Alpha-synuclein (46-58) Heavy EGVVHGVTTVAE-[U-13C6,15N2-Lys]-acid

Description

Alpha-synuclein (46-58) Heavy is derived from the alpha-synuclein intrinsically disordered protein which is found in the neurons and presynaptic terminals. The accumulation of alpha-synuclein has been associated with the pathogenesis of neurodegenerative diseases such as Parkinson’s disease, dementia with Lewy bodies and multiple system atrophy. The lysine residue at position 12 has been isotopically labelled with carbon-13 (6) and nitrogen-15 (2).

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Catalogue number crb1300958
Sequence (one letter code) EGVVHGVTTVAE-[U-13C6,15N2-Lys]-acid
Sequence (three letter code) Glu-Gly-Val-Val-His-Gly-Val-Thr-Thr-Val-Ala-Glu-[U-13C6,15N2-Lys]-OH
Disease Area Neurodegenerative diseases, parkinson’s disease, dementia with lewy bodies and multiple system atrophy
Purity >95%
Storage -20°C
Molecular Weight 1332.7
References

Huang et al. (2019) α-Synuclein: A Multifunctional Player in Exocytosis, Endocytosis, and Vesicle Recycling. Front. Neurosci DOI: https://doi.org/10.3389/fnins.2019.00028

Li et al (2019) Early Stages of aggregation of engineered α-synuclein monomers and oligomers in solution. Sci. Rep. 9 1734 DOI: https://www.nature.com/articles/s41598-018-37584-6

Wong and Kranic (2017) α-Synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies. Nat. Med. 23 1 DOI: https://www.nature.com/articles/nm.4269

Alpha-synuclein (46-58) Heavy is derived from the alpha-synuclein intrinsically disordered protein which is found in the neurons and presynaptic terminals. Encoded by the SNCA1/PARK1 gene alpha-synclein is structurally composed of 140 amino acids, making up the three domains: N-terminal membrane binding domain, a hydrophobic non-amyloid-beta component domain and a hydrophilic C-terminal domain. Usually alpha-synuclein plays a role in protecting neurons from apoptotic stimuli and is involved in synaptic vesical trafficking.


However it has been found that the accumulation of alpha-synuclein aggregates can lead to neurodegenerative diseases such as Parkinson’s disease, dementia with Lewy bodies and multiple system atrophy. It is further involved in the fibrilisation of amyloid-b and tau which play a major role in Alzheimer’s disease. Amyloid fibrils are formed from alpha synuclein monomers within the cytosol and when bound to membranes these monomers can undergo conformational changes to form protofibrils and then ring like oligomers. This can result in the formation of transmembrane pores which disrupts the membrane, calcium homeostasis and signalling.


In familial Parkinson’s disease the SNCA1 gene, can be subjected to point mutations such as A30P, E46K and A53T, or over expression. These can result in the increased aggregation of alpha-synuclein.


The lysine residue at position 12 has been isotopically labelled with carbon-13 (6) and nitrogen-15 (2), giving this peptide a mass increase of 8 compared to the unlabelled peptide.

Alpha-synuclein (46-58) Heavy

Cat No. Pack Size Price Qty

crb1300958c

25nmol

$330.00