Thermo Fisher Scientific beta Amyloid (1-43) Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

-

View 1 publication 1 publication

Immunohistochemistry (IHC)

-

View 2 publications 2 publications

Functional Assay (Functional)

Assay-dependent

-

Radioimmune Assays (RIA)

Assay-dependent

-

Dot blot (DB)

0.05-1.0 µg/mL

-

Product Specifications

Species Reactivity

Human

Published species

Human, Mouse

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

a 40 to 43 amino acid peptide cleaved from amyloid precursor protein (APP). if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:beta Amyloid,uniProtId:P05067-1,ncbiNodeId:9606,antigenRange:40-43,antigenLength:770,antigenImageFileName:44-340_beta_Amyloid_P05067-1_Rabbit.svg,antigenImageFileNamePDP:44-340_beta_Amyloid_P05067-1_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

View immunogen .st0{fill:#FFFFFF;} .st1{fill:#1E8AE7;}

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Purification

Antigen affinity chromatography

Storage buffer

PBS, pH 7.4

Contains

no preservative

Storage conditions

-20°C

Shipping conditions

Ambient (domestic); Wet ice (international)

RRID

AB_2533635

Product Specific Information

This beta Amyloid (1-43) antibody (44-340) is purified from rabbit serum by epitope-specific affinity chromatography. Any reactivity towards both full length A beta 40 and A beta 42 protein has been eliminated through a series of preabsorption steps.

This antibody shows no significant cross-reactivity against A beta 40 or A beta 42.

Target Information

Amyloid beta peptide (Abeta/Beta-amyloid) is the major constituent of amyloid plaques in the brains of individuals afflicted with Alzheimers 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. Alzheimers 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.