Difference between revisions of "Part:BBa K3381003"

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<partinfo>BBa_K3381003 short</partinfo>
 
<partinfo>BBa_K3381003 short</partinfo>
  
FutA1-CBM2a is a fusion protein consisting of FutA1, an iron-binding domain, as well as CBM2a, a cellulose-binding domain. A linker sequence that was found to naturally occur in a CBM2a fusion was used as a linker domain between FutA1 and CBM2a (Courtade, 2018). Additionally, a sequence for a His-tag as well as a TEV recognition sequence was added to the N-terminus for ease of purification (by immobilized-metal affinity chromatography [IMAC]).
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FutA1-CBM2a is a fusion protein consisting of FutA1, an iron-binding domain, as well as CBM2a, a cellulose-binding domain. A linker sequence that was found to naturally occur in a CBM2a fusion was used as a linker domain between FutA1 and CBM2a (Courtade, 2018). The CBM2a and flexible linker sequence was submitted as part [https://parts.igem.org/Part:BBa_K3381007 BBa_K3381007]. Additionally, a sequence for a His-tag as well as a TEV recognition sequence was added to the N-terminus for ease of purification (by immobilized-metal affinity chromatography [IMAC]).
 
Fusion proteins containing cellulose-binding modules (CBMs) have readily been used in industrial purification processes, where the CBMs act as affinity tags. Strikingly enough, waste processing seems to be an application that has not been as fervently explored (Zhou, 2020). Furthermore, current waste processing methods fail to provide a way to recover metal ions once extracted, leaving the playing field open to technologies that make metal recovery possible.
 
Fusion proteins containing cellulose-binding modules (CBMs) have readily been used in industrial purification processes, where the CBMs act as affinity tags. Strikingly enough, waste processing seems to be an application that has not been as fervently explored (Zhou, 2020). Furthermore, current waste processing methods fail to provide a way to recover metal ions once extracted, leaving the playing field open to technologies that make metal recovery possible.
 
FutA1-CBM2a is a fusion protein that allows for extraction and recovery of iron(III) from aqueous waste. It binds irreversibly to cellulose, and can also bind Fe(III) (Koropatkin, 2007). This makes it appropriate for affinity chromatography or related uses.  
 
FutA1-CBM2a is a fusion protein that allows for extraction and recovery of iron(III) from aqueous waste. It binds irreversibly to cellulose, and can also bind Fe(III) (Koropatkin, 2007). This makes it appropriate for affinity chromatography or related uses.  

Revision as of 22:45, 22 October 2020

FutA1-CBM2a (fusion)

FutA1-CBM2a is a fusion protein consisting of FutA1, an iron-binding domain, as well as CBM2a, a cellulose-binding domain. A linker sequence that was found to naturally occur in a CBM2a fusion was used as a linker domain between FutA1 and CBM2a (Courtade, 2018). The CBM2a and flexible linker sequence was submitted as part BBa_K3381007. Additionally, a sequence for a His-tag as well as a TEV recognition sequence was added to the N-terminus for ease of purification (by immobilized-metal affinity chromatography [IMAC]). Fusion proteins containing cellulose-binding modules (CBMs) have readily been used in industrial purification processes, where the CBMs act as affinity tags. Strikingly enough, waste processing seems to be an application that has not been as fervently explored (Zhou, 2020). Furthermore, current waste processing methods fail to provide a way to recover metal ions once extracted, leaving the playing field open to technologies that make metal recovery possible. FutA1-CBM2a is a fusion protein that allows for extraction and recovery of iron(III) from aqueous waste. It binds irreversibly to cellulose, and can also bind Fe(III) (Koropatkin, 2007). This makes it appropriate for affinity chromatography or related uses.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 496
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 46
    Illegal BamHI site found at 1493
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]