Note: Not all species have been tested for usefulness with this product. Only those species listed have been tested. We cannot make any guarantees about additional reactivities which may or may not occur.
Cell Membrane (single-pass type I membrane protein), Golgi Apparatus and Secreted
Species Reactivity:
Human A40. Mouse, rat, pig, cow, sheep, dog, rabbit, frog and polar bear (100% homologous) have not been tested, but are expected to react. No significant cross-reactivity to A?42 has been observed.
Applications:
Uses:
The antibody has been used to detect Ab 40 in dot blots, RIA, ELISA and other related assays. *The optimal antibody concentration should be determined for each specific application.
Dilutions:
ELISA , Western Blot 0.05-1.0 mg/ml , Radioimmunoassay , Dot Blot
Unit Size:
0.025 mg
Concentration:
2.35 mg/ml
Packaging:
Storage:
Aliquot and store at -20 °C or -80 °C. Avoid freeze-thaw cycles.
Buffer:
PBS [pH7.2]
Preservative:
0.1% Sodium Azide
Limitations:
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Products are guaranteed for 6 months from date of receipt, except for peptides and proteins which are guaranteed for 3 months.
Alzheimer's Disease is characterized by the presence of extracellular plaques and intracellular neurofibrillary tangles (NFTs) in the brain. The major component of these plaques is Ab peptide, a 40 to 43 amino acid peptide cleaved from amyloid precursor protein (APP). Increased release of the "longer forms" of Ab peptide, Ab42 or Ab43, which have a greater tendency to aggregate than Ab40, occurs in individuals expressing certain genetic mutations, expressing certain ApoE alleles, or may involve other, still undiscovered, factors. Many researchers theorize that this increased release of Ab42/Ab43 leads to the abnormal deposition of Ab and the associated neurotoxicity in the brains of affected individuals.
Ulery, P.G., et al. (2000) Modulation of b-amyloid precursor protein processing by the low density lipoprotein receptor-related protein (LRP): Evidence that LRP contributes to the pathogenesis of Alzheimer's Disease. J. Biol. Chem. 275:7410-7415.
Vassar, R., et al. (1999) b-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286:735-741.