InVivoSIM anti-human amyloid-beta (Solanezumab Biosimilar)

About InVivoSIM anti-human amyloid-beta (Solanezumab Biosimilar)

This non-therapeutic biosimilar antibody uses the same variable regions as the therapeutic antibody, Solanezumab, making it ideal for research use. Solanezumab is a humanized IgG1κ anti-human APP antibody, and it reacts preferentially with soluble monomers rather than fibrillar beta-amyloid or abeta. Solanezumab does not bind Aβ’s aggregated forms. Aβ is a peptide that is suggested to play a critical role in the pathogenesis of Alzheimer’s disease (AD), and this peptide is generated through the aberrant protein processing of amyloid-β protein precursor (APP or AβPP). APP undergoes its initial cleavage by either α- or β-Secretase (or BACE1). α-Secretase mediated cleavage of APP leads to the formation of sAPPα and the α-C-terminal fragment (α-CTF or APP-C83). β-Secretase cleaves sAPPβ and the β-C-terminal fragment (β-CTF or APP-C99). γ-Secretase further cleaves C99 and C83 to P3 and Aβ respectively. Aβ’s amino acid length can range from 37 to 43, depending on the location of γ-secretase cleavage and the two main Aβ species are Aβ42 and Aβ40. Aβ42 is present in amyloid plaques more frequently than Aβ40, and Aβ drives the basic neuropathological abnormalities in AD that are characterized by the presence of neurofibrillary tangles, i.e., intraneuronal protein clusters, composed of paired helical filaments of the hyperphosphorylated tau protein, a microtubule-associated protein, and extracellular Aβ aggregates (senile plaques). Solanezumab recognizes a conformational epitope in the central region of human Aβ (amino acid residues 16-26), thereby reacting with various N-terminally truncated species of Aβ (e.g., Ab3-42) that are known to exist alongside full-length Aβ (Ab1-42) in AD senile plaques. Preclinical studies involving the in vivo administration of Solanezumab have shown that this antibody promotes Aβ clearance from the brain.