|Cat. No. 127 002||200 µl antiserum, lyophilized. For reconstitution add 200 µl H2O, then aliquot and store at -20°C until use.|
WB: 1 : 500 up to 1 : 1000 (AP staining)
IP: not tested yet
ICC: 1 : 500 gallery
IHC: 1 : 500 up to 1 : 1000 gallery
IHC-P/FFPE: 1 : 500 up to 1 : 1000 gallery
|Immunogen||Synthetic peptide corresponding to AA 756 to 770 from rat APP (UniProt Id: P08592)|
Reacts with: rat (P08592), mouse (P12023), chicken, frog, human (P05067).
Other species not tested yet.
|Specificity||Specific for APP.|
|Matching control protein/peptide||127-0P|
Alzheimer's disease is characterized by the accumulation of β-amyloid peptides in plaques and vessel walls and by the intraneuronal accumulation of paired helical filaments composed of hyperphosphorylated tau.
Amyloid precursor protein APP is part of a super-family of transmembrane and secreted proteins. It appears to have a number of roles, including regulation of haemostasis and mediation of neuroprotection. APP also has metal and heparin-binding properties. Cleavage of amyloid precursor protein by β- and γ-secretases results in the generation of the Aβ (βA4)peptide, whereas α-secretase cleaves within the Aβ sequence and prevents formation from APP.
Recent findings indicate that the site of γ-secretase cleavage is critical to the development of amyloid deposits. Aβ1-42 is much more amyloidogenic than Aβ1-40. Aβ1-42 formation is favoured by mutations in the two presenilin genes (PS1 and PS2), and by the commonest amyloid precursor protein mutations.