Thermo Fisher Scientific beta-Amyloid Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

0.1-1.0 µg/mL

-

Immunocytochemistry (ICC/IF)

5-20 µg/mL

-

ELISA (ELISA)

0.1-1 µg/mL

-

Product Specifications

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

A synthetic peptide corresponding to amino acids 1-17 of beta-amyloid conjugated to KLH if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:beta Amyloid,uniProtId:P05067-1,ncbiNodeId:9606,antigenRange:1-17,antigenLength:770,antigenImageFileName:A00685-40_beta_Amyloid_P05067-1_Rabbit.svg,antigenImageFileNamePDP:A00685-40_beta_Amyloid_P05067-1_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

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Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Storage conditions

-20°C or -80°C if preferred

Shipping conditions

Wet ice

Product Specific Information

Reconstitute the lyophilized antibody with deionized water (or equivalent) to a final concentration of 0.5 mg/ml.

A number of mutations, identified in the gene encoding the β-amyloid precursor protein (βAPP), have been linked to early-onset Familial Alzheimers Disease. βAPP is cleaved sequentially by the proteolytic enzymes β-secretase and γ-secretase to produce β-amyloid (Aβ) peptides with the Aβ1-42(43) and the Aβ1-40 forms being the most prevalent. Secreted Aβ peptides can bind to scavenger receptors and the receptor for advanced glycation endproducts. Aβ peptides are degraded either via a reuptake mechanism followed by endosomal degradation or by an extracellular insulin-degrading enzyme. Extracellular accumulation of Aβ leads to formation of aggregates, fibrils, and eventually amyloid deposits called neuritic plaques, a hallmark of Alzheimer`s disease. β-amyloid antibodies and peptides have been developed as tools for elucidating the biology of Alzheimers disease.

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.