Team:Fatih Turkey/Devices

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Devices
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.alignright {
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float: right;
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.alignleft {
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float: left;
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font-size: 30px;
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h2 {
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font-size: 25px;
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h3 {
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font-size: 20px;
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h4 {
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font-size: 18px;
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}
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h5 {
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font-size: 16px;
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h6 {
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font-size: 15px;
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a{
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a{
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margin-top: 41px;
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margin-left: 40px;
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background: #707070;
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border-left: 1px #888 solid;
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border-right: 1px #888 solid;
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width: 988px;
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margin: 0px auto 0px;
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overflow: hidden;
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#footer div{
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color: #bbb;
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#footer a{
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color: #c4c5cc;
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text-decoration: none;
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#footer a:hover{
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color: #666;
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 +
.footer-sh-wrapper {
 +
    height: 22px;
 +
    margin: auto;
 +
    position: relative;
 +
    width: 990px;
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.footer-sh-left {
 +
    background: url("https://static.igem.org/mediawiki/2011/b/b7/Footer-sh-left.png") no-repeat scroll 0 0 transparent;
 +
    height: 112px;
 +
    left: 0;
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    position: absolute;
 +
    top: -90px;
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    width: 10px;
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.footer-sh {
 +
    background: url("https://static.igem.org/mediawiki/2011/b/bf/Footer-sh.png") repeat-x scroll center bottom #F9F9F9;
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    bottom: 0;
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    height: 22px;
 +
    left: 10px;
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    position: absolute;
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    width: 970px;
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.footer-sh-right {
 +
    background: url("https://static.igem.org/mediawiki/2011/b/b5/Footer-sh-right.png") no-repeat scroll 0 0 transparent;
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    height: 112px;
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    position: absolute;
 +
    right: 0;
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    top: -90px;
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    width: 10px;
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}
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 +
.copyright-open{
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width: 988px;
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height: 0px;
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margin:auto;
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display: block-inline;
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h1, h2, h3, h4, h5, h6{
 +
color: #333333;
 +
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#header-whole{
 +
 
 +
position: relative;
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z-index: 200;
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width: 980px;
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margin: 0 auto;
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#header{
 +
height: 100px;
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clear: both;
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background: #f9f9f9;
 +
margin: 0 auto;
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    width: 970px;
 +
}
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#header .logo{
 +
float: left;
 +
margin-top: 15px;
 +
margin-left: 20px;
 +
}
 +
 
 +
#container{
 +
width: 970px;
 +
margin: 0px auto 0px;
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background: none repeat scroll 0 0 #F9F9F9;
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}
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.copyright-open{
 +
border-top: 1px #a8a8a8 solid;
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border-bottom: 1px #888 solid;
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border-left: 1px #888 solid;
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border-right: 1px #888 solid;
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}
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.nav-wrapper{
 +
margin: 0px 90px 0px 0px;
 +
float:right;
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}
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.ddsmoothmenu ul{
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padding: 0px;
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list-style-type: none;
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background: #666666;
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 +
.ddsmoothmenu ul li{
 +
position: relative;
 +
display: block;
 +
float: left;
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.ddsmoothmenu ul li a{
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line-height: 140%;
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overflow: hidden;
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text-align: left;
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font-family: 'Lucida Grande', Arial, Verdana, sans-serif;
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word-spacing: 1px;
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font-size: 14px;
 +
font-weight: normal;
 +
display: block; /*background of menu items (default state)*/
 +
padding: 34px 20px 10px 17px;
 +
text-decoration: none;
 +
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 +
.ddsmoothmenu ul li a span {
 +
font-weight: normal;
 +
color: #888;
 +
font-size: 10px;
 +
clear: both;
 +
display:block;
 +
width: 60px;
 +
}
 +
* html .ddsmoothmenu ul li a{ /*IE6 hack to get sub menu links to behave correctly*/
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display: inline-block;
 +
}
 +
 
 +
.ddsmoothmenu ul li a:link, .ddsmoothmenu ul li a:visited{
 +
color: #333;
 +
}
 +
 
 +
.ddsmoothmenu ul li a.selected{ /*CSS class that's dynamically added to the currently active menu items' LI A element*/
 +
color: #888;
 +
}
 +
 
 +
.ddsmoothmenu ul li a:hover{
 +
color: #888;
 +
}
 +
 +
/*1st sub level menu*/
 +
.ddsmoothmenu ul li ul{
 +
position: absolute;
 +
left: 0;
 +
visibility: hidden;
 +
display: none; /*collapse all sub menus to begin with*/
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border: 1px #222 solid;
 +
-webkit-box-shadow: rgba(0, 0, 0, 0.2) 0px 0px 2px 1px;
 +
-moz-box-shadow: rgba(0, 0, 0, 0.2) 0px 0px 2px 1px;
 +
box-shadow: rgba(0, 0, 0, 0.2) 0px 0px 2px 1px;
 +
}
 +
 
