Anti Alpha Synuclein (Amino Acids 41-50) pAb (Rabbit, Antiserum)

Neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.

Alpha-Synuclein, a 140-amino acid protein abundantly expressed in presynaptic terminals, is a component of intraneuronal or glial inclusions observed in cases of Parkinson's disease (PD), Dementia with Lewy bodies (DLB) and Multiple system atrophy (MSA). Although alpha-synuclein is a natively unfolded protein, fibrillization or conformational change(s) of alpha-synuclein is central to the pathogenesis of alpha-synucleinopathies. The amino-terminal region of alpha-synuclein consists of seven imperfect repeats, each 11 amino acids in length, with the consensus sequence KTKEGV. The repeats partially overlap with a hydrophobic region (amino acids 61-95). The carboxy-terminal region (amino acids 96-140) is negatively charged. These antibodies are powerful tools for biochemical and IHC analyses of neurodegenerative diseases and for evaluation of conformational changes of alpha-synuclein.

References:
1) Masami Masuda et al., Inhibition of a-synuclein fibril assembly by small molecules: Analysis using epitope-specific antibodies. FEBS Letters (2009) 583, 787-791. PMID 19183551
2) Motokuni Yonetani et al., Conversion of wild-type alpha-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant. Journal of Biological Chemistry (2009) 284, 7940-7950. PMID 19164293