Background: Accumulation of the amyloid-peptide (A ) in the cerebral cortex is a critical event in the pathogenesis of Alzheimers disease. The amyloid protein precursor (APP) is cleaved by secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for secretase to generate the 4 kDa amyloid-peptide (A ), which is deposited in the brains of all suffering from Alzheimers disease.
Positive Control: Murine brain lysate.
Purification Method: Antigen Immunoaffiinity Purification.
Source: Rabbits were immunized with a synthetic peptide corresponding to amino acids 653 to 662 of human amyloid A4 protein precursor (APP) or 1 to 10 of the 4kDa Amyloid-peptide generated by secretases. This sequence is identical to those of rabbit, pig, bovine, guinea pig and chickens.
References: 1. Ponte, P., et al. A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors. Nature 1988, 331, 525-527.
2. Selkoe, D.J. Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 1994, 10, 373-403.
UniProt: P05067.
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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