 +
/*Sub level menu list items (undo style from Top level List Items)*/
 +
.ddsmoothmenu ul li ul li{
 +
text-align:left;
 +
float: none;
 +
background: url('img/bg-menu2.png');
 +
}
 +
 
 +
.ddsmoothmenu ul li ul li a{
 +
color: #fff;
 +
font-size: 12px;
 +
}
 +
.ddsmoothmenu ul li ul li  a.selected{ /*CSS class that's dynamically added to the currently active menu items' LI A element*/
 +
color: #fff;
 +
}
 +
.ddsmoothmenu ul li ul li a:link, .ddsmoothmenu ul li ul li a:visited{
 +
color: #fff;
 +
}
 +
.ddsmoothmenu ul li ul li a:hover{
 +
color: #ffc;
 +
}
 +
.ddsmoothmenu ul li ul li ul{
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top: 0;
 +
}
 +
 
 +
/* Sub level menu links style */
 +
.ddsmoothmenu ul li ul li a{
 +
width: 160px; /*width of sub menus*/
 +
padding: 0px 0px 0px 10px;
 +
height: 38px;
 +
line-height: 320%;
 +
border-left: 1px #555 solid;
 +
overflow: hidden;
 +
}
 +
 
 +
/* Holly Hack for IE \*/
 +
* html .ddsmoothmenu{height: 1%;} /*Holly Hack for IE7 and below*/
 +
 
 +
.copyright{
 +
width: 930px;
 +
color: #959595;
 +
background: #eee;
 +
clear: both;
 +
line-height: 190%;
 +
text-align: right;
 +
padding: 10px 20px 10px;
 +
margin: 0px auto 0px;
 +
}
 +
.copyright a{
 +
color: #bbb;
 +
text-decoration: none;
 +
}
 +
.copyright a:hover{
 +
color: #ccc;
 +
}
 +
.bar-title-whole{
 +
overflow: visible;
 +
position: relative;
 +
width: 990px;
 +
margin: auto;
 +
z-index: 10;
 +
}
 +
.bar-title{
 +
background: #999 url('https://static.igem.org/mediawiki/2011/e/e9/Bar-title-bg.jpg') top;
 +
border-left: 1px #8a8a8a solid;
 +
border-right: 1px #8a8a8a solid;
 +
 
 +
width: 918px;
 +
height: 122px;
 +
margin: auto;
 +
overflow: hidden;
 +
padding-left: 35px;
 +
padding-right: 35px;
 +
color: #ddd;
 +
line-height: 150%;
 +
font-size: 12px;
 +
 +
position: relative;
 +
z-index: 10;
 +
}
 +
 
 +
.bar-title h2{
 +
color: #fff;
 +
margin-top: 15px;
 +
margin-bottom: 30px !important;
 +
}
 +
.bar-title h5{
 +
color: #eee;
 +
}
 +
.bar-title-sh-left{
 +
width: 10px;
 +
height: 112px;
 +
background: url('https://static.igem.org/mediawiki/2011/6/69/Bar-title-sh-left.png') no-repeat;
 +
display: block-inline;
 +
position: absolute;
 +
top: 122px;
 +
left: 0px;
 +
}
 +
.bar-title-sh{
 +
width: 970px;
 +
height: 8px;
 +
background: url('https://static.igem.org/mediawiki/2011/3/37/Bar-title-sh.png') repeat-x;
 +
display: block-inline;
 +
position: absolute;
 +
top: 122px;
 +
left: 10px;
 +
}
 +
.bar-title-sh-right{
 +
width: 10px;
 +
height: 112px;
 +
background: url('https://static.igem.org/mediawiki/2011/c/c6/Bar-title-sh-right.png') no-repeat;
 +
display: block-inline;
 +
position: absolute;
 +
top: 122px;
 +
right: 0px;
 +
}
 +
#page{
 +
    width: 970px;
 +
    margin: 0px auto 0px;
 +
    overflow: hidden;
 +
    background: #f9f9f9;
 +
   
