Difference between revisions of "Part:BBa K4241020"
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__NOTOC__ | __NOTOC__ | ||
<partinfo>BBa_K4241020 short</partinfo> | <partinfo>BBa_K4241020 short</partinfo> | ||
+ | <partinfo>BBa_K4241020 SequenceAndFeatures</partinfo> | ||
− | Cecropin B | + | ===Overview=== |
+ | This part is Cecropin B, an antimicrobial peptide derived from the Cecropia moth. This specific sequence is optimized for bacterial expression. | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
+ | Cecropins, a group of antimicrobial peptides fround primarily from insects, are a group of cationic antimicrobial peptides. Like most of the members of the group, Cecropin B has an amphipathic N-terminal segment and a largely hydrophobic C-terminal segment. These form a helix-hinge-helix structure, that is essential in maintaining antimicrobial effect. | ||
+ | <br/> | ||
+ | This is simply the coding region of Cecropin B, to be used in typical bacterial protein expression systems and chassis. | ||
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Latest revision as of 15:45, 9 October 2022
Cecropin B bacterial expression
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Overview
This part is Cecropin B, an antimicrobial peptide derived from the Cecropia moth. This specific sequence is optimized for bacterial expression.
Usage and Biology
Cecropins, a group of antimicrobial peptides fround primarily from insects, are a group of cationic antimicrobial peptides. Like most of the members of the group, Cecropin B has an amphipathic N-terminal segment and a largely hydrophobic C-terminal segment. These form a helix-hinge-helix structure, that is essential in maintaining antimicrobial effect.
This is simply the coding region of Cecropin B, to be used in typical bacterial protein expression systems and chassis.