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Anti-GST Tag antibody
Catalog# BTL1008
Lot # Check on the product label
Size 100 μg
Isotype IgG1
Host Mouse
Reactivity
All
Specificity
Recognize GST and GST fusion proteins.
Product Form Liquid (1mg/ml)
Immunogen
Recombinant GST protein with full length.
Recommend Application
Western Blot (1:5000)
ELISA (1:2000)
Other applications have not been tested.
The optimal dilutions should be determined by end user.
Storage Instruction
Store at -20°C for 1 year. Or aliquot and store at -80°C for long term.
Avoid repeated freeze and thaw cycles.
Lot # Check on the product label
Size 100 μg
Isotype IgG1
Host Mouse
Reactivity
All
Specificity
Recognize GST and GST fusion proteins.
Product Form Liquid (1mg/ml)
Immunogen
Recombinant GST protein with full length.
Recommend Application
Western Blot (1:5000)
ELISA (1:2000)
Other applications have not been tested.
The optimal dilutions should be determined by end user.
Storage Instruction
Store at -20°C for 1 year. Or aliquot and store at -80°C for long term.
Avoid repeated freeze and thaw cycles.
Background
The glutathione S-transferase (GST, previously known as ligandins) family of enzymes are composed of many cytosolic, mitochondrial, and microsomal (now designated as MAPEG) proteins. GSTs are present in eukaryotes and in prokaryotes, where they catalyze a variety of reactions and accept endogenous and xenobiotic substrates. GST is commonly used to create fusion proteins. The tag has the size of 220 amino acids (roughly 26 KDa), which, compared to other tags like the myc- or the FLAG-tag, is quite big. A GST-tag is often used to separate and purify proteins that contain the GST-fusion. GST-fusion proteins can be produced in Escherichia coli, as recombinant proteins.
The glutathione S-transferase (GST, previously known as ligandins) family of enzymes are composed of many cytosolic, mitochondrial, and microsomal (now designated as MAPEG) proteins. GSTs are present in eukaryotes and in prokaryotes, where they catalyze a variety of reactions and accept endogenous and xenobiotic substrates. GST is commonly used to create fusion proteins. The tag has the size of 220 amino acids (roughly 26 KDa), which, compared to other tags like the myc- or the FLAG-tag, is quite big. A GST-tag is often used to separate and purify proteins that contain the GST-fusion. GST-fusion proteins can be produced in Escherichia coli, as recombinant proteins.
Reference
1. Udomsinprasert R, Pongjaroenkit S, Wongsantichon J, Oakley AJ, Prapanthadara LA, Wilce MC, Ketterman AJ (June 2005). "Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme". Biochem. J. 388 (Pt 3): 763–71.
2. Sheehan D, Meade G, Foley VM, Dowd CA (November 2001). "Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily". Biochem. J. 360 (Pt 1): 1–16.
3. Allocati N, Federici L, Masulli M, Di Ilio C (January 2009). "Glutathione transferases in bacteria". FEBS J. 276 (1): 58–75.
1. Udomsinprasert R, Pongjaroenkit S, Wongsantichon J, Oakley AJ, Prapanthadara LA, Wilce MC, Ketterman AJ (June 2005). "Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme". Biochem. J. 388 (Pt 3): 763–71.
2. Sheehan D, Meade G, Foley VM, Dowd CA (November 2001). "Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily". Biochem. J. 360 (Pt 1): 1–16.
3. Allocati N, Federici L, Masulli M, Di Ilio C (January 2009). "Glutathione transferases in bacteria". FEBS J. 276 (1): 58–75.