 +
}
 +
 
 +
#page .page-wrapper{
 +
margin: 15px 30px 0px 30px;
 +
width: 910px;
 +
overflow: hidden;
 +
float: left;
 +
}
 +
#page .page-wrapper-right{
 +
margin: 30px 40px 0px 25px;
 +
width: 935px;
 +
overflow: hidden;
 +
float: right;
 +
}
 +
#page .title-wrapper h1{
 +
margin-top: 0.5em;
 +
margin-bottom: 0.3em;
 +
}
 +
#page .meta-left-full{
 +
margin: 15px 0px 5px 0px;
 +
overflow: hidden;
 +
}
 +
#page .meta-left-button{
 +
margin: 5px 0px 60px 0px;
 +
overflow: hidden;
 +
}
 +
#page .w600{
 +
width: 600px;
 +
}
 +
 +
</style>
 +
 
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<script type="text/javascript" src="http://simsekburak.com/fatihigem/ddsmoothmenu.js"></script>
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 +
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jQuery(window).load(function() {
 +
setTimeout(function(){
 +
jQuery('#slider').nivoSlider({
 +
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controlNavThumbsFromRel:true,
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}, 1000),
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setTimeout(function(){
 +
/* For slider shortcode */
 +
jQuery('#slider2').nivoSlider({
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 +
animSpeed:600,
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captionOpacity: 0.8,
 +
pauseOnHover:true,
 +
directionNavHide:true });
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}, 1000);
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});
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</script>
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<div class="body-2">
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<img width="258" src="https://static.igem.org/mediawiki/2011/b/b6/Fatih_turkey_logo.png">
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<li>
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<a href="https://2011.igem.org/Team:Fatih_Turkey">Home</a>
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</li>
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<li>
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<a href="https://2011.igem.org/Team:Fatih_Turkey/Project">Project<span>Rainbow Graveyard</span></a>
 +
<ul>
 +
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Project">Overall Project</a></li>
 +
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/LALF">LALF</a></li>
 +
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Reflectin">Reflectin</a></li>
 +
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Biofilm">Biofilm</a></li>
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<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Experiments">Experiments</a></li>
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<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Results">Results</a></li>
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<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Future_Plan">Future Plan</a></li>
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</ul>
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<a href="https://2011.igem.org/Team:Fatih_Turkey/Biobricks">Biobricks</a>
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<ul>
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<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Parts">Parts</a></li>
 +
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Devices">Devices</a></li>
 +
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Modelling">Modelling</a></li>
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</ul>
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<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Safety">Safety</a></li>
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<a href="https://2011.igem.org/Team:Fatih_Turkey/Human_Practice">Human Practice</a>
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<ul>
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<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Sporocide">Sporocide</a></li>
 +
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/iGEM_for_7_to_77">iGEM for 7 to 77</a></li>
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<li><a href="https://2011.igem.org/Team:Fatih_Turkey/game">Game</a></li>
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<li><a href="https://2011.igem.org/Team:Fatih_Turkey/canvas_times">Canvas Times</a></li>
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<a href="https://2011.igem.org/Team:Fatih_Turkey/Lab_Garage">Lab Garage</a>
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<ul>
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<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Notebook">Notebook</a></li>
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<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Procedures">Procedures</a></li>
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</ul>
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<div class="bar-title-whole">
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  <div class="bar-title">
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      <h2 style="font-family: Verdana, Arial, SunSans-Regular, sans-serif;">Human Practice</h2>
 +
      <h5 style="font-family: Verdana, Arial, SunSans-Regular, sans-serif;">Sporocide</h5>
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    </div>
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  <div class="bar-title-sh-left"></div>
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<!-- post container -->
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<p><img src="https://static.igem.org/mediawiki/2011/4/4f/Reflectin.jpg"></p>
 +
<p><img src="https://static.igem.org/mediawiki/2011/7/7a/LALF_device.jpg"></p>
 +
<p>&nbsp;</p>
 +
<p><strong>K541515</strong></p>
 +
<p><strong>Limulus anti-LPS factor (LALF) for Bacillus subtilis</strong></p>
 +
<p><img src="https://static.igem.org/mediawiki/2011/5/5d/K41515.jpg"></p>
 +
