|Tested species reactivity||Human|
|Published species reactivity||Not Applicable|
|Host / Isotype||Rabbit / IgG|
|Immunogen||The antibody was produced using a synthetic peptide derived from amino acids 34-40 within the carboxyl-terminus region of human beta-Amyloid protein.|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.3|
|Tested Applications||Dilution *|
|Dot blot (DB)||Assay Dependent|
|ELISA (ELISA)||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.
|Not Applicable||Not Cited||
Hyperphosphorylated tau in young and middle-aged subjects.
44-348A was used in immunohistochemistry - paraffin section to examine the brains of cognitively unimpaired subjects for neurodegenerative changes
|Elobeid A,Soininen H,Alafuzoff I||Acta neuropathologica (123:97)||2012|
Abeta-related angiitis: primary angiitis of the central nervous system associated with cerebral amyloid angiopathy.
44-348A was used in immunohistochemistry - paraffin section to describe patients with Abeta-related angiitis
|Scolding NJ,Joseph F,Kirby PA,Mazanti I,Gray F,Mikol J,Ellison D,Hilton DA,Williams TL,MacKenzie JM,Xuereb JH,Love S||Brain : a journal of neurology (128:500)||2005|
Osteopetrotic (op/op) mice have reduced microglia, no Abeta deposition, and no changes in dopaminergic neurons.
44-348A was used in immunohistochemistry to test if the lack of CSF-1 affects dopaminergic neuron development and CD200 expression
|Kondo Y,Lemere CA,Seabrook TJ||Journal of neuroinflammation (4:null)||2007|
Upregulation of tPA/plasminogen proteolytic system in the periphery of amyloid deposits in the Tg2576 mouse model of Alzheimer's disease.
44-348A was used in immunohistochemistry to characterize a Tg2576 mouse model of Alzheimer's disease and upregulation of tPA/plasminogen proteolytic system in the periphery of amyloid deposits
|Lee JY,Kweon HS,Cho E,Lee JY,Byun HR,Kim DH,Kim YH,Han PL,Koh JY||Neuroscience letters (423:82)||2007|
Intraneuronal Abeta immunoreactivity is not a predictor of brain amyloidosis-beta or neurofibrillary degeneration.
44-348A was used in immunohistochemistry to test if intraneuronal Abeta immunoreactivity is an early manifestation of Alzheimer-type pathology
|Wegiel J,Kuchna I,Nowicki K,Frackowiak J,Mazur-Kolecka B,Imaki H,Wegiel J,Mehta PD,Silverman WP,Reisberg B,Deleon M,Wisniewski T,Pirttilla T,Frey H,Lehtimäki T,Kivimäki T,Visser FE,Kamphorst W,Potempska A,Bolton D,Currie JR,Miller DL||Acta neuropathologica (113:389)||2007|