A5213
Anti-β-Amyloid antibody, Mouse monoclonal
clone BAM-10, ascites fluid
Synonym(s):
Anti-β-Amyloid antibody, Mouse monoclonal, Anti-A-BETA, Anti-Amyloid β Precursor Protein, Clone BAM91
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About This Item
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biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
BAM-10, monoclonal
contains
15 mM sodium azide
species reactivity
human
enhanced validation
independent
Learn more about Antibody Enhanced Validation
technique(s)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:2,000 using formic acid-treated, formalin-fixed, human Alzheimer′s disease (AD) brain sections.
indirect ELISA: suitable
isotype
IgG1
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
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General description
β-amyloid protein or aβ4 is derived from larger protein that belongs to the family of 70kDa transmembrane glycoproteins (amyloid precursor proteins, APP). These are produced in various isoforms by alternative splicing. APPs are synthesized by many tissues including brain cells. Abnormal β-amyloid protein deposits have been associated with Alzheimer′s disease, Down′s syndrome, Dutch-type amyloidosis and Lewy body dementia.
The antibody reacts specifically with β-amyloid protein. The epitope recognized by the antibody resides within amino acids 1-12 of the β-amyloid protein. It specifically stains amyloid plaques within the cortex and amyloid deposits in blood vessels using formic acid-treated, formalin-fixed, paraffin-embedded, and Methacarn-fixed sections of human Alzheimer′s disease (AD) brain tissue.
Specificity
Monoclonal Anti-β-Amyloid Protein reacts specifically with β-amyloid protein. The epitope recognized by the antibody resides within amino acid residues 1-12 of the β-amyloid protein. The antibody specifically stains amyloid plaques within the cortex, and amyloid deposits in blood vessels, in formic acid-treated, formalin-fixed, paraffin-embedded and Methacarn-fixed sections of human Alzheimer′s disease (AD) brain tissue.
Immunogen
Synthetic β-amyloid peptide, conjugated to KLH.
Application
Monoclonal Anti- β Amyloid Protein may be used for the localization of β -amyloid protein using various immunochemical assays such as ELISA, competitive ELISA and immunohistochemistry.
Mouse monoclonal anti-ABETA was used to treat old WT PDAPP mice with amyloid accumulation and learning deficits in an attempt to improve learning and decrease accumulation, however no response was observed.
The antibody is useful in immunohistochemistry, immunoblotting, ELISA, and competitive ELISA. Also, this antibody has been used to neutralize Aβ assemblies in brains of transgenic mice expressing a mutant form of amyloid precursor protein, and for in vivo deep tissue imaging using near-IR optical spectrum.
Biochem/physiol Actions
β-amyloid fragments are amyloidogenic and neurotoxic both in vitro and in vivo. The presence of a large number of neuritic (senile) plaques and neurofibrillary tangles in the cerebral cortex is used as a pathological marker for a disease state and presents the major criterion for the diagnosis of Alzheimer′s disease at autopsy. A monoclonal antibody reacting specifically with β-amyloid protein is valuable for studying the nature of the β-amyloid protein by enabling detection and localization of β-amyloid protein and fragments.
Physical form
Monoclonal Anti-β-Amyloid Protein is provided as ascites fluid with 15mM sodium azide as a preservative.
Storage and Stability
For continuous use, store at 2-8 °C for no more than one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in "frost-free" freezers is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Tian Tian et al.
Nutrients, 8(9) (2016-09-13)
Alzheimer's disease (AD) is the most common type of dementia. Amyloid-β protein (Aβ) is identified as the core protein of neuritic plaques. Aβ is generated by the sequential cleavage of the amyloid precursor protein (APP) via the APP cleaving enzyme
Jessica F Jordão et al.
PloS one, 5(5), e10549-e10549 (2010-05-21)
Immunotherapy for Alzheimer's disease (AD) relies on antibodies directed against toxic amyloid-beta peptide (Abeta), which circulate in the bloodstream and remove Abeta from the brain. In mouse models of AD, the administration of anti-Abeta antibodies directly into the brain, in
Jared Ehrhart et al.
Journal of neuroinflammation, 2, 29-29 (2005-12-14)
Activated microglial cells have been implicated in a number of neurodegenerative disorders, including Alzheimer's disease (AD), multiple sclerosis (MS), and HIV dementia. It is well known that inflammatory mediators such as nitric oxide (NO), cytokines, and chemokines play an important
Deficits in object-in-place but not relative recency performance in the APPswe/PS1dE9 mouse model of Alzheimer?s disease: Implications for object recognition
Bonardi, C, et al.
Behavioural Brain Research, 313, 71-81 (2016)
Kendra L Puig et al.
Neurobiology of aging, 40, 22-40 (2016-03-15)
APP/PS1 double transgenic mice expressing human mutant amyloid precursor protein (APP) and presenilin-1 (PS1) demonstrate robust brain amyloid beta (Aβ) peptide containing plaque deposition, increased markers of oxidative stress, behavioral dysfunction, and proinflammatory gliosis. On the other hand, lack of
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