|APP Antibody 2452||20 µl||
||H M R Mk||100 to 140||Rabbit|
|β-Amyloid (1-42) (D3E10) Rabbit mAb 12843||20 µl||
|β-Amyloid (1-40) (D8Q7I) Rabbit mAb 12990||20 µl||
|β-Amyloid (1-37) (D2A6H) Rabbit mAb 12467||20 µl||
|β-Amyloid (1-39) (D5Y9L) Rabbit mAb 12077||20 µl||
|β-Amyloid (D54D2) XP® Rabbit mAb 8243||20 µl||
|β-Amyloid (pE3 Peptide) (D5N5H) Rabbit mAb 14975||20 µl||
|Anti-rabbit IgG, HRP-linked Antibody 7074||100 µl||
APP Antibody is a polyclonal antibody produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Thr668 of human APP695 protein. Antibodies are purified by protein A and peptide affinity chromatography. β-Amyloid fragment-specific monoclonal antibodies are produced by immunizing rabbits with synthetic peptides corresponding to residues at the carboxy terminus of each indicated human β-Amyloid fragment. β-Amyloid (D54D2) XP® Rabbit mAb is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human β-amyloid peptide (Aβ). β-Amyloid (pE3 Peptide) (D5N5H) Rabbit mAb is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human β-amyloid (pE3) peptide.
Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains an amyloid domain, which can be processed and released by two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). Several fragments corresponding to progressive APP processing at alternative cleavage sites have been identified (2). These include Aβ (1-37), Aβ (1-39), Aβ (1-40), and Aβ (1-42) (2). These fragments can also be N-terminally modified to generate pyroglutamate-3 Aβ (pE3-peptide) (3). Fragment-specific and pan-Aβ antibodies are used to detect and examine relative levels of individual Aβ fragments.
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