|Tested species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||1-42 of Amyloid Beta|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS, pH 7.2|
|Contains||0.1% sodium azide|
|Tested Applications||Dilution *|
|Dot blot (DB)||0.05-1.0 ug/ml|
|Functional Assay (FN)||Assay Dependent|
|Radioimmune Assays (RIA)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Amyloid beta peptide is the major constituent of amyloid plaques in the brains of individuals afflicted with Alzheimer and quote;s disease. This peptide is generated from the beta-amyloid precursor protein (beta APP) in a two-step process. The first step involves cleavage of the extracellular, amino-terminal domain of beta APP. Protein cleavage is performed by an aspartyl protease termed beta-secretase (BACE). This enzyme is synthesized as a propeptide that must be modified to the mature and active form by the prohormone convertase, furin. Beta APP cleavage by the mature form of BACE results in the cellular secretion of a segment of beta APP and a membrane-bound remnant. This remnant is then processed by another protease termed gamma-secretase. Gamma-secretase cleaves an intra-membrane site in the carboxyl-terminal domain of beta APP, thus generating the amyloid beta peptide. Gamma-secretase is believed to be a multi-subunit complex containing presenilin-1 and 2 as central components. Found associated with the presenilins is the transmembrane glycoprotein nicastrin. Nicastrin has been found to bind to the carboxyl-terminus of betaAPP and helps to modulate the production of the amyloid beta peptide.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.