Recombinant Human Galectin-2 (HEK-293-expressed) Protein, CF

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Recombinant Human Galectin-2 (Catalog # 9874‑GA)agglutinates human red blood cells. The ED50 for this effect is 5‑25 μg/mL.
2 μg/lane of Recombinant Human Galectin‑2 was resolved with SDS-PAGEunder reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 12-15 kDa.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Galectin-2 (HEK-293-expressed) 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 5-25 μg/mL. Measured by the ability of the immobilized protein to enhance the adhesion of HUVEC human umbilical vein endothelial cells. The ED50 for this effect is 1-6 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human Galectin-2 protein
Met1-Glu132
Accession #
N-terminal Sequence
Thr2
Protein/Peptide Type
Recombinant Proteins
Purity
>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
  • Bioactivity2
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.
SDS-PAGE
12-15 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °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 400 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 Human Galectin-2 (HEK-293-expressed) Protein, CF

  • Beta-galactoside-binding lectin L-14-II
  • GAL2
  • Gal-2
  • galectin 2
  • Galectin2
  • Galectin-2
  • HL14gal-2
  • Lactose-binding lectin 2
  • lectin, galactoside-binding, soluble, 2
  • LGALS2
  • MGC75071
  • S-Lac lectin 2

Background

Galectins constitute a large family of carbohydrate-binding proteins with specificity for N‑acetyl-lactosamine-containing glycoproteins. To date, 15 mammalian galectins, which share structural similarities in their carbohydrate-recognition domains (CRD), have been identified. Twelve galectin genes are found in humans, including two for galectin-9. The galectins have been classified into the prototype galectins (-1, -2, -5, -7, -10, -11, -13, -14, -15), which contain one CRD and exist either as a monomer or a noncovalent homodimer; the chimera galectin (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. (1). Galectin-2 is an approximately 14-kDa homodimeric protein, and like other prototype galectins, consists of a single CRD (2-4). Human Galectin-2 shares 66% and 67% amino acid sequence identity with mouse and rat Galectin-2, respectively. 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 (5-7). Galectin-2 is expressed in hepatoma, stomach epithelial cells and in colorectal and neural tumors. The specific functions of Galectin-2 have not been reported but increased serum levels of Galectin-2 have been associated with metastatic cancer and this may also be involved in cancer cell adhesion to vascular endothelium (8).
  1. Cummings, R.D. and Liu, F. (2009) Essentials of Glycobiology. 2nd edition. Chapter 33.
  2. Hokama, A. et al. (2008) World J. Gastroenterol. 14:5133.
  3. Barondes, S.H. et al. (1994) Cell 76:597.
  4. Hirabayashi, J. and K. Kasai (1993) Glycobiology 3:297.
  5. Rabinovich, A. et al. (2002) Trends in Immunol. 23:313.
  6. Rabinovich, A. et al. (2002) J. Leukocyte Biology 71:741.
  7. Hughes, R.C. (2001) Biochimie 83:667.
  8. Barrow, H. et al. (2011) Clinical Cancer Research 22:7035.

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