Alzheimer’s disease (AD) is characterized by the progressive formation in the brain of insoluble amyloid plaques and vascular deposits consisting of the 4-kD amyloid b-peptide (Ab).  Ab generation is initiated by proteolytic cleavage of the amyloid precursor protein (APP) at the N-terminal of Ab by b-secretase.  The Ab peptide is then released by proteolytic cleavage at its C-terminus by 8-secretase.  Because both these proteases are prime candidates for therapeutic intervention, an intense search has been underway to identify these two enzymes.

b-secretase is a transmembrane aspartic–protease (Asp2), referred to as BACE or memapsin 2, has been characterized and shown to have all the properties of b-secretase.  Four groups in all have now confirmed that BACE (or memapsin 2) is a convincing candidate for b-secretase. 

A goat antiserum to a synthetic peptide that corresponds to amino acids 485-501 of the C-terminus of the human BACE is currently available. This antiserum has been shown to be immunoreactive with the unconjugated immunizing peptide by ELISA.  It can be used to immunolabel neurons in formalin-fixed, paraffin-embedded sections of AD brain.  This antiserum is also suitable for western blots and will identify the 70 kD glycosylated form of the enzyme.  This antibody should be a valuable tool for scientists working to understand the role of b-secretase in AD and how to inhibit its acitivity.

This antiserum was produced using proprietary methodology whereby the peptide is attached to a carrier that elicits minimal immunoreactivity so that the antiserum has a higher degree of specificity for the peptide.  Since there is no overwhelming production of interfering antibodies to the carrier, this antiserum can routinely be used without further purification.  Pseud-Immune™ control immune serum (Cat no. GPA018E) from a mock immunized animal is available to be used in conjunction with this antibody as well as the immunizing peptide (Cat no. HSP019C), which can be used to neutralize immunoreactivity.

Manufacturing Reference:

Vassar, R., et al.  Science 286:735-741, 1999.