<p>Constitutive promoter veg(BBa_K143012) coupled to the strong Ribosome Binding Site spoVG(BBa_K143021) from B. subtilis. These parts have been taken from 2008_Imperial_Collage. Pveg is a constitutive promoter that constitutively expresses the P43 protein in B. subtilis.</p>
 +
<p>SpoVG is an endogenous ribosome binding site from B. subtilis. The sequence of the spoVG ribosome binding site is AAAGGUGGUGA which is complementary to the sequence UUUCCUCCACU from the 3&#8242; region of the 16s rRNA from B. subtilis.</p>
 +
<p>SacB is a signal peptide used in the Sec-SRP (secretory signal recognition particle) pathway by B. subtilis. Signal peptides are responsible for directing preproteins (secretory proteins with a signal peptide region attached) through an appropriate secretory pathway. In the case of the Sec-SRP signal peptide, they direct preproteins from the cytoplasm into the growth medium.</p>
 +
<p>Lipopolysaccharide (LPS), or endotoxin, is the major mediator of septic shock, a serious complication of Gram-negative bacterial infections in humans. Molecules that bind LPS and neutralize its biological effects or enhance its clearance could have important clinical applications. Limulus anti-LPS factor (LALF) binds LPS tightly, and, in animal models, reduces mortality when administered before or after LPS challenge or bacterial infection. The wedge- shaped molecule has a striking charge distribution and amphipathicity that suggest how it can insert into membranes. The binding site for LPS probably involves an extended amphipathic loop, and it has been proposed that two mammalian LPS-binding proteins will have a similar loop. The amphipathic loop structure may be used in the design of molecules with therapeutic properties against septic shock.</p>
 +
<p>K541596</p>
 +
<p><strong>Reflectin gene with J04500 promoter</strong></p>
 +
<p><img src="https://static.igem.org/mediawiki/2011/a/a0/K541596.jpg"><br />
 +
Lipopolysaccharide (LPS), or endotoxin, is the major mediator of septic shock, a serious complication of Gram-negative bacterial infections in humans. Molecules that bind LPS and neutralize its biological effects or enhance its clearance could have important clinical applications. Limulus anti-LPS factor (LALF) binds LPS tightly, and, in animal models, reduces mortality when administered before or after LPS challenge or bacterial infection. The wedge- shaped molecule has a striking charge distribution and amphipathicity that suggest how it can insert into membranes. The binding site for LPS probably involves an extended amphipathic loop, and it has been proposed that two mammalian LPS-binding proteins will have a similar loop. The amphipathic loop structure may be used in the design of molecules with therapeutic properties against septic shock.</p>
 +
<p>&nbsp;</p>
 +
<p>&nbsp;</p>
 +
<p>K541545</p>
 +
<p><img src="https://static.igem.org/mediawiki/2011/b/b1/K541545.jpg"></p>
 +
<p><strong> </strong></p>
 +
<p><strong>Limulus Anti-Lipopolysaccharide Factor for E.coli (IPTG Inducible)</strong></p>
 +
<p>Lipopolysaccharide (LPS), or endotoxin, is the major mediator of septic shock, a serious complication of Gram-negative bacterial infections in humans. Molecules that bind LPS and neutralize its biological effects or enhance its clearance could have important clinical applications. Limulus anti-LPS factor (LALF) binds LPS tightly, and, in animal models, reduces mortality when administered before or after LPS challenge or bacterial infection. The wedge- shaped molecule has a striking charge distribution and amphipathicity that suggest how it can insert into membranes. The binding site for LPS probably involves an extended amphipathic loop, and it has been proposed that two mammalian LPS-binding proteins will have a similar loop. The amphipathic loop structure may be used in the design of molecules with therapeutic properties against septic shock.</p>
 +
<p>&nbsp;</p>
 +
<p>K541800</p>
 +
<p><img src="https://static.igem.org/mediawiki/2011/5/50/K541800.jpg"></p>
 +
<p><strong> </strong></p>
 +
<p><strong>B.subtilis and E.coli Episomal Shuttle Vector with Consitutive RFP to express in E.coli</strong></p>
 +
<p>This episomal vector has within its BioBrick region a constitutively expressed RFP gene in E.coli. It uses LacI promoter, B0034, mRFP1 (E0010) and B0015.</p>
 +
<p>K541915</p>
 +
<p><strong>Multi-host vector pTG262 converted to BioBrick vector wtih LALF protein and SacB signal peptide</strong></p>
 +
<p><img src="https://static.igem.org/mediawiki/2011/5/5d/K41515.jpg"></p>
 +
<p>&nbsp;</p>
 +
<p>Lipopolysaccharide (LPS), or endotoxin, is the major mediator of septic shock, a serious complication of Gram-negative bacterial infections in humans. Molecules that bind LPS and neutralize its biological effects or enhance its clearance could have important clinical applications. Limulus anti-LPS factor (LALF) binds LPS tightly, and, in animal models, reduces mortality when administered before or after LPS challenge or bacterial infection. The wedge- shaped molecule has a striking charge distribution and amphipathicity that suggest how it can insert into membranes. The binding site for LPS probably involves an extended amphipathic loop, and it has been proposed that two mammalian LPS-binding proteins will have a similar loop. The amphipathic loop structure may be used in the design of molecules with therapeutic properties against septic shock.</p>
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<p>&nbsp;</p>
 +
<p><strong><br />
 +
</strong></p>
 +
 
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Revision as of 02:45, 22 September 2011

deneme baslik

 

K541515

Limulus anti-LPS factor (LALF) for Bacillus subtilis

Constitutive promoter veg(BBa_K143012) coupled to the strong Ribosome Binding Site spoVG(BBa_K143021) from B. subtilis. These parts have been taken from 2008_Imperial_Collage. Pveg is a constitutive promoter that constitutively expresses the P43 protein in B. subtilis.

