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|Tested species reactivity||Human, Non-human primate|
|Published species reactivity||Human|
|Host / Isotype||Mouse / IgG1|
|Immunogen||Native, secreted form of APP|
|Storage buffer||PBS, pH 7.4|
|Storage Conditions||-80° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|ELISA (ELISA)||10 µg/ml|
|Immunocytochemistry (ICC)||0.5-5 µg/ml|
|Immunoprecipitation (IP)||25 µg/ml*|
|Western Blot (WB)||5 µg/ml|
* 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.
|ELISA (ELISA)||See 1 publications below|
OMA1-03132 detects amyloid precursor protein (APP) from human and monkey tissues. This antibody is specific for native, non-denatured protein, and does not cross-react with mouse, rat APP or other APP homologs.
OMA1-03132 has been successfully used in Western blot (non-reducing conditions), immunocytochemistry, immunoprecipitation and ELISA procedures. This antibody does not work in in IHC on paraffin embedded tissues nor does it recognize APP if the samples are boiled in Laemmli (SDS) sample buffer containing a reducing agent such as DTT or ß-ME. Can be used in immunoprecipitation utilizing 25 µg/ml of OMA1-03132 linked sepharose.
OMA1-03132 antigen is the native, secreted form of human APP. The epitope recognized by OMA1-03132 maps to residues 104-118 of APP
Amyloid beta peptide is the major constituent of amyloid plaques in the brains of individuals afflicted with Alzheimer"e;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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Spirocyclic sulfamides as β-secretase 1 (BACE-1) inhibitors for the treatment of Alzheimer's disease: utilization of structure based drug design, WaterMap, and CNS penetration studies to identify centrally efficacious inhibitors.
OMA1-03132 was used in ELISA to report on the design of novel spirocyclic sulphamide BACE-1 inhibitors as potential Alzheimer's disease therapeutics
|Brodney MA,Barreiro G,Ogilvie K,Hajos-Korcsok E,Murray J,Vajdos F,Ambroise C,Christoffersen C,Fisher K,Lanyon L,Liu J,Nolan CE,Withka JM,Borzilleri KA,Efremov I,Oborski CE,Varghese A,O'Neill BT||Journal of medicinal chemistry (55:9224)||2012|
AAA antibody; alzheimer disease amyloid protein; amyloid beta (A4) precursor protein; amyloid precursor protein; APP; beta-amyloid peptide; beta-amyloid peptide(1-40); beta-amyloid peptide(1-42); beta-amyloid precursor protein; cerebral vascular amyloid peptide; CVAP; peptidase nexin-II; PN-II; preA4; protease nexin-II; testicular tissue protein Li 2
A4; AAA; ABETA; ABPP; AD1; APP; APPI; CTFgamma; CVAP; PN-II; PN2