Difference between revisions of "Part:BBa K4241795"
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===Overview===
 
===Overview===
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+
This part is Cecropin B, an antimicrobial peptide derived from the Cecropia moth. This specific sequence is optimized for microalgal expression.
−
This part is Cecropin B, an antimicrobial peptide derived from the Cecropia moth. This specific sequence is optimized for microalgal expression
+
  
 
===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/>
+
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 sequence is isolated from Hyalophora cecropia <br/>
 
This is simply the coding region of Cecropin B, to be used in microalgal expression systems.
 
This is simply the coding region of Cecropin B, to be used in microalgal expression systems.
  

Revision as of 00:36, 12 October 2022


Cecropin B (Microalgal Expression)


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 64
  • 1000
    COMPATIBLE WITH RFC[1000]

Overview

This part is Cecropin B, an antimicrobial peptide derived from the Cecropia moth. This specific sequence is optimized for microalgal 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 sequence is isolated from Hyalophora cecropia
This is simply the coding region of Cecropin B, to be used in microalgal expression systems.