CloneID: 10H (syn-10H)
Heavy Chain modification: Fc Silent™
Antigen Long Description: The original antibody was isolated from a human Tomlinson I and J scFv antibody libraries by panning the library against diluted sample of alpha-synuclein (20 uM) containing predominantly larger aggregate forms.
Buffer Composition: PBS only.
Chimeric Use Statement: This is a reformatted human IgG1 Fc Silent™ antibody, based on the original human scFv format, created for improved compatibility with existing reagents, assays and techniques.
Uniprot Accession No.: P37840
Specificity Statement: This antibody recognizes the later-stage oligomeric morphological form of human alpha-synuclein. Alpha-synuclein is a small 140 amino acid presynaptic neuronal protein, a major component of Lewy bodies and a member of the synuclein family. Misfolding, abnormal accumulation, and secretion of α-Synuclein (α-Syn) are closely associated with synucleinopathies, including Parkinson’s disease (PD). α-syn is abundant in the brain, and smaller amounts are found in the heart, muscles, and other tissues. In the brain, α-syn is found mainly at the tips of neurons in the specialized structures known as presynaptic terminals and has been shown to comprise up to ∼1% of total proteins in the neuronal cytosol. Recent evidence suggests that α-synuclein (α-syn) can contribute to the pathogenesis of amyotrophic lateral sclerosis (ALS).
Application Notes (Clone): The binding of this antibody to oligomeric forms of alpha-synuclein was confirmed using ELISA. This antibody is not capable of recognizing monomeric and fibrillar forms of alpha-synuclein. This antibody could recognize the late stage alpha-synuclein aggregates occurring during (10–22 day) time points. It was capable of binding aggregates with molecular masses of 42 and ~80 kDa corresponding to trimeric and hexameric forms in a western blot. The scFv version of this antibody inhibits aggregation of alpha-synuclein in vitro, blocks extracellular alpha-synuclein-induced toxicity in both undifferentiated and differentiated human neuroblastoma cell lines (SH-SY5Y), and specifically recognizes naturally occurring aggregates in Parkinson's disease but not in healthy human brain tissue (PMID: 19141614). A fusion protein comprising D5 scFv, cell pentrating peptide like penetratin were found to be effective in Lewy body disease. It specifically targeted α-syn oligomers and reduced the accumulation of α-syn and ameliorated functional deficits when delivered late in disease development (PMID: 27606342).
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