SpoVG is an endogenous ribosome binding site from B. subtilis. The sequence of the spoVG ribosome binding site is AAAGGUGGUGA which is complementary to the sequence UUUCCUCCACU from the 3′ region of the 16s rRNA from B. subtilis.

SacB is a signal peptide used in the Sec-SRP (secretory signal recognition particle) pathway by B. subtilis. Signal peptides are responsible for directing preproteins (secretory proteins with a signal peptide region attached) through an appropriate secretory pathway. In the case of the Sec-SRP signal peptide, they direct preproteins from the cytoplasm into the growth medium.

Lipopolysaccharide (LPS), or endotoxin, is the major mediator of septic shock, a serious complication of Gram-negative bacterial infections in humans. Molecules that bind LPS and neutralize its biological effects or enhance its clearance could have important clinical applications. Limulus anti-LPS factor (LALF) binds LPS tightly, and, in animal models, reduces mortality when administered before or after LPS challenge or bacterial infection. The wedge- shaped molecule has a striking charge distribution and amphipathicity that suggest how it can insert into membranes. The binding site for LPS probably involves an extended amphipathic loop, and it has been proposed that two mammalian LPS-binding proteins will have a similar loop. The amphipathic loop structure may be used in the design of molecules with therapeutic properties against septic shock.

K541596

Reflectin gene with J04500 promoter


Lipopolysaccharide (LPS), or endotoxin, is the major mediator of septic shock, a serious complication of Gram-negative bacterial infections in humans. Molecules that bind LPS and neutralize its biological effects or enhance its clearance could have important clinical applications. Limulus anti-LPS factor (LALF) binds LPS tightly, and, in animal models, reduces mortality when administered before or after LPS challenge or bacterial infection. The wedge- shaped molecule has a striking charge distribution and amphipathicity that suggest how it can insert into membranes. The binding site for LPS probably involves an extended amphipathic loop, and it has been proposed that two mammalian LPS-binding proteins will have a similar loop. The amphipathic loop structure may be used in the design of molecules with therapeutic properties against septic shock.

 

 

K541545

Limulus Anti-Lipopolysaccharide Factor for E.coli (IPTG Inducible)

Lipopolysaccharide (LPS), or endotoxin, is the major mediator of septic shock, a serious complication of Gram-negative bacterial infections in humans. Molecules that bind LPS and neutralize its biological effects or enhance its clearance could have important clinical applications. Limulus anti-LPS factor (LALF) binds LPS tightly, and, in animal models, reduces mortality when administered before or after LPS challenge or bacterial infection. The wedge- shaped molecule has a striking charge distribution and amphipathicity that suggest how it can insert into membranes. The binding site for LPS probably involves an extended amphipathic loop, and it has been proposed that two mammalian LPS-binding proteins will have a similar loop. The amphipathic loop structure may be used in the design of molecules with therapeutic properties against septic shock.

 

K541800

B.subtilis and E.coli Episomal Shuttle Vector with Consitutive RFP to express in E.coli

This episomal vector has within its BioBrick region a constitutively expressed RFP gene in E.coli. It uses LacI promoter, B0034, mRFP1 (E0010) and B0015.

K541915

Multi-host vector pTG262 converted to BioBrick vector wtih LALF protein and SacB signal peptide

 

Lipopolysaccharide (LPS), or endotoxin, is the major mediator of septic shock, a serious complication of Gram-negative bacterial infections in humans. Molecules that bind LPS and neutralize its biological effects or enhance its clearance could have important clinical applications. Limulus anti-LPS factor (LALF) binds LPS tightly, and, in animal models, reduces mortality when administered before or after LPS challenge or bacterial infection. The wedge- shaped molecule has a striking charge distribution and amphipathicity that suggest how it can insert into membranes. The binding site for LPS probably involves an extended amphipathic loop, and it has been proposed that two mammalian LPS-binding proteins will have a similar loop. The amphipathic loop structure may be used in the design of molecules with therapeutic properties against septic shock.