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Merck

A5213

Sigma-Aldrich

Anti-β-Amyloid antibody, Mouse monoclonal

enhanced validation

clone BAM-10, ascites fluid

Szinonimák:

Anti-β-Amyloid antibody, Mouse monoclonal, Anti-A-BETA, Anti-Amyloid β Precursor Protein, Clone BAM91

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.41

biológiai forrás

mouse

Minőségi szint

konjugátum

unconjugated

antitest forma

ascites fluid

antitest terméktípus

primary antibodies

klón

BAM-10, monoclonal

