Anti-Glutathione Synthase (GSH) Antibodies
These mouse IgG1 monoclonal antibodies were generated against synthetic peptide and recognize plants and fission yeast (Schizosaccharomyces pombe) tripeptide glutathione synthetase (GSH).
Highlights:
- Recognize plants and fission yeast (Schizosaccharomyces pombe) GSH
- Antibodies developed using N-MAP tripeptide glutathione synthetase (GSH). N-MAP SEQ (30 aa res): IKLGIVMDPPIANINIKKDSSFAMLLEAQRR
- Useful for the study of synthesis of, and development of, phytochelatins and related metabolic pathways, as well as in the development of phytoremediation tools, and in the study of metal toxicity in plants and closely related organisms
- Suitable for ELISA, Immunofluorescence and Western Blot applications
Glutathione (GSH) is an important antioxidant in plants, animals, fungi, and some bacteria and archaea. GSH acts by preventing damage to important cellular components caused by reactive oxygen species such as free radicals, peroxides, lipid peroxides, and heavy metals. It consists of a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and the amine group of cysteine, and the carboxyl group of cysteine is attached by normal peptide linkage to a glycine.
From the laboratory of Richard B. Meagher, PhD, University of Georgia.
These mouse IgG1 monoclonal antibodies were generated against synthetic peptide and recognize plants and fission yeast (Schizosaccharomyces pombe) tripeptide glutathione synthetase (GSH).
Highlights:
- Recognize plants and fission yeast (Schizosaccharomyces pombe) GSH
- Antibodies developed using N-MAP tripeptide glutathione synthetase (GSH). N-MAP SEQ (30 aa res): IKLGIVMDPPIANINIKKDSSFAMLLEAQRR
- Useful for the study of synthesis of, and development of, phytochelatins and related metabolic pathways, as well as in the development of phytoremediation tools, and in the study of metal toxicity in plants and closely related organisms
- Suitable for ELISA, Immunofluorescence and Western Blot applications
Glutathione (GSH) is an important antioxidant in plants, animals, fungi, and some bacteria and archaea. GSH acts by preventing damage to important cellular components caused by reactive oxygen species such as free radicals, peroxides, lipid peroxides, and heavy metals. It consists of a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and the amine group of cysteine, and the carboxyl group of cysteine is attached by normal peptide linkage to a glycine.
From the laboratory of Richard B. Meagher, PhD, University of Georgia.
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Antibody |
| Antigen: | Tripeptide glutathione synthetase (GSH) |
| Accession ID: | P48637 |
| Molecular Weight: | 37 kDa |
| Isotype: | IgG1 |
| Clonality: | Monoclonal |
| Clone Name: | 12G7.D5.A11, 7E7.B4.F8 or 1D5.F4.B4 |
| Reactivity: | Plants and fission yeast (Schizosaccharomyces pombe). Possibly, other closely related organisms |
| Immunogen: | Synthetic peptide |
| Species Immunized: | Mouse with N-MAP derivative |
| Purification Method: | Protein G |
| Buffer: | PBS, 0.05% (w/v) Sodium Azide |
| Tested Applications: | WB, ELISA, IF |
| Storage: | -20C |
| Shipped: | Cold packs |
- Li Y, Kandasamy MK, Meagher RB. Rapid isolation of monoclonal antibodies. Monitoring enzymes in the phytochelatin synthesis pathway. Plant Physiol. 2001 Nov;127(3):711-9. PubMed PMID: 11706154; PubMed Central PMCID: PMC1540151.
- LeBlanc MS, Lima A, Montello P, Kim T, Meagher RB, Merkle S. Enhanced arsenic tolerance of transgenic eastern cottonwood plants expressing gamma-glutamylcysteine synthetase. Int J Phytoremediation. 2011 Aug;13(7):657-73. PubMed PMID: 21972493.
- Li Y, Dhankher OP, Carreira L, Balish RS, Meagher RB. Arsenic and mercury tolerance and cadmium sensitivity in Arabidopsis plants expressing bacterial gamma-glutamylcysteine synthetase. Environ Toxicol Chem. 2005 Jun;24(6):1376-86. PubMed PMID: 16117113.
- Dhankher OP, Li Y, Rosen BP, Shi J, Salt D, Senecoff JF, Sashti NA, Meagher RB. Engineering tolerance and hyperaccumulation of arsenic in plants by combining arsenate reductase and gamma-glutamylcysteine synthetase expression. Nat Biotechnol. 2002 Nov;20(11):1140-5.
If you publish research with this product, please let us know so we can cite your paper.
