Sensitivity:

0.92 pM (range 11.72 - 1500 pM)

Assay Time:

~2 hours

Applications:

ELISA, Colorimetric detection

Application Notes:

For the quantitative determination of human APP ΔC31 in   cell lysate, cerebral spinal fluid, plasma and serum samples. Sequence   alignments indicate multiple species are probable.

Species reactivity:

Human

Shipping:

Blue Ice Not Frozen

Long Term Storage:

+4°C

Kit/Set Contains:

Microtiter Plate, Assay Buffer, Standard, Detector   Antibody, Antibody-HRP-conjugate, TMB Substrate, Stop Solution, Wash Buffer   Concentrate

Scientific Background:

Alzheimer’s disease (AD) is a progressive   neurodegenerative disease characterized by the senile plaques,   neurofibrillary tangles and loss of synapses and neurons. AD has been largely   viewed as a disease of toxicity being mediated by the accumulation of the   amyloid beta (Aβ) peptide as plaques within the brain resulting in damage to   brain cells from the binding of damaging metals, reactive oxygen species   production and direct damage to cellular membranes. Recent research has   suggested that the Aβ peptide is a multifunctional peptide with   non-pathological effects and that its association with AD is in conjunction   with its roles in combination with other proteins such as the amyloid   precursor protein (APP) resulting in the imbalance between the processes of memory   formation and normal forgetting. It is through the interactions of the Aβ   peptide with APP that the Aβ peptide itself can affect normal modulation and   signaling of APP resulting in its indicated role in the pathogenesis of AD   via signaling effects rather than chemical or physical effects.
     There are three major APP isoforms (APP695, APP751 and APP770)   that are formed through alternative splicing of precursor mRNA. APP770   represents the canonical sequence. The APP695 isoform is preferentially   expressed in the central nervous system, while APP770 and APP751 are more   highly expressed in peripheral tissues. It has been demonstrated that the   full length APP695 can be cleaved via caspase at an intracellular site   (Asp664) resulting in the release of a 31 amino acid C-terminal peptide (C31)   from the remaining larger neo-APP fragment (APP ΔC31) with both of these   entities being pro-apoptotic. Immunohistochemical analysis of human brain   tissue demonstrated that this cytoplasmic cleavage occurs 4-fold greater in patients   with AD versus normal patients and that these cleavage products are localized   to plaques and tangles in key areas of the brain affected by the disease. A   single genetic mutation of aspartic acid residue 664 to alanine of APP695 led   to the complete blockage of the C-terminal cleavage in vivo reversing many   characteristics of the AD phenotype in a transgenic mouse model.   Additionally, in cell culture it has been suggested that the neurotoxicity of   Aβ is dependent on the cleavage of APP at Asp664 and the resulting   Aβ-facilitated APP multimerization.