Press Release Body: Alpha Synuclein, 1-60 MW: 6,149 Da Lyophilized powder. Purity > 95% by SDS-PAGE; A deletion mutant of Alpha-Synuclein (amino acids 1-60), which contains the N-terminal amphipathic domain. Alpha-Synuclein is a 14 kD (140 amino acids) acidic presynaptic protein. It is a major component of Parkinson’s disease aggregates and is implicated in the pathogenesis of Parkinson’s Disease and related neurodegenerative disorders. Alpha-Synuclein accumulates in the brains of sporadic Parkinson’s disease patients as a major component of Lewy bodies, which are intraneuronal cytoplasmic inclusions characteristic of Parkinson’s disease. Alpha-Synuclein appears to associate with other proteins that aggregate and is found in amyloid plaques and neuritic tangles in Alzheimer’s disease. References: Conway, K.A. et. al., (2000) Biochemistry, 39: 2552 Jakes, R. et al. 1994, FEBS Letters, 345, 27 Masliah, E. et. al., 2001. Proc. Natl. Acad. Sci., USA, 98, 12245 Ueda, K., et. al. 1993. Proc. Natl. Acad. Sci., USA, 90, 11282 For more info: http://www.rpeptide.com/products/product_details_112.html Alpha Synuclein, 1-95 MW: 9,391 Da Description: Lyophilized powder. Purity > 95% by SDS-PAGE; A deletion mutant of Alpha-Synuclein (amino acids 1-95), which contains the N-terminal amphipathic domain and the NAC region. Alpha-Synuclein is a 14 kD (140 amino acids) acidic presynaptic protein. It is a major component of Parkinson’s disease aggregates and is implicated in the pathogenesis of Parkinson’s Disease and related neurodegenerative disorders. Alpha-Synuclein accumulates in the brains of sporadic Parkinson’s disease patients as a major component of Lewy bodies, which are intraneuronal cytoplasmic inclusions characteristic of Parkinson’s disease. Alpha-Synuclein appears to associate with other proteins that aggregate and is found in amyloid plaques and neuritic tangles in Alzheimer’s disease. References: Conway, K.A. et. al., (2000) Biochemistry, 39: 2552 Jakes, R. et al. 1994, FEBS Letters, 345, 27 Masliah, E. et. al., 2001. Proc. Natl. Acad. Sci., USA, 98, 12245 Ueda, K., et. al. 1993. Proc. Natl. Acad. Sci., USA, 90, 11282 For more info: http://rpeptide.com/products/product_details_113.html Alpha-Synuclein, 61-140
MW: 8,460 Da Description: Lyophilized powder. Purity > 95% by SDS-PAGE; A deletion mutant of Alpha-synuclein (amino acids 61-140). Additional amino acid (Met) is attached at the N-terminus. Alpha-Synuclein is a 14 kD (140 amino acids) acidic presynaptic protein. It is a major component of Parkinson’s disease aggregates and is implicated in the pathogenesis of Parkinson’s Disease and related neurodegenerative disorders. Alpha-Synuclein accumulates in the brains of sporadic Parkinson’s disease patients as a major component of Lewy bodies, which are intraneuronal cytoplasmic inclusions characteristic of Parkinson’s disease. Alpha-Synuclein appears to associate with other proteins that aggregate and is found in amyloid plaques and neuritic tangles in Alzheimer’s disease. References: Park, S. M. et al. (2002) Blood, 100(7) 2506 Park, S. M. et al. (2002) Biochemisty. 41, 4137 Conway, K.A. et. al., (2000) Biochemistry, 39: 2552 Jakes, R. et al. 1994, FEBS Letters, 345, 27 Masliah, E. et. al., 2001. Proc. Natl. Acad. Sci., USA, 98, 12245 Ueda, K., et. al. 1993. Proc. Natl. Acad. Sci., USA, 90, 11282 For more info: http://rpeptide.com/products/product_details_114.html Alpha-Synuclein, 96-140
MW: 5,217 Da Description: Lyophilized powder. Purity > 95% by SDS-PAGE; A deletion mutant of Alpha-Synuclein (amino acids 96-140). Additional amino acid (Met) is attached at the N-terminus. Alpha-Synuclein is a 14 kD (140 amino acids) acidic presynaptic protein. It is a major component of Parkinson’s disease aggregates and is implicated in the pathogenesis of Parkinson’s Disease and related neurodegenerative disorders. Alpha-Synuclein accumulates in the brains of sporadic Parkinson’s disease patients as a major component of Lewy bodies, which are intraneuronal cytoplasmic inclusions characteristic of Parkinson’s disease. Alpha-Synuclein appears to associate with other proteins that aggregate and is found in amyloid plaques and neuritic tangles in Alzheimer’s disease. References: Park, S. M. et al. (2002) Blood, 100(7) 2506 Park, S. M. et al. (2002) Biochemisty. 41, 4137 Conway, K.A. et. al., (2000) Biochemistry, 39: 2552 Jakes, R. et al. 1994, FEBS Letters, 345, 27 Masliah, E. et. al., 2001. Proc. Natl. Acad. Sci., USA, 98, 12245 Ueda, K., et. al. 1993. Proc. Natl. Acad. Sci., USA, 90, 11282 For more info: http://rpeptide.com/products/product_details_115.html
Web Site: http://www.rpeptide.com
Contact Details: Sanjay Bhardwaj 4241 Mars Hill Road, Bogart, GA 30622, USA Tel: 678-753-0747 Fax: 678-753-0746 sanjayb@rpeptide.com www.rpeptide.com
2010
