epitope corresponding to phosphorylated Thr 668 of β-Amyloid of human origin
Modification
Phosphoralated
Modification Notes
Proteolytic cleavage of the Amyloid protein precursor (APP) gives rise to the ∫-Amyloid and Amyloid A4 proteins, which are present in human platelets. Amyloid deposition is associated with type II diabetes, Down syndrome and a variety of neurological disorders, including Alzheimer’s disease. The Amyloid precursor protein (APP) undergoes alternative splicing, resulting in several isoforms. Proteolytic cleavage of APP leads to the formation of the ∫-Amyloid/Amyloid A4 protein, which plays a role in the formation of neurofibrillary tangles and plaques that characterize the senile plaques of Alzheimer’s patients. In humans, ∫-Amyloid can be phosphorylated at a variety of locations, such as Thr 668. This phosphyryloation can modulate the function of ∫-Amyloid)APLP1 (Amyloid precursor-like protein 1) and APLP2 are structurally similar to APP. Human APLP2 is a membrane- bound sperm protein that contains a region highly homologous to the transmembrane-cytoplasmic domains of APP found in brain plaques of Alzheimer’s disease patients.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIP
recommended for detection of Thr 668 phosphorylated β-Amyloid of mouse, rat and human origin by WB and IP:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to phosphorylated Thr 668 of &beta -Amyloid of human origin
Tissue Specificity
epitope corresponding to phosphorylated Thr 668 of β-Amyloid of human origin