CloneID: VH14 (NAC14)
Antigen Long Description: The original antibody was isolated from a naïve repertoire of human scFv antibodies using yeast surface display to select binders against NAC peptide of human alpha-synuclein.
Buffer Composition: PBS with 0.02% Proclin 300.
Chimeric Use Statement: This is a chimeric antibody, developed from the original camelid VHH antibody, specifically engineered for enhanced compatibility with existing reagents, assays, and techniques.
Available Custom Conjugation Options: AP, HRP, Fluorescein, APC, PE, Biotin Type A, Biotin Type B, Streptavidin, FluoroProbes 647H, Atto488, APC/Cy7, PE/Cy7
Uniprot Accession No.: P37840
Specificity Statement: This antibody binds the hydrophobic non-amyloid component (NAC) of α-synuclein between amino acids 53-87. More specifically, this antibody showed high binding to linear epitope comprising aa 61-78 of alpha-syn. 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 fusion of a proteasome-targeting PEST motif to this intrabody enhanced the solubility of the nanobody in cytoplasm and significantly enhanced degradation of the target protein, α-syn-GFP (PMID: 22929188). The in vivo therapeutic potential of gene therapy for delivery of proteasome-directed nanobodies selectively targeting α-syn was evaluated in a synuclein overexpression-based PD model. Post-mortem assessments of the substantia nigra (SN) of Sprague–Dawley rats after intracellular delivery of VH14-PEST showed that it markedly reduced the level of phosphorylated Serine-129 α-syn labeling relative to saline-treated animals (PMID: 30155513). A bifunctional antibody generated by fusing VH14 to a proteosome-targeting signal was able to counteract heterologous proteostatic effects of mutant α-Syn on mutant huntingtin Exon1 and protect against α-Syn toxicity using propidium iodide or Annexin V readouts (PMID: 27824888).
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