A5213
Anti-β-Amyloid antibody, Mouse monoclonal
clone BAM-10, ascites fluid
Synonyme(s) :
Anti-A-BETA, Anti-Amyloid Beta Precursor Protein
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About This Item
Produits recommandés
Source biologique
mouse
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
ascites fluid
Type de produit anticorps
primary antibodies
Clone
BAM-10, monoclonal
Contient
15 mM sodium azide
Espèces réactives
human
Validation améliorée
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
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
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Description générale
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.
Spécificité
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.
Immunogène
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.
Actions biochimiques/physiologiques
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.
Forme physique
Monoclonal Anti-β-Amyloid Protein is provided as ascites fluid with 15mM sodium azide as a preservative.
Stockage et stabilité
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.
Clause de non-responsabilité
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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Produit(s) apparenté(s)
Réf. du produit
Description
Tarif
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
nwg
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
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
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
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
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
Folic acid deficiency enhances aβ accumulation in APP/PS1 mice brain and decreases amyloid-associated miRNAs expression
Liu, H, et al.
The Journal of Nutritional Biochemistry, 26(12), 1502-1508 (2015)
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