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Specification
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Product name
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Galectin-3 Blocking Antibody 8-2
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Description
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Mouse monoclonal antibody raised against a full-length recombinant Galectin-3. Monoclonal antibodies block the binding of Galectin-3 to laminin.
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Immunogen
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Recombinant full length protein. This information is proprietary to RMi and/or its suppliers.
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Source/Isotype
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Mouse IgG2b
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Reactivity
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Human
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Specificity
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Detects human Galectin-3 in ELISAs. In indirect ELISAs, no cross-reactivity with recombinant human Galectin-1, Galectin-9 is observed.
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Purification
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Protein G purified from hybridoma culture supernatant
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Application
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ELISA, others unspecified.
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Form
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Liquid
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Storage Buffer
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In 1✕PBS, pH 7.2
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Storage Instruction
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Shipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -20°C or lower long term.. Aliquot to avoid repeated freezing and thawing.
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Size
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25ug, 100ug, 500ug
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Data Background
The galectins constitute a large family of carbohydrate-binding proteins with specificity for N-acetyl-lactosamine-containing glycoproteins. At least 14 mammalian galectins, which share structural similarities in their carbohydrate recognition domains (CRD), have been identified. The galectins have been classified into the prototype galectins (-1, -2, -5, -7, -10, -11, -13, -14), which contain one CRD and exist either as a monomer or a noncovalent homodimer; the chimera galectins (Galectin-3) containing one CRD linked to a nonlectin domain; and the tandem-repeat galectins (-4, -6, -8, -9, -12) consisting of two CRDs joined by a linker peptide. Members of the galectin family have been implicated in a variety of biological functions including cell adhesion, growth regulation, cytokine production, T-cell apoptosis, and immune responses. Galectin-3 is involved in several diverse biological functions. Galectin-3 binds IgE. Galectin-3 is an unusual protein in that it can be found both extracellularly and intracellularly. Intracellularly, galectin-3 can localize to the cytoplasm, nucleus, or both, depending on cell type and experimental conditions. Nuclear galectin-3 has been identified as a pre-mRNA splicing factor. Galectin-3 production has been shown to increase during inflammation and in obesity, and the protein itself can have an inflammatory effect under certain conditions. Galectin-3 forms a complex with α3, β1 integrin to act as a surface receptor on endothelial cells for the NG2 proteoglycan, which triggers cell motility and angiogenesis. In addition to these functions, galectin-3 is also a required factor for the terminal differentiation of epithelial cells.
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