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Anti-Phytochelatin Synthase Monoclonal Antibodies (3 lines)

Detailed Technology Description: These mouse IgG2a monoclonal antibodies were generatedagainst synthetic peptide and recognize plants, fission yeast (Schizosaccharomyces pombe) and itsclosely-related organisms’ phytochelatin synthetase (PS), N-MAP. All lines havebeen validated for use in WB, ELISA, and IF. Together with gamma-glutamyl Cys sythetase (γ-ECS) andglutathione synthetase, phytochelatin synthetase (PS) is an enzyme involved in,and required for, synthetizing phytochelatins (PC). In certain plants,deficiency of such enzymes leads to low tolerance to metal contamination whilemutants over-expressing them are highly tolerant to metal contamination and maybe used in phyto-remediation of heavy metals. Monoclonal antibodies to PC weredeveloped using N-terminal peptides synthesized as MAPs. N-terminal MAP was 29amino acids long. They are useful for the study of synthesis and development ofphytochelatins and related metabolic pathways, as well as in the development ofphytoremediation tools and in the study of metal toxicity in plants and closelyrelated organisms.

*Abstract

ReagentsDescription

Clone Name	Antigen	MW (kDa)	Isotype	Immunogen	Reactivity/Recognition
mAbPS1 (1.2E12.G5.C9)	Phytochelatin synthetase (PS), N-MAP	57	IgG2a	Synthetic peptide	Recognizes plants and fission yeast (Schizosaccharomyces pombe) PS
mAbPS2 (2.8H4.A7.C1)	Phytochelatin synthetase (PS), N-MAP	57	IgG2a	Synthetic peptide	Recognizes plants and fission yeast (Schizosaccharomyces pombe) PS
mAbPS3 (1.9D2.A8.E8)	Phytochelatin synthetase (PS), N-MAP	57	IgG2a	Synthetic peptide	Recognizes plants and fission yeast (Schizosaccharomyces pombe) PS

N-MAP SEQ:NIVKRAVPELLRGMTMATPNIGLIKNKVV

Species Immunized: Mouse

PurificationMethod: Protein G column

Buffer: 0.1M SodiumPhosphate, pH 7.4, 0.15M

NaCl, 0.05% (w/v) Sodium Azide

Tested Applications: WB,ELISA, IF

Antibodystorage temperature: -80^oC

References

Li Y, KandasamyMK, Meagher RB. Rapid isolation of monoclonal antibodies. Monitoring enzymes inthe phytochelatin synthesis pathway. Plant Physiol.2001 Nov;127(3):711-9. PubMed PMID: 11706154; PubMed Central PMCID: PMC1540151.

LeBlanc MS, LimaA, Montello P, Kim T, Meagher RB, Merkle S. Enhanced arsenic tolerance oftransgenic eastern cottonwood plants expressing gamma-glutamylcysteinesynthetase. Int JPhytoremediation. 2011 Aug;13(7):657-73. PubMed PMID: 21972493.

Li Y, DhankherOP, Carreira L, Balish RS, Meagher RB. Arsenic and mercury tolerance and cadmiumsensitivity in Arabidopsis plants expressing bacterial gamma-glutamylcysteinesynthetase. Environ ToxicolChem. 2005 Jun;24(6):1376-86. PubMed PMID: 16117113.

Dhankher OP, LiY, Rosen BP, Shi J, Salt D, Senecoff JF, Sashti NA, Meagher RB. Engineeringtolerance and hyperaccumulation of arsenic in plants by combining arsenatereductase and gamma-glutamylcysteine synthetase expression. NatBiotechnol. 2002 Nov;20(11):1140-5

Country/Region: USA

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