Difference between revisions of "Team:Cooper Union/Parts"

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<h3>TdT delta1-27 (N-terminal Truncated Variant of TdT)</h3>
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<h3>BBa_K1746000 - TdT delta1-27 (N-terminal Truncated Variant of TdT)</h3>
 
<p>This DNA sequence is a truncation of full length bovine TdT that was originally designed by Repasky et. all in a Mutational Analysis of Terminal Deoxynucleotidyltransferase Mediated N-Nucleotide Addition in V(D)J Recombination. This deletion was of a putative nuclear localization sequence. This sequence was demonstrated to show 80% catalytic activity relative to full length, untruncated, TdT in 293T cells. Expression of this sequence results in a protein that can be used for 3'-end non-templated synthesis of oligonucleotides.</p>
 
<p>This DNA sequence is a truncation of full length bovine TdT that was originally designed by Repasky et. all in a Mutational Analysis of Terminal Deoxynucleotidyltransferase Mediated N-Nucleotide Addition in V(D)J Recombination. This deletion was of a putative nuclear localization sequence. This sequence was demonstrated to show 80% catalytic activity relative to full length, untruncated, TdT in 293T cells. Expression of this sequence results in a protein that can be used for 3'-end non-templated synthesis of oligonucleotides.</p>
  
  
<h3>TdT delta26-143 (Truncated TdT Variant)</h3>
+
<h3>BBa_K1746001 - TdT delta26-143 (Truncated TdT Variant)</h3>
 
<p>This DNA sequence is a mutated variant of a sequence coding for the bovine terminal deoxynucleotidyltransferase (TdT) enzyme. The sequence was originally desinged by Repasky et. al in a Mutational Analysis of Terminal Deoxynucleotidyltransferase Mediated N-Nucleotide Addition in V(D)J Recombination. It includes a deletion of the 26th to 143rd amino acids of the naturally occurring TdT protein. It shows catalytic activity similar to that of full length TdT in 293T cells. It is intended to be used for adding nucleotides to the 3 prime end of a DNA sequence.</p>
 
<p>This DNA sequence is a mutated variant of a sequence coding for the bovine terminal deoxynucleotidyltransferase (TdT) enzyme. The sequence was originally desinged by Repasky et. al in a Mutational Analysis of Terminal Deoxynucleotidyltransferase Mediated N-Nucleotide Addition in V(D)J Recombination. It includes a deletion of the 26th to 143rd amino acids of the naturally occurring TdT protein. It shows catalytic activity similar to that of full length TdT in 293T cells. It is intended to be used for adding nucleotides to the 3 prime end of a DNA sequence.</p>
  
<h3>TdT GIP 213-215 subAAA (Mutated TdT Variant)</h3>
+
<h3>BBa_K1746002 - TdT GIP 213-215 subAAA (Mutated TdT Variant)</h3>
 
<p>This DNA sequence is a mutation of full length bovine TdT that was originally designed by Repasky et. all in a Mutational Analysis of Terminal Deoxynucleotidyltransferase Mediated N-Nucleotide Addition in V(D)J Recombination. To create this sequence, amino acids 215-218 GIP, were substituted with AAA. This sequence was demonstrated to show 63% catalytic activity relative to full length, un-mutated, TdT. Expression of this sequence results in a protein that can be used for 3'-end non-templated synthesis of oligonucleotides.</p>
 
<p>This DNA sequence is a mutation of full length bovine TdT that was originally designed by Repasky et. all in a Mutational Analysis of Terminal Deoxynucleotidyltransferase Mediated N-Nucleotide Addition in V(D)J Recombination. To create this sequence, amino acids 215-218 GIP, were substituted with AAA. This sequence was demonstrated to show 63% catalytic activity relative to full length, un-mutated, TdT. Expression of this sequence results in a protein that can be used for 3'-end non-templated synthesis of oligonucleotides.</p>
  

Revision as of 05:16, 18 September 2015

Cooper Union 2015 iGEM




Part Documentation

Each team will make new parts during iGEM and will submit them to the Registry of Standard Biological Parts. The iGEM software provides an easy way to present the parts your team has created. The <groupparts> tag (see below) will generate a table with all of the parts that your team adds to your team sandbox.

Remember that the goal of proper part documentation is to describe and define a part, so that it can be used without needing to refer to the primary literature. Registry users in future years should be able to read your documentation and be able to use the part successfully. Also, you should provide proper references to acknowledge previous authors and to provide for users who wish to know more.

BBa_K1746000 - TdT delta1-27 (N-terminal Truncated Variant of TdT)

This DNA sequence is a truncation of full length bovine TdT that was originally designed by Repasky et. all in a Mutational Analysis of Terminal Deoxynucleotidyltransferase Mediated N-Nucleotide Addition in V(D)J Recombination. This deletion was of a putative nuclear localization sequence. This sequence was demonstrated to show 80% catalytic activity relative to full length, untruncated, TdT in 293T cells. Expression of this sequence results in a protein that can be used for 3'-end non-templated synthesis of oligonucleotides.

BBa_K1746001 - TdT delta26-143 (Truncated TdT Variant)

This DNA sequence is a mutated variant of a sequence coding for the bovine terminal deoxynucleotidyltransferase (TdT) enzyme. The sequence was originally desinged by Repasky et. al in a Mutational Analysis of Terminal Deoxynucleotidyltransferase Mediated N-Nucleotide Addition in V(D)J Recombination. It includes a deletion of the 26th to 143rd amino acids of the naturally occurring TdT protein. It shows catalytic activity similar to that of full length TdT in 293T cells. It is intended to be used for adding nucleotides to the 3 prime end of a DNA sequence.

BBa_K1746002 - TdT GIP 213-215 subAAA (Mutated TdT Variant)

This DNA sequence is a mutation of full length bovine TdT that was originally designed by Repasky et. all in a Mutational Analysis of Terminal Deoxynucleotidyltransferase Mediated N-Nucleotide Addition in V(D)J Recombination. To create this sequence, amino acids 215-218 GIP, were substituted with AAA. This sequence was demonstrated to show 63% catalytic activity relative to full length, un-mutated, TdT. Expression of this sequence results in a protein that can be used for 3'-end non-templated synthesis of oligonucleotides.