WB | 1/1000 | Human,Mouse,Rat |
IF | 咨询技术 | Human,Mouse,Rat |
IHC | 咨询技术 | Human,Mouse,Rat |
ICC | 技术咨询 | Human,Mouse,Rat |
FCM | 咨询技术 | Human,Mouse,Rat |
Elisa | 咨询技术 | Human,Mouse,Rat |
Aliases | Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase, Alpha-1,2-glucosyltransferase ALG10-A, Alpha-2-glucosyltransferase ALG10-B, Asparagine-linked glycosylation protein 10 homolog B, Potassium channel regulator 1, ALG10B, KCR1 |
Entrez GeneID | 144245 |
WB Predicted band size | 55.4kDa |
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 |
Immunogen | This ALG10B antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 324-353 amino acids from the C-terminal region of human ALG10B. |
Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于ALG10B抗体的3篇模拟参考文献示例(注:ALG10B相关研究较少,以下内容为虚构示例,仅作格式参考):
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1. **文献名称**: *ALG10B Antibody Development for Glycosylation Analysis in Cancer Cells*
**作者**: Smith J, et al.
**摘要**: 本研究开发了一种特异性识别ALG10B蛋白的单克隆抗体,用于分析其在乳腺癌细胞中的表达及定位。抗体验证显示其对内源性ALG10B具有高亲和力,并通过免疫印迹和免疫荧光证实ALG10B在细胞高尔基体中的功能。
2. **文献名称**: *Structural Characterization of ALG10B in N-linked Glycosylation Using Polyclonal Antibodies*
**作者**: Lee H, et al.
**摘要**: 通过兔源多克隆抗体探究ALG10B在N-糖基化中的结构作用,发现ALG10B缺失导致糖蛋白折叠异常。抗体应用于蛋白质免疫沉淀(IP)和质谱分析,揭示其与内质网应激通路的关联。
3. **文献名称**: *ALG10B as a Biomarker in Autoimmune Disorders: An Antibody-based Study*
**作者**: Garcia R, et al.
**摘要**: 利用ALG10B抗体检测类风湿性关节炎患者血清样本,发现ALG10B水平与疾病活动度呈正相关,提示其可能作为新型炎症标志物,并探讨了抗体在诊断试剂开发中的潜力。
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如需真实文献,建议通过PubMed或Google Scholar以“ALG10B antibody”或“ALG10B function”为关键词检索。
The ALG10B antibody is designed to target the ALG10B protein, a member of the ALG (asparagine-linked glycosylation) family involved in N-glycan biosynthesis. ALG10B, also known as alpha-1.2-glucosyltransferase, plays a critical role in the endoplasmic reticulum (ER) by catalyzing the transfer of the second glucose residue to the lipid-linked oligosaccharide (LLO) precursor during N-glycosylation. This process is essential for proper protein folding, quality control, and cellular secretion. Dysregulation of ALG10B has been implicated in congenital disorders of glycosylation (CDGs), a group of metabolic diseases characterized by defective protein glycosylation, leading to multisystemic clinical manifestations.
The ALG10B antibody is primarily utilized in research to study ER-associated glycosylation mechanisms, protein trafficking, and disease models of CDGs. It enables detection and localization of ALG10B in various tissues and cell lines via techniques like Western blotting, immunofluorescence, and immunohistochemistry. Recent studies also explore its potential role in cancer, as aberrant glycosylation is a hallmark of tumor progression and metastasis.
Despite its specialized applications, ALG10B antibodies remain niche tools, with limited commercial availability. Ongoing research aims to clarify its regulatory interactions within the glycosylation pathway and therapeutic relevance in glycosylation-related disorders.
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