The amyloid precursor protein (APP) is a large membrane protein whose N-terminus projects into the extracellular space. In Alzheimer's disease (AD), this protein is broken down and releases the Ab peptide that is found in senile plaques and vessels.  A frameshift mutant of APP has been found that results from a GA dinucleotide deletion which results in a frameshift mutation that gives rise to a truncated APP with a unique C-terminus.  The role of the amyloid precursor protein frameshift mutant (APPFM) in AD is currently unknown. These abnormal proteins may accumulate and lead to cellular disturbances and neuronal degeneration.

A goat antiserum to a synthetic peptide that corresponds to amino acids 339-348 of the C-terminus of human APPFM is currently available. This antiserum has been shown to be immunoreactive with the unconjugated immunizing peptide by ELISA. The antiserum will immunolabel dystrophic neurites in senile plaques and with neurons containing the APPFM in formalin­-fixed, paraffin-embedded sections from AD brain.  It also immunolabels a 45 kD band on western blots that corresponds to the expected molecular weight of the APPFM protein based on the amino acid sequence.  This antibody should be a valuable tool for scientists working to understand the role of APPFM in AD.

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. HSP011C), which can be used to neutralize immunoreactivity.

Manufacturing Reference:

Van Leewen, FW, et al.  Science 279:242-247, 1998.