Anticorps ACYP2 (G-5): sc-398251

The formation of stable highly organized protein aggegrates, known as amyloid fibrils, is associated with several debilitating human diseases, including Alzheimer's disease, Parkinson's disease, and Creutzfeldt-Jakob disease. In each of these conditions, a peptide or protein that is normally soluble accumulates into insoluble fibrils. Muscle acylphosphatase (AcP) has emerged as a significant model system to study protein misfolding and aggregation. It is particularly suitable for these studies because muscle AcP is a small, simple protein of only 98 amino acids consisting of a five-stranded antiparallel b-sheet and two parallel a-helices. Mutations in the muscle AcP between residues 16-31 and 87-98, which includes its phosphate binding site at Arg-23, significantly increases the rate of aggregation. These mutations correlate with changes in the hydrophobicity of AcP and a conversion of the a-helical structures to b-sheets. Therefore, a reduction in the net charge of a protein may be a key determinant in some forms of protein deposition diseases.

L'anticorps ACYP2 préféré est l'Anticorps ACYP2 (B-3): sc-398298.