CD43 Monoclonal / PE-Vio615 / REA840
Product Details
Description | Clone REA840 recognizes the mouse CD43 antigen, a glycosylated protein also known as leukosialin or sialophorin, which is expressed on IL-7–responsive pro–B cells, plasma cells, peritoneal and spleen CD5+ B cells (B-1 cells), granulocytes, monocytes, macrophages, platelets, NK cells, thymocytes, peripheral cytotoxic T cells, and most T helper cells. CD43 is not expressed on resting conventional peripheral B cells. Thus, resting B cells are easily identified by the lack of CD43 expression. | Additional information: Clone REA840 displays negligible binding to Fc receptors. | |
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Conjugate | PE-Vio615 | |
Clone | REA840 | |
Target Species | Mouse | |
Applications | FC | |
Supplier | Miltenyi Biotec | |
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About CD43
This gene encodes a highly sialylated glycoprotein that functions in antigen-specific activation of T cells, and is found on the surface of thymocytes, T lymphocytes, monocytes, granulocytes, and some B lymphocytes. It contains a mucin-like extracellular domain, a transmembrane region and a carboxy-terminal intracellular region. The extracellular domain has a high proportion of serine and threonine residues, allowing extensive O-glycosylation, and has one potential N-glycosylation site, while the carboxy-terminal region has potential phosphorylation sites that may mediate transduction of activation signals. Different glycoforms of this protein have been described. In stimulated immune cells, proteolytic cleavage of the extracellular domain occurs in some cell types, releasing a soluble extracellular fragment. Defects in expression of this gene are associated with Wiskott-Aldrich syndrome. [provided by RefSeq, Sep 2017]
This gene encodes a highly sialylated glycoprotein that functions in antigen-specific activation of T cells, and is found on the surface of thymocytes, T lymphocytes, monocytes, granulocytes, and some B lymphocytes. It contains a mucin-like extracellular domain, a transmembrane region and a carboxy-terminal intracellular region. The extracellular domain has a high proportion of serine and threonine residues, allowing extensive O-glycosylation, and has one potential N-glycosylation site, while the carboxy-terminal region has potential phosphorylation sites that may mediate transduction of activation signals. Different glycoforms of this protein have been described. In stimulated immune cells, proteolytic cleavage of the extracellular domain occurs in some cell types, releasing a soluble extracellular fragment. Defects in expression of this gene are associated with Wiskott-Aldrich syndrome. [provided by RefSeq, Sep 2017]
About PE-Vio615
PE-Vio®615 from Miltenyi Biotec has an excitation peak at 565 nm and an emission peak at 619 nm. It is spectrally similar to PE-eFluor™ 610, PE-Dazzle 594 and PE-CF®594
PE-Vio®615 from Miltenyi Biotec has an excitation peak at 565 nm and an emission peak at 619 nm. It is spectrally similar to PE-eFluor™ 610, PE-Dazzle 594 and PE-CF®594
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Validation References
PMID 2144340 | |
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PMID 2347365 | |
PMID 11238599 | |
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