#156390

Methionine Deficient Green Florescent Protein (mGFP) vector

Cat. #156390

Methionine Deficient Green Florescent Protein (mGFP) vector

Cat. #: 156390

Availability: Please enquire for quantities and pricing

Target: mGFP

This fee is applicable only for non-profit organisations. If you are a for-profit organisation or a researcher working on commercially-sponsored academic research, you will need to contact our licensing team for a commercial use license.

Contributor

Inventor: Dr. Bob Beitle

Institute: University of Arkansas, Fayetteville

Tool Details
Target Details
References

Tool Details

*FOR RESEARCH USE ONLY

  • Tool name: Methionine Deficient Green Florescent Protein (mGFP) vector
  • Description: Methionine Deficient Green Florescent Protein (mGFP) is a mutated form of GFPuv (from Aequorea victoria) a GFP variant optimised for maximal fluorescence when excited by UV light. GFPuv can be used as a fusion partner to assist in the expression and isolation of peptides and to monitor biological processes. When GFPuv is fused to other proteins/peptides cyanogen bromide (CNBr) has been used to cleave the fused proteins at methionine residues. However, purification of the protein becomes more complex as the number of methionine residues in the reporter protein increases. GFPuv has four methionine residues which will lead to five fragments in the digestion mixture making purification more difficult. To reduce the downstream burden this mGFP mutant is resistant to CNBr cleavage making the purification process of proteins more efficient.
  • Additional notes: Methionine Deficient Green Florescent Protein (mGFP) is a mutated form of GFPuv (from Aequorea victoria) a GFP variant optimised for maximal fluorescence when excited by UV light. GFPuv can be used as a fusion partner to assist in the expression and isolation of peptides and to monitor biological processes. When GFPuv is fused to other proteins/peptides cyanogen bromide (CNBr) has been used to cleave the fused proteins at methionine residues. However, purification of the protein becomes more complex as the number of methionine residues in the reporter protein increases. GFPuv has four methionine residues which will lead to five fragments in the digestion mixture making purification more difficult. To reduce the downstream burden this mGFP mutant is resistant to CNBr cleavage making the purification process of proteins more efficient.

Target Details

  • Target: mGFP

References

  • Cloning, Fed-Batch Expression And Purification Of A Novel Anti-Candida Peptide And Development Of A Cleavage Resistant Variant Of Green Fluorescence Protein