Methionine Deficient Green Florescent Protein (mGFP) vector

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…

Contributors

Inventor Institute
Dr. Bob Beitle University of Arkansas, Fayetteville
SKU: 156390
Product 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.
Cat. #: 156390
Research Fields: Other
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

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