Equine, Latherin
Latherin is a 22 kD (208 amino acids) hydrophobic protein found in equines. It functions as a surfactant protein and has an amino acid sequence that shows similarities to PLUNC (palate, lung, and nasal epithelium) proteins 1. This protein has been shown to reduce the surface tension of water at concentrations below 1mg/ml 1 and increase the rate of evaporation. Latherin may assist in breaking up microbial biofilms and help limit the buildup of such biofilms on various surfaces 2 and may be useful to study alongside other biosurfactants such as Surfactant Proteins A, B, C, and D which can be found in the lungs and other areas of the human body. Latherin belongs to an intriguing group of natural surfactant proteins that are bio-compatible unlike current commercially available detergents 3. The latter are disruptive to cell membranes and also denature proteins resulting in their bio-incompatibility, where Latherin does not. Natural surfactant proteins such as Latherin have critical implications in nanotechnology and the amelioration of effects of oil spills after environmental disasters. Further investigation of Latherin in these contexts will result in new and pioneering inventions in biotechnology.
$300.00 – $1,500.00
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Product Details
- Physical State: White lyophilized powder
- Temperature Storage: -20°C
- Temperature Shipping: Ambient
- Sequence:
QQIPPEVSSQITDALTQGLLDGNFLSLLNAINLEGLLNTILDQVTGLLNILVGPLLGPSDAEIKLQDTRLLQLSLEFSPDSKGIDIWIPLELSVYLKLLILEPLTLYVRTDIRVQLRLESDEDGKYRLAFGHCSLLPRAIELQSGNPLSLPVNAVLGTIENALGNFITEDLGAGLCPTLNSLVSNLDLQLVNNLINLILDRANVDLSV
- Source: Recombinant. A DNA sequence encoding the equine latherin sequence, was expressed in E. coli
- Purity: >98% by SDS-PAGE
- Molecular Mass: 22,635 Da theoretical
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References
1. McDonald, R.E., et al., (2009) PLoS ONE 4(5) : e5726
2. Kennedy, M.W., (2011) Biochemical Society Transactions, 39 (4) : 1017-1022
3. Cooper, A., et al., (2017) Physicochem Eng Asp, 534 : 120-129