Purified anti-β-Amyloid Pyroglutamyl (Glu3) (clone 337.48)
A large fraction of Aβ peptide in Alzheimer's Disease patients' hippocampus and cortex is cleaved to remove the first two amino acids. Subsequently, glutamate at the third residue position can be modified into pyroglutamate (pE). Aβ (pE3) tends to aggregate more easily and shows increased stability. This is potentially due to the loss of charged residues and the formation of a lactam ring, which leads to increased hydrophobicity, enhanced β-sheet formation, and resistance to peptidases. Others have shown that Aβ (pE3) is more toxic to neurons and astrocytes when compared to full length Aβ peptide. Like other Aβ peptides, Aβ (pE3) can form soluble oligomers. These oligomers can slip between synapses, preventing neurotransmitters from making contact with their receptors, causing synaptic failure and cell death. Oligomers can then join together to make amyloid plaques, which block cell communication and trigger inflammation.