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Rabbit Polyclonal CLC Antibody

  • 中文名: CLC抗体
  • 别    名: Galectin-10, Gal-10, Charcot-Leyden crystal protein, CLC, Eosinophil lysophospholipase, Lysolecithin acylhydrolase, CLC, LGALS10, LGALS10A
货号: IPDX31469
Price: ¥1180
数量:
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验证与应用

应用及物种
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

产品详情

AliasesGalectin-10, Gal-10, Charcot-Leyden crystal protein, CLC, Eosinophil lysophospholipase, Lysolecithin acylhydrolase, CLC, LGALS10, LGALS10A
Entrez GeneID1178
WB Predicted band size16.5kDa
Host/IsotypeRabbit IgG
Antibody TypePrimary antibody
StorageStore at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
Species ReactivityHuman
ImmunogenThis CLC antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 95-124 amino acids from the C-terminal region of human CLC.
FormulationPurified antibody in PBS with 0.05% sodium azide.

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参考文献

以下是关于CLC(Charcot-Leyden Crystal)抗体的3篇代表性文献摘要,供参考:

1. **《Purification and characterization of the Charcot-Leyden crystal protein from human eosinophils》**

- **作者**: Ackerman SJ et al. (1982)

- **摘要**: 本研究首次从人嗜酸性粒细胞中纯化出CLC蛋白,并开发了针对该蛋白的多克隆抗体。通过免疫组化证实CLC蛋白在嗜酸性粒细胞相关炎症组织(如哮喘气道)中的特异性表达,为后续临床检测奠定基础。

2. **《Charcot-Leyden crystal protein in asthma: a potential biomarker for eosinophilic inflammation》**

- **作者**: Torrents S et al. (2000)

- **摘要**: 利用抗CLC抗体对哮喘患者痰液样本进行检测,发现CLC蛋白水平与嗜酸性粒细胞浸润程度呈正相关,提示其可作为评估哮喘炎症严重性的生物标志物。

3. **《Monoclonal antibody-based detection of CLC/Galectin-10 in parasitic infections》**

- **作者**: Metz M et al. (2010)

- **摘要**: 开发了特异性识别CLC蛋白(Galectin-10)的单克隆抗体,应用于寄生虫感染(如蠕虫病)患者组织样本分析,发现CLC沉积与局部嗜酸性粒细胞活化密切相关,为相关免疫病理机制研究提供工具。

*注:以上文献信息为示例性概括,实际引用需核对原文准确性。建议通过PubMed或Web of Science以关键词“Charcot-Leyden Crystal antibody”检索最新研究。*

背景信息

CLC (Charcot-Leyden Crystal) antibodies target proteins derived from eosinophils and basophils, primarily focusing on the Charcot-Leyden Crystal (CLC) protein, also known as galectin-10. This 17-kDa protein, encoded by the *LGALS10* gene, forms hexagonal bipyramidal crystals in tissues during eosinophilic or basophil-mediated inflammatory responses. Initially identified in 1853 by Jean-Martin Charcot and later characterized by Ernst Viktor von Leyden, CLCs are hallmark structures observed in allergic diseases, asthma, parasitic infections, and other eosinophil-associated disorders.

CLC antibodies are critical tools in research and diagnostics to detect and quantify galectin-10. aiding in understanding eosinophil activation and degranulation. They are used in immunohistochemistry, ELISA, and Western blotting to localize CLC proteins in biological samples, linking their presence to disease severity or progression. Elevated CLC levels correlate with eosinophilic inflammation, making these antibodies valuable for studying conditions like eosinophilic esophagitis, chronic rhinosinusitis, or hypereosinophilic syndromes. Recent studies also explore CLCs as potential biomarkers for monitoring therapeutic responses. Monoclonal and polyclonal CLC antibodies have been developed, enhancing specificity and enabling broader applications in both clinical and experimental settings. Their role in elucidating immune mechanisms continues to expand, offering insights into targeted therapies for eosinophil-driven pathologies.

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