>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
27 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.
SDS-PAGE
27-36 kDa, reducing conditions
Publications
Read Publication using 9039-GAB in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in HEPES, NaCl, TCEP, PEG and Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in water.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Galectin-3 (Hek293-expressed) Protein, CF
AGE-R3
Carbohydrate-binding protein 35
CBP 35,35 kDa lectin
CBP35
GAL3
Gal-3
galactin-3
Galactose-specific lectin 3
Galactoside-binding protein
GALBPCBP35
Galectin3
Galectin-3
GALIG
IgE-binding protein
L29
L31
L-31
Laminin-binding protein
Lectin L-29
lectin, galactoside-binding, soluble, 3
LGALS2
LGALS3
Mac-2 antigen
Mac-2
MAC2GAL3
Background
Galectin-3,
also known as Mac-2, L29, CBP35, and epsilon BP, is classified as a chimeric
member of the Galectin superfamily and contains one carbohydrate recognition
domain (CRD) linked to a non-lectin domain (1, 2). Mature mouse Galectin-3
shares 80% and 86% amino acid (aa) sequence identity with human and
rat Galectin-3, respectively. Galectin-3 is a 26-kDa protein that can be
nuclear, cytoplasmic, or secreted (3, 4). Nuclear Galectin-3 can modulate
gene expression, while cytosolic Galectin-3 can inhibit apoptosis and can
participate in exocytosis, Caveolin-mediated endocytosis, and
macrophage-mediated clearance of apoptotic cells (5-7). Extracellular
Galectin-3 has been shown to form high-order oligomers that promote the
crosslinking of cell surface oligosaccharides as well as integrin-dependent
cell adhesion and apoptosis (8-11). Galectin-3 contributes to the innate immune
response against Candida albicans and Streptococcus pneumoniae, and it can
facilitate acute inflammatory responses via neutrophil activation and
opsonization, macrophage recruitment, and mast cell activation (12-14).
Galectin-3 can also contribute to chronic inflammation and fibrosis (15). It is
implicated in neuroinflammatory disorders of the central nervous system,
cardiac fibrosis, and heart failure, as well as tumor growth, progression, and
metastasis (16-18).
Robertson, M.W. et al. (1990) Biochemistry 29:8093.
Elola, M.T. et al. (2007) Cell. Mol. Life Sci. 64:1679.
Haudek, K.C. et al. (2010) Biochim. Biophys. Acta 1800:181.
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