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Recombinant Mouse Galectin-4 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse Galectin-4 Protein, CF Summary

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 1.25‑16.0 µg/mL.
Source
E. coli-derived mouse Galectin-4 protein
Met1-Ile326
Accession #
N-terminal Sequence
Ala2
Protein/Peptide Type
Recombinant Proteins
Gene
Lgals4
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
36.2 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
36 kDa, reducing conditions
Publications
Read Publications using
2128-GA in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, 2 to 8 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS, EDTA, DTT and Trehalose.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Galectin-4 Protein, CF

  • Antigen NY-CO-27
  • GAL4
  • gal-4
  • galectin 4
  • Galectin4
  • Galectin-4
  • L-36 lactose-binding protein
  • L36LBP
  • Lactose-binding lectin 4
  • lectin, galactoside-binding, soluble, 4
  • LGALS4

Background

Galectins are a family of carbohydrate-binding proteins with specificity for N-acetyl-lactosamine-containing glycoproteins. At least 14 mammalian galectins share structural similarities in their carbohydrate recognition domains (CRD), forming three groups often termed prototype (one CRD), tandem-repeat (two CRDs) and chimeric (one CRD, unique N-terminus) (1, 2). All lack classical signal peptides, but are present and active both within and outside of the cell. Galectins are involved in cell adhesion, migration, survival and apoptosis, and are often up- or down-regulated in cancer (1 - 3). Galectin-4 is a 36 kDa tandem-repeat galectin found throughout the gastrointestinal tract, but also present in well-differentiated breast and liver carcinomas (3, 4). Each CRD binds a different set of carbohydrate groups, including those found on erythrocyte blood group antigens (3, 5). CRD1 also binds cholesterol 3-sulfate and other sulfatides, which are concentrated within lipid raft membrane microdomains (6, 7). Endocytosed Galectin-4 is thought to play a role in forming the rafts, delivering them to the intestinal apical membrane, and stabilizing highly detergent-resistant "superrafts" (7 - 9). Human Galectin-4 shares 76%, 77%, 78% and 80% amino acid (aa) identity with mouse, rat, bovine and porcine Galectin-4, respectively, with the highest identity occurring within the CRDs. A potential splice variant begins at aa 132 and lacks most of the first CRD (10). Galectin-4 expression is concentrated within microvilli in the gastrointestinal epithelium, where it can interact with CD3 and bind activated T cells in the lamina propria during intestinal inflammation (11, 12). Either pro- or anti-inflammatory activity has been shown, depending on the mouse model used. Galectin-4 can also bind lung, spleen and kidney macrophages, although its expression is normally low in these tissues (5).

  1. Yang, R-Y. et al. (2008) Expert Rev. Mol. Med. 10:e17.
  2. Elola, M. T. et al. (2007) Cell. Mol. Life Sci. 64:1679.
  3. Huflejt, M. E. and H. Leffler (2004) Glycoconj. J. 20:247.
  4. Recreche, H. et al. (1997) Eur. J. Biochem. 248:225.
  5. Markova, V. et al. (2006) Int. J. Mol. Med. 18:65.
  6. Ideo, H. et al. (2007) J. Biol. Chem. 282:21081.
  7. Delacour, D. et al. (2005) J. Cell Biol. 169:491.
  8. Braccia, A. et al. (2003) J. Biol. Chem. 278:15679.
  9. Stechly, L. et al. (2009) Traffic 10:438.
  10. Entrez accession # EAW56820.
  11. Hokama, A. et al. (2004) Immunity 20:681.
  12. Paclik, D. et al. (2008) PLoS ONE 3:e2629.

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    Bioinformatics

    Gene Symbol Lgals4
    Uniprot