Recombinant Human Galectin-3C Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in HEPES, NaCl, TCEP, PEG and Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in water.|
|Shipping||The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human Integrin alpha 5 beta 1 (Catalog # 3230-A5) is coated at 1 μg/mL (100 μL/well), Recombinant Human Galectin-3C (Catalog # 10110-GA) binds with an ED50 of 1‑6 μg/mL
2 μg/lane of Recombinant Human Galectin‑3C was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 14-18 kDa.
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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