Goat Anti-Mouse LGALS7 polyclonal antibody for ELISA(Det), WB. 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, 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 consisting of two CRDs joined by a linker peptide. Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified non-classical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell-surface glycoproteins. Mouse Galectin-7 is a prototype monomeric galectin. It is expressed in stratified epithelia and is significantly down-regulated in squamous cell carcinomas. Galectin-7 is a pro-apoptotic protein that is highly induced by the tumor suppressor protein p53. It functions intracellularly upstream of JNK activation to enhance cytochrome c release during apoptosis. Galectin-7 may also be involved in cell-cell and cell-matrix interactions and exogenous galectin has been found to accelerate the re-epithelialization of wounds.
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