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
*FOR RESEARCH USE ONLY (for other uses, please contact the licensing team)
- Tool name: Methionine Deficient Green Florescent Protein (mGFP) vector
- Research fields: Other
- 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
