|Cat. No. 127 002||
200 µl antiserum, lyophilized. For reconstitution add 200 µl H2O, then aliquot and store at -20°C until use.
Antibodies should be stored at +4°C when still lyophilized. Do not freeze!
Immunoprecipitation (IP); Immunoisolation or pulldown of a target molecule using an antibody. For details and product specific hints, please refer to the ”Remarks” section.', $event)" style="cursor: help;">IP: not tested yet
Immunocytochemistry (ICC) on 4% PFA fixed cells. Immunoreactivity is usually revealed by fluorescence. Some antibodies require special fixation methods. For details, please refer to the “Remarks” section.', $event)" style="cursor: help;">ICC: 1 : 500 gallery
Immunohistochemistry (IHC) on 4% PFA perfusion fixed tissue with 24h PFA post fixation. Immunoreactivity is usually revealed by fluorescence or a chromogenic substrate. Some antibodies require special fixation methods or antigen retrieval steps. For details, please refer to the ”Remarks” section.', $event)" style="cursor: help;">IHC: 1 : 500 up to 1 : 1000 gallery
Immunohistochemistry (IHC-P) of formalin fixed, paraffin embedded (FFPE) tissue (some antibodies require special antigen retrieval steps, please refer to the ”Remarks” section). Immunoreactivity is usually revealed by fluorescence or a chromogenic substrate.', $event)" style="cursor: help;">IHC-P: 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.