A5213

Sigma-Aldrich

Monoclonal Anti-β-Amyloid antibody produced in mouse

clone BAM-10, ascites fluid

Synonym(s):
Anti-A-BETA, Anti-Amyloid β Precursor Protein, Clone BAM91
MDL number:
NACRES:
NA.41
Pricing and availability is not currently available.

Quality Level

biological source

mouse

antibody form

ascites fluid

antibody product type

primary antibodies

clone

BAM-10, monoclonal

contains

15 mM sodium azide

species reactivity

human

application(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

conjugate

unconjugated

shipped in

dry ice

storage temp.

−20°C

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General description

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.
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.

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

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.
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.
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.

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.

RIDADR

NONH for all modes of transport

WGK Germany

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Anyang Sun et al.
Experimental neurology, 175(1), 10-22 (2002-05-16)
Chronic accumulation of beta-amyloid in the brain has been shown to result in complex molecular and cellular changes that accompany neurodegeneration in Alzheimer's disease (AD). In this study, we examined the expression of a newly identified beta-secretase, memapsin 2 (M2)...
Tae-Kyung Kim et al.
Experimental & molecular medicine, 44(8), 492-502 (2012-05-31)
Adequate assessment of plaque deposition levels in the brain of mouse models of Alzheimer disease (AD) is required in many core issues of studies on AD, including studies on the mechanisms underlying plaque pathogenesis, identification of cellular factors modifying plaque...
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)
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...
Xian-Hui Dong et al.
Experimental and therapeutic medicine, 9(4), 1319-1327 (2015-03-18)
Alzheimer's disease (AD) is a neurodegenerative brain disorder and the most common cause of dementia. New treatments for AD are required due to its increasing prevalence in aging populations. The present study evaluated the effects of the active components of
Articles
Alzheimer's disease (AD) is the most common cause of dementia in the elderly and is characterized by gradual loss of cognitive functions.
Read More

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