Recombinant Human Galectin-3C Protein, CF Summary
| Details of Functionality |
Measured by its binding ability in a functional ELISA. When
Recombinant Human Integrin alpha 5 beta 1
Recombinant
Human Integrin alpha 5 beta 1 (Catalog # 3230-A5)
is immobilized at 1 µg/mL (100 µL/well), the concentration of Recombinant Human Galectin-3C that produces 50% of the
optimal binding response is 1-6 μg/mL. |
| Source |
Human embryonic kidney cell, HEK293-derived human Galectin-3C protein Gly108-Ile250 |
| Accession # |
|
| N-terminal Sequence |
Gly108 |
| Structure / Form |
|
| 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 |
16 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 |
14-18 kDa, reducing conditions
|
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.
- 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 500 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-3C Protein, CF
Background
Human 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 nonlectin domain
(1, 2). The truncated form, Galectin-3C, which consists of the carboxy-terminal
amino acid residues of Galectin-3 and lacks the N-terminal domain, has been
shown to inhibit tumor growth and metastasis (3, 4). Within this region,
human Galectin-3C shares 87% and 83% amino acid (aa) sequence identity with
mouse and rat Galectin-3C, respectively. Galectin-3C
has been found to interact with Integrin beta 1 in Hela cell lateral mobility
assays (5). It can also be found endogenously attached to cell surface of
neutrophils (6). Galectin-3C has been shown to enhance the activity of cancer
therapy drugs as well as inhibiting tubule formation during angiogenesis (3).
- Robertson, M.W. et al. (1990) Biochemistry 29:8093.
- Elola, M.T. et al. (2007) Cell. Mol. Life Sci. 64:1679.
- Mirandola, L. et al. (2011) PloS One 6:e21811.
- John, C.M. et al. (2003) Clin. Cancer Res. 9:2374.
- Yang, E.H. et al. (2017) PLoS ONE 12:e0184378.
- Sundqvist, M. et al. (2018) J. Leukoc. Biol. 103:341.
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