Product Name: APP Antibody
Species Reactivity: Human, Mouse, Rat
Tested Applications: ELISA, IHC-P, WB
Applications: APP antibody can be used for detection of APP and Ab peptide by Western blot at 1 μg/mL. Antibody can also be used for immunohistochemistry starting at 2.5 μg/mL.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: Predicted: 83 kDa Observed: 115 kDa
Immunogen: APP antibody was raised against a peptide corresponding to 10 amino acids of human amyloid A4 protein precursor (APP) corresponding to the amino terminus of the 4K Ab peptide generated by beta- and gamma-secretases.The immunogen is located within amino acids 650 – 700 of APP.
Host Species: Rabbit
Purification: APP Antibody is affinity chromatography purified via peptide column.
Physical State: Liquid
CAS NO.: 58569-55-4
Product: Tyr-Gly-Gly-Phe-Met-OH
Buffer: APP Antibody is supplied in PBS containing 0.02% sodium azide.
Concentration: 1 mg/mL
Storage Conditions: APP antibody can be stored at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: APP Antibody: AAA, AD1, PN2, ABPP, APPI, CVAP, ABETA, PN-II, CTFgamma, A4, Amyloid beta A4 protein, APP
Accession NO.: CAA30050
Protein Ino: 28721
Official Symbol: APP
Geneid: 351
Background: APP Antibody: Accumulation of the amyloid-beta peptide (Abeta) in the cerebral cortex is a critical event in the pathogenesis of Alzheimers disease. The beta-amyloid protein precursor (APP) is cleaved by beta-secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide (Abeta), which is deposited in the brains of all suffers of Alzheimers disease.
PubMed ID:http://aac.asm.org/content/53/3/926.abstract
