1's involvement in cytokine receptor shedding (e.g., IL-6R, TNF-α receptor 1) further connects it to inflammatory pathways.
Recombinant ERAP1 proteins, typically produced in mammalian or insect expression systems, enable mechanistic studies of these disease associations. Researchers employ purified ERAP1 to characterize enzymatic kinetics, screen inhibitors, and investigate structural dynamics through crystallography and cryo-EM. Recent therapeutic strategies explore ERAP1 modulation as a potential treatment for autoimmune disorders and cancer immunotherapy, particularly through engineering MHC-I-restricted neoantigens. However, challenges remain in understanding its substrate selection mechanisms and tissue-specific regulation, making recombinant protein tools essential for unraveling its complex biology.
×
