Technical Data
Amyloid beta (A4) precursor protein (APP) is a 100–140kD transmembrane glycoprotein existing in several different isoforms. The amino acid sequence of APP contains the amyloid domain (A-beta), which can be released by a two-step proteolytic cleavage. The extracellular deposition and accumulation of the released A-beta fragments form the main
components of amyloid plaque in Alzheimer’s disease. APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion pathway of this protein. The phosphorylation at Thr668 (at a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell cycle (G2/Mphase) dependent. The APP Thr668 phosphorylated form exists in adult rat brain and correlates with cultured neuronal differentiation.

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

Recommended Dilutions:
Western Blot: 1:1000
Immunofluorescence (Paraffin): 1:250
Immunohistochemistry (Paraffin): 1:200
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 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. 
PabIgGAffinity Purified
100ul-20°CBlue IceHumanRabbit
Not Determined
Synthetic peptide corresponding to residues at the amino terminus of human beta-amyloid peptides (KLH).
Purified by Protein A and peptide affinity chromatography.
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.
Recognizes several isoforms of human beta-amyloid peptide (Abeta) such as beta-amyloid 40, beta-amyloid 42 (regardless of phosphoralytation state) and others at ~5kD.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Selkoe, D.J. (1996) J. Biol. Chem. 271, 18295–18298. 2. Caporaso, G.L. et al. (1992) Proc. Natl. Acad. Sci. USA 89, 3055–3059. 3. Hung, A.Y. and Selkoe, D.J. (1994) EMBO J. 13, 534–542. 4. Suzuki, T. et al. (1994) EMBO J. 13, 1114–1122. 5. Ando, K. et al. (1999) J. Neurosci. 19, 4421–4427. 6. Iijima, K.I. et al. (2000) J. Neurochem. 75, 1085–1091.