Recombinant Proteins

A Parkinson's disease-related point mutant (A30P) of alpha-synuclein. A30P mutant of alpha-synuclein was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by taking advantage of the thermosolubility of the protein and by using conventional column chromatography techniques.

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Expression Host E.Coli

A deletion mutant of alpha-synuclein (amino acids 1-60), which contains the N-terminal amphipathic domain.?Syn1-60 was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques.

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Expression Host E.Coli

A deletion mutant of alpha-synuclein (amino acids 61-140). Syn61-140 was overexpressed in E. coli and was purified to apparent homogeneity by taking advantage of the thermosolubility of protein and by using conventional column chromatography techniques. Additional amino acid(Met) is attached at the N-terminus.

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Expression Host E.Coli

Alpha-Synuclein E46K was overexpressed in E. coli and purified to apparent homogenity by using conventional column chromatography techniques.

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Expression Host E.Coli

An alternatively spliced (103-129) form of alpha-synuclein, alpha-Synuclein 112 was cloned into an E. coli expression vector by RT-PCR. The recombinant protein was purified to apparent homogeneity by taking advantage of the thermosolubility of the protein and by using conventional column chromatography techniques.

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Expression Host E.Coli

A deletion mutant of alpha-Synuclein (amino acids 61-140). Syn61-140 was overexpressed in E. coli and was purified to apparent homogeneity by taking advantage of the thermosolubility of protein and by using conventional column chromatography techniques. Additional amino acid(Met) is attached at the N-terminus.

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Expression Host E.Coli

A deletion mutant of alpha-synuclein that lacks the NAC region (amino acid 61-95). Alpha-synuclein (deltaNAC) was overexpressed in E. coli and purified to apparent homogeneity by taking advantage of the thermosolubility of the protein and by using conventional column chromatography techniques. 6 amino acids were added as a linker.

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Expression Host E.Coli

A Parkinson's disease-related double mutant (A30P/A53T) of a-synuclein. The recombinant protein was purified to apparent homogeneity by taking advantage of the thermosolubility of the protein and by using conventional column chromatography techniques.

Tag Tag Free
Expression Host E.Coli

A deletion mutant of alpha-synuclein (amino acids 1-60), which contains the N-terminal amphipathic domain.?Syn1-60 was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques.

Tag Tag Free
Expression Host E.Coli