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 |
|
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
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).
- Cummings, R.D. and Liu, F. (2009) Essentials of Glycobiology. 2nd edition. Chapter 33.
- Hokama, A. et al. (2008) World J. Gastroenterol. 14:5133.
- Barondes, S.H. et al. (1994) Cell 76:597.
- Hirabayashi, J. and K. Kasai (1993) Glycobiology 3:297.
- Rabinovich, A. et al. (2002) Trends in Immunol. 23:313.
- Rabinovich, A. et al. (2002) J. Leukocyte Biology 71:741.
- Hughes, R.C. (2001) Biochimie 83:667.
- Barrow, H. et al. (2011) Clinical Cancer Research 22:7035.
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