Mouse Galectin-7 Biotinylated Antibody
Mouse Galectin-7 Biotinylated Antibody Summary
Accession # Q99ML7
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Mouse Galectin-7 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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. 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 (1‑4).
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 (5). 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 (6).
- Rabinovich, A. et al. (2002) TRENDS in Immunol. 23:313.
- Rabinovich, A. et al. (2002) J. Leukocyte Biology 71:741.
- Hughes, R.C. (2002) Biochimie 83:667.
- R&D Systems' Cytokine Bulletin, Summer (2002).
- Kuwabara, I. et al. (2002) J. Biol. Chem. 277:3487.
- Cao, Z. et al. (2002) J. Biol. Chem. 277:42299.
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