Technical Data
-Amyloid Peptide
The progressive deposition of insoluble amyloid protein plaques in speci c areas of the brain and its blood vessels is associated with a number of neuropathologies and is an early invariant feature of Alzheimer’s disease. The major component of these protein plaques is a peptide of 39–42 amino acids derived from a group of 695–770 amino acid precursor proteins collectively referred to as the b-amyloid precursor protein (Beta-APP). b-APP is highly conserved in vertebrates; however, its normal function has not been well de ned. In each of the b-APPs, the b-Amyloid peptide (b-AP) is an internal peptide that begins about 99 residues from the carboxy-terminal end of the b-APP and extends from the extracellular domain into the middle of the hydrophobic, membrane spanning domain of the precursor protein. The precise mechanism whereby b-AP accumulates in brain remains poorly de ned.

Suitable for use in ELISA, Immunohistochemistry and Western Blot. Other applications not tested.

Recommended Dilution:
Immunohistochemistry (alcohol-fixed, parrafin embedded, frozen): ~10ug/ml It is nessessary to pretreat the tissue with trypsin digestion.
Western Blot: 0.1-0.2ug/ml
ELISA: 0.5-1.0ug/ml
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. 
100ug-20°CBlue IceHumanMouse
28aa synthetic peptide derived from the b-amyloid peptide (aa1-28).
Puri ed
Supplied as a liquid in PBS, pH 7.4, 0.05% sodium azide.
Recognizes the 4-5kD b-amyloid peptide (b-AP). High concentrations of antibody will also react with A-a, B-a and g subunits of brinogen. Species Crossreactivity: human
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Stern RA et al; Am J Pathol 134:973–978 (1989). 2. Stern RA et al; FEBS Lett 266:43–47 (1990). 3. Hill WDet al; Brain Res 585:386–390 (1992). 4. Solomon, B. et al; PNAS 93:452–455 (1996).