Details of Functionality | Measured by its ability to agglutinate human red blood cells. Hadari, Y.R. et al. (2000) J. Cell Sci. 113:2385. The ED50 for this effect is 1-6 µg/mL. |
Source | E. coli-derived mouse Galectin-7 protein Ser2-Phe136 |
Accession # | |
N-terminal Sequence | Ser2 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Lgals7 |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 15 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS and Betamercaptoethanol with BSA as a carrier protein. |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 200 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
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).
Publication using 1304-GA | Applications | Species |
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Demers M, Magnaldo T, St-Pierre Y A novel function for galectin-7: promoting tumorigenesis by up-regulating MMP-9 gene expression. Cancer Res., 2005-06-15;65(12):5205-10. 2005-06-15 [PMID: 15958565] (Bioassay, Mouse) | Bioassay | Mouse |
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