Difference between revisions of "Part:BBa K660201"
 
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<partinfo>BBa_K660201 short</partinfo>
 
<partinfo>BBa_K660201 short</partinfo>
  
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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.  
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<h3>Origin</h3>
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Horse sweat <i>(Equus caballus)</i><br/>
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<h3>Function</h3>
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Latherin is a surfactant protein with detergent like properties. <br/>
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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. <Br/>
  
 
<h4>Applications</h4>
 
<h4>Applications</h4>
 
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>
  
 
This is a version of the latherin biobrick (K660200) with an attached 6xHIS tag. Use this biobrick for affinity purification to isolate the protein.
 
This is a version of the latherin biobrick (K660200) with an attached 6xHIS tag. Use this biobrick for affinity purification to isolate the protein.
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<h3>Additional Information</h3>
 
<h3>Additional Information</h3>
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Note: Latherin is suspected to be the cause of allergic reaction in individuals with an allergy to horses.
 
Note: Latherin is suspected to be the cause of allergic reaction in individuals with an allergy to horses.
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<h3>References</h3>
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Beegley J, et al., 1986. Isolation and characterization of latherin, a surface-active protein from horse sweat<br/>http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=search&term=3753435>.
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<br/><br/>
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Kennedy M., 2011., Latherin and other biocompatible surfactant proteins<br/>
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http://www.biochemsoctrans.org/bst/039/bst0391017.htm<br/><br/>
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Information on "Affinity Purification" <br/>
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http://www.brunschwig-ch.com/pdf/downloads/ABT_RapidRun_Procedure.pdf?PHPSESSID=cb79f5862da62a654bb1a6aefe87c62b
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<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here
 
===Usage and Biology===
 
===Usage and Biology===

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.

Gla latherin.jpg

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


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 691
    Illegal PstI site found at 922
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 691
    Illegal PstI site found at 922
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 462
    Illegal BglII site found at 1005
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 691
    Illegal PstI site found at 922
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 691
    Illegal PstI site found at 922
  • 1000
    COMPATIBLE WITH RFC[1000]