human galectin-3, codon optimized for E. coli
Galectin-3 is a 26 kDa protein that binds certain LPS patterns. It especially bind the O-section of the LPS.
Galectins are proteins of the lectin family, which posess carbonhydrate recognition domains binding specifically to β-galactoside sugar residues. In humans, 10 different galectines have been identified, among which is galectin-3.
Galectin-3 has a size of about 31 kDA and is encoded by a single gene, LGALS3. It has many physiological functions, such as cell adhesion, cell growth and differentiation, and contributes to the development of cancer, inflammation, fibrosis and others.
Human galectin-3 is a protein of the lectin-family that was shown to bind the LPS of multiple human pathogens. Some of them, including Pseudomonas aeruginosa protect themselves against the human immune system by mimicking the lipopolysaccharides (LPS) present on human erythrocytes.
Usage and Biology
We also cloned our K1319003 into the pET17 expression vector and expressed all combinations of fusion proteins in E. coli BL21(DE3). An SDS-PAGE showed that all fusion proteins were fully translated:
Sequence and Features
- 10COMPATIBLE WITH RFC
- 12Illegal NheI site found at 112
- 21COMPATIBLE WITH RFC
- 23COMPATIBLE WITH RFC
- 25COMPATIBLE WITH RFC
- 1000COMPATIBLE WITH RFC
Galectins are proteins of the lectin family, which posess carbonhydrate recognition domains binding specifically to β-galactoside sugar residues. It is encoded by a single gene, LGALS3. It has many physiological functions, such as cell adhesion, cell growth and differentiation, and contributes to the development of cancer, inflammation, fibrosis and others. In the nucleus it acts as a pre-mRNA splicing factor. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes.
1. Henderson, N. C., & Sethi, T. (2009). The regulation of inflammation by galectin-3. Immunological reviews, 230(1), 160–171. https://doi.org/10.1111/j.1600-065X.2009.00794.x
2. Haudek, K. C., Spronk, K. J., Voss, P. G., Patterson, R. J., Wang, J. L., & Arnoys, E. J. (2010). Dynamics of galectin-3 in the nucleus and cytoplasm. Biochimica et biophysica acta, 1800(2), 181–189. https://doi.org/10.1016/j.bbagen.2009.07.005
3. Fukushi, J., Makagiansar, I. T., & Stallcup, W. B. (2004). NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin. Molecular biology of the cell, 15(8), 3580–3590. https://doi.org/10.1091/mbc.e04-03-0236