Difference between revisions of "Part:BBa K1228006"
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<partinfo>BBa_K1228006 short</partinfo> | <partinfo>BBa_K1228006 short</partinfo> | ||
− | + | This generator contains BBa_K541503(https://parts.igem.org/Part:BBa_K541503) and BBa_K1228005(https://parts.igem.org/Part:BBa_K1228005). The generator can secrete 25 aminoacid peptide that is a part of Lactoferrin in ''B.subtilis''. It has a broad anti-bacterial range and strong anti-bacterial activity. | |
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<partinfo>BBa_K1228006 parameters</partinfo> | <partinfo>BBa_K1228006 parameters</partinfo> | ||
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+ | |||
+ | == Experiment and Results == | ||
+ | <p>1. Inoculate recombinant strains into 20ml LB.Cultivate at 37°C overnight.</p> | ||
+ | <p>2. Add 200ul indicator inoculum (''Micrococcus Lysodeikticus'' or ''Escherichia Coli'') untill heated LB solid medium (100ml) cool to about 50°C.</p> | ||
+ | <p>3. Use puncher make several hole on the LB plate.Add 80ul recombinant strains inoculum into the hole.Cultivate at 37°C overnight.</p> | ||
+ | 4. Observe whether LB plate will appear inhibition zone. | ||
+ | |||
+ | |||
+ | <html> | ||
+ | <head> | ||
+ | <meta http-equiv="Content-Type" content="text/html; charset=utf-8" /> | ||
+ | <style type="text/css"> | ||
+ | .zoomPan{width:800px;position:relative; } | ||
+ | .sh{zoom:1;background:url(https://static.igem.org/mediawiki/2013/8/80/Old_wall.jpg);filter:progid:DXImageTransform.Microsoft.dropShadow(color='#54000000', OffX=2,OffY=2);-webkit-box-shadow:4px 4px 4px #666;-moz-box-shadow:4px 4px 4px #666;} | ||
+ | #zoom{position:absolute;width:254px;height:254px;border:3px solid #fff;left:-9999px;top:0;overflow:hidden;background:#fff;} | ||
+ | #zoom img{position:relative;} | ||
+ | </style> | ||
+ | </head> | ||
+ | |||
+ | <script type="text/javascript"> | ||
+ | //<![CDATA[ | ||
+ | function zoomBox() {this.index.apply(this, arguments)} | ||
+ | zoomBox.prototype = { | ||
+ | index: function(win,zoom) { | ||
+ | var win=document.getElementById(win); | ||
+ | var box=document.getElementById(zoom); | ||
+ | var img=box.getElementsByTagName('IMG')[0]; | ||
+ | var zoom=img.width/win.getElementsByTagName('IMG')[0].width; | ||
+ | var z=Math.round(box.offsetWidth/2); | ||
+ | win.onmousemove=function (e){ | ||
+ | e = e || window.event; | ||
+ | var x=e.clientX,y=e.clientY, ori=win.getBoundingClientRect(); | ||
+ | if (x>ori.right+20||y>ori.bottom+20||x<ori.left-20||y<ori.top-20)box.style.display='none'; | ||
+ | x-=ori.left; | ||
+ | y-=ori.top; | ||
+ | box.style.left=x-z+'px'; | ||
+ | box.style.top=y-z+'px'; | ||
+ | img.style.left=-x*zoom+z+'px'; | ||
+ | img.style.top=-y*zoom+z+'px'; | ||
+ | } | ||
+ | win.onmouseover=function (){box.style.display=''} | ||
+ | } | ||
+ | }; | ||
+ | window.onload=function (){ | ||
+ | x=new zoomBox('zoomPan','zoom') | ||
+ | } | ||
+ | //]]> | ||
+ | </script> | ||
+ | |||
+ | |||
+ | |||
+ | <div id="paragraphs"> | ||
+ | <div class="zoomPan" id="zoomPan"> | ||
+ | <img src="https://static.igem.org/mediawiki/2013/6/64/ZswM21S.jpg" width="800px;"> | ||
+ | <div id="zoom" class="sh"><img src="https://static.igem.org/mediawiki/2013/1/16/ZswM21b.jpg" width="1500px;"></div> | ||
+ | </div> | ||
+ | </div> | ||
+ | </html> | ||
+ | |||
+ | https://static.igem.org/mediawiki/2013/4/46/ZswM21_M22s.jpg | ||
== Reference == | == Reference == | ||
− | BellamyW,TakaseM,Yamauchi K,et al. Identification of the bactericidal domainof lactoferrin[J]. | + | <p>1.BellamyW,TakaseM,Yamauchi K,et al. Identification of the bactericidal domainof lactoferrin[J]. BiochimicaetBiophysicaActa,1992,1121( 1/2):130-136.</p> |
− | EliassenLT,Berge G,SveinbjornssonB,et al. Evidenceforadirect antitumormechanismof actionof | + | <p>2.EliassenLT,Berge G,SveinbjornssonB,et al. Evidenceforadirect antitumormechanismof actionof Bovinel actoferricin[J].AnticancerResearch,2002,22(5):2703-2710.</p> |
− | Wakabayashi H,TakaseM,TomitaM. Lactoferricin derived from milk protein lactoferrin[J]. Current Pharmaceutical Design,2003,9(16):1277-1287. | + | <p>3.Wakabayashi H,TakaseM,TomitaM. Lactoferricin derived from milk protein lactoferrin[J]. Current Pharmaceutical Design,2003,9(16):1277-1287.</p> |
Latest revision as of 15:55, 27 September 2013
25aa with T1 terminator and Constitutive promoter veg
This generator contains BBa_K541503(https://parts.igem.org/Part:BBa_K541503) and BBa_K1228005(https://parts.igem.org/Part:BBa_K1228005). The generator can secrete 25 aminoacid peptide that is a part of Lactoferrin in B.subtilis. It has a broad anti-bacterial range and strong anti-bacterial activity.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Experiment and Results
1. Inoculate recombinant strains into 20ml LB.Cultivate at 37°C overnight.
2. Add 200ul indicator inoculum (Micrococcus Lysodeikticus or Escherichia Coli) untill heated LB solid medium (100ml) cool to about 50°C.
3. Use puncher make several hole on the LB plate.Add 80ul recombinant strains inoculum into the hole.Cultivate at 37°C overnight.
4. Observe whether LB plate will appear inhibition zone.
Reference
1.BellamyW,TakaseM,Yamauchi K,et al. Identification of the bactericidal domainof lactoferrin[J]. BiochimicaetBiophysicaActa,1992,1121( 1/2):130-136.
2.EliassenLT,Berge G,SveinbjornssonB,et al. Evidenceforadirect antitumormechanismof actionof Bovinel actoferricin[J].AnticancerResearch,2002,22(5):2703-2710.
3.Wakabayashi H,TakaseM,TomitaM. Lactoferricin derived from milk protein lactoferrin[J]. Current Pharmaceutical Design,2003,9(16):1277-1287.