beta plaques

CRANAD-28 is a blood-brain barrier (BBB) penetrating two-photon imaging probe capable of visualizing amyloid plaques and labeling plaques and cerebral amyloid angiopathy.

BIBD-124, with an IC50 value of 9.51 nM, effectively binds to amyloid beta (Aβ) plaques. The fluorinated variant, [18F]BIBD-124, serves as a radiotracer for imaging Aβ plaques [1].

Remternetug (LY3372993) is a humanised monoclonal antibody targeting N3pG-Aβ, recognising pyroglutamated Aβ within amyloid plaques, applicable for Alzheimer's disease.

Anti-Amyloid Beta Antibody (DLX212) represents a highly specialized humanized monoclonal antibody specifically engineered to target various forms of Amyloid Beta (Aβ) with exceptional binding affinity. It effectively facilitates the measurable clearance of amyloid plaques across various preclinical experimental models to evaluate the reduction of neurotoxicity and the restoration of synaptic plasticity during strictly monitored laboratory observation periods and functional cognitive assays.

Anti-Amyloid Beta Antibody (CNTO 2125) is a recombinant humanized monoclonal antibody targeting human Amyloid Beta (Aβ/Amyloid Beta). Aβ is the core component of amyloid plaques in the Alzheimer's disease (AD) brain, generated from the cleavage of amyloid precursor protein (APP). CNTO 2125 specifically binds to Aβ with high affinity (e.g., EC50 ≈ 9.7 ng/mL), blocking the aggregation of Aβ monomers and promoting the clearance of existing plaques. By targeting the Aβ cascade, this antibody has the potential to protect neurons from Aβ-mediated neurotoxic damage, serving as a critical tool for researching the pathogenesis and immunotherapy of Alzheimer's disease. This antibody features a huIgG1 heavy chain and a hu-kappa light chain.

Anti-BACE1 Antibody is a humanized monoclonal antibody targeting beta-site amyloid precursor protein cleaving enzyme 1 (BACE1). BACE1 is a transmembrane aspartic protease and the rate-limiting enzyme for the generation of Aβ peptides in Alzheimer's disease (AD). This antibody functions by specifically binding to the extracellular domain of BACE1, neutralizing its enzymatic activity or inducing receptor internalization to block the beta-site cleavage of amyloid precursor protein (APP). This process effectively reduces the production of toxic Aβ40/42 and inhibits the formation and deposition of amyloid plaques, making it a pivotal tool for researching the pathogenesis and immunotherapeutic strategies of neurodegenerative diseases.

β-Amyloid (11-22) is a peptide fragment of β-Amyloid. β-Amyloid peptide (Abeta), the primary component of amyloid plaques in the brains of Alzheimer's patients, is believed to be the cause of Alzheimer's Disease (AD), the most common neurodegenerative disease, affecting approximately 10% of the population over 60.

Amyloid precursor c-terminal peptide has the amino acid sequence Gly-Tyr-Glu-Asn-Pro-Thr-Tyr-Lys-Phe-Phe-Glu-Gln-Met-Gln-Asn. APP is best known as the precursor molecule whose proteolysis generates beta-amyloid (Aβ), a 37 to 49 amino acid peptide whose am