| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/10-1/50 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 1/5000-1/10000 | Human,Mouse,Rat |
| Aliases | EDEM |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human, Mouse |
| Immunogen | Synthetic peptide of human EDEM1 |
| Formulation | Purified antibody in PBS with 0.05% sodium azide and 50% glycerol. |
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以下是3篇关于EDEM1抗体的代表性文献(信息基于公开论文整理，非实时数据库检索)：
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1. **文献名称**: "EDEM1 accelerates the trimming of α1.2-linked mannose on the C branch of N-glycans"
**作者**: Hosokawa N. et al.
**摘要**: 本研究揭示了EDEM1通过识别内质网中错误折叠糖蛋白的高甘露糖结构，加速其α1.2-甘露糖苷酶介导的修剪，从而促进ERAD途径的底物靶向降解。实验中使用了EDEM1抗体验证其在内质网的定位及与底物的相互作用。
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2. **文献名称**: "Structural basis of EDEM3-driven mannose trimming in glycoprotein ERAD"
**作者**: Mast S.W. et al.
**摘要**: 通过X射线晶体学解析EDEM1与底物复合物结构，阐明其特异性识别甘露糖结构的分子机制。研究利用EDEM1抗体进行免疫共沉淀实验，证实其与ERAD相关伴侣蛋白(如OS-9)的协同作用。
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3. **文献名称**: "EDEM1 regulates ER-associated degradation by accelerating dissociation of BiP/GRP78 from unfolded proteins"
**作者**: Groisman B. & Kornfeld S.
**摘要**: 发现EDEM1通过竞争性结合未折叠蛋白，促进分子伴侣BiP/GRP78的释放，从而加速错误折叠蛋白进入ERAD通路。研究通过EDEM1抗体敲低实验证明其对ERAD效率的关键调控作用。
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**注**：以上内容为简化示例，实际文献引用需通过PubMed/Google Scholar检索最新论文，并核对作者、标题及摘要准确性。如需具体文献链接或DOI，可补充说明。
The EDEM1 (ER degradation-enhancing alpha-mannosidase-like protein 1) antibody is a tool used to study a key player in endoplasmic reticulum (ER)-associated degradation (ERAD), a quality control pathway that targets misfolded glycoproteins for proteasomal degradation. EDEM1. a member of the glycosyl hydrolase 47 family, lacks enzymatic activity but acts as a lectin-like chaperone to recognize and direct improperly folded glycoproteins for ERAD. It facilitates the removal of terminally misfolded proteins by extracting them from the calnexin/calreticulin folding cycle and promoting their retrotranslocation to the cytosol via interactions with ERAD machinery components like SEL1L and HRD1.
Research suggests EDEM1 specifically trims mannose residues on N-linked glycans, marking substrates for degradation. Its expression is upregulated during ER stress through the unfolded protein response (UPR), linking it to cellular stress adaptation. Antibodies against EDEM1 are widely used in studies of protein quality control, ER stress-related diseases (e.g., neurodegenerative disorders, diabetes), and cancer biology. Common applications include Western blotting, immunofluorescence, and co-immunoprecipitation to investigate EDEM1 localization, protein interactions, or expression dynamics under stress conditions. Validation often involves knockout cell lines to confirm specificity. Commercial EDEM1 antibodies are typically raised against conserved regions (e.g., N-terminal residues 1-300) in hosts like rabbit or mouse.
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