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Invitrogen
Amyloid Precursor Protein Polyclonal Antibody
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FIGURE: 1 / 2
Amyloid Precursor Protein Antibody (PA1-33107) in WB
Western blot was performed using Anti-Amyloid Precursor Protein Polyclonal Antibody(Product # PA1-33107) and a 120, 90kDa band corresponding to Amyloid Precursor Protein was observed across the panel tested except for Mouse Skeletal Muscle and Rat Skeletal Muscle which are reported to be negative. Tissue extracts (30 µg lysate) of Mouse Brain (Lane 1), Mouse Skeletal Muscle (Lane 2), Rat Brain (Lane 3) and ... View More
Product Details
PA1-33107
Applications
Tested Dilution
Publications
Product Specifications
Host/Isotype
Rabbit
/ IgG
Class
Polyclonal
Type
Antibody
Immunogen
Proprietary immunogen
Conjugate
Form
Liquid
Concentration
Conc. Not Determined
Storage conditions
Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.
Shipping conditions
Wet ice
RRID
AB_1956112
Product Specific Information
PA1-33107 detects APP from human, monkey, and mouse samples.
Target Information
Amyloid beta peptide (Abeta/Beta-amyloid) is the major constituent of amyloid plaques in the brains of individuals afflicted with Alzheimer's disease. Abeta peptide is 40-43 amino acids long and 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, beta-secretase (BACE) which is synthesized as a propeptide and 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. The remnant protein is processed by another protease, 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. The transmembrane glycoprotein, nicastrin, is associated with presinilins and has been found to bind to the carboxyl-terminus of beta APP and helps to modulate the production of the amyloid beta peptide. Abeta is an extracellular filamentous protein component of amyloid cores, neuritic plaques and is also found as a deposit in neurofibrillary tangles. Alzheimer's disease, the most common cause of senile dementia, is characterized by abnormal filamentous protein deposits in the brain. Beta amyloid deposits are also detected in Lewy body dementia, Down's syndrome, amyloidosis (Dutch type), cerebroarterial amyloidosis (cerebral amyloid angiopathy) and in the Guam Parkinson-Dementia complex.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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