Difference between revisions of "Part:BBa K660201"
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Latherin is able to temporarily bind to hydrophobic surfaces and has therefore been investigated as a possible method of breaking up biofilms. It is also suspected that the protein may have antimicrobial functions. <br/> | Latherin is able to temporarily bind to hydrophobic surfaces and has therefore been investigated as a possible method of breaking up biofilms. It is also suspected that the protein may have antimicrobial functions. <br/> | ||
The 2011 University of Glasgow iGEM team used this part in their system, DISColi, to aid in the dispersal of biofilms. | The 2011 University of Glasgow iGEM team used this part in their system, DISColi, to aid in the dispersal of biofilms. | ||
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+ | This biobrick was tested under the control of a pBAD promoter, the assay used to determine whether latherin expressed surfactant properties involved sonication to lyse the cells, all samples were then shaken vigorously for 30 seconds. The results below show that the sample expressing latherin not only became more frothy than the other samples for a prolonger period of time, it also increased the transparency of the media. | ||
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+ | [[Image:Gla_latherin.jpg|500px]] | ||
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+ | https://parts.igem.org/wiki/index.php?title=Part:BBa_K660201 | ||
<br/><h4>Part:BBa_K660200</h4> | <br/><h4>Part:BBa_K660200</h4> |
Latest revision as of 00:43, 30 September 2011
Latherin (Surfactant Protein) + 6xHIS Tag
Origin
Horse sweat (Equus caballus)
Function
Latherin is a surfactant protein with detergent like properties.
Its normal biological function is temperature regulation and is believed to function by enhancing evaporation from the pelt. It does so by binding to hydrophobic surfaces and allowing them to become wettable.
Applications
Latherin is able to temporarily bind to hydrophobic surfaces and has therefore been investigated as a possible method of breaking up biofilms. It is also suspected that the protein may have antimicrobial functions.
The 2011 University of Glasgow iGEM team used this part in their system, DISColi, to aid in the dispersal of biofilms.
This biobrick was tested under the control of a pBAD promoter, the assay used to determine whether latherin expressed surfactant properties involved sonication to lyse the cells, all samples were then shaken vigorously for 30 seconds. The results below show that the sample expressing latherin not only became more frothy than the other samples for a prolonger period of time, it also increased the transparency of the media.
https://parts.igem.org/wiki/index.php?title=Part:BBa_K660201
Part:BBa_K660200
This is a version of the latherin biobrick (K660200) with an attached 6xHIS tag. Use this biobrick for affinity purification to isolate the protein.
Additional Information
Note: Latherin is suspected to be the cause of allergic reaction in individuals with an allergy to horses.
References
Beegley J, et al., 1986. Isolation and characterization of latherin, a surface-active protein from horse sweat
http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=search&term=3753435>.
Kennedy M., 2011., Latherin and other biocompatible surfactant proteins
http://www.biochemsoctrans.org/bst/039/bst0391017.htm
Information on "Affinity Purification"
http://www.brunschwig-ch.com/pdf/downloads/ABT_RapidRun_Procedure.pdf?PHPSESSID=cb79f5862da62a654bb1a6aefe87c62b
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 691
Illegal PstI site found at 922 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 691
Illegal PstI site found at 922 - 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 462
Illegal BglII site found at 1005 - 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 691
Illegal PstI site found at 922 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 691
Illegal PstI site found at 922 - 1000COMPATIBLE WITH RFC[1000]