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
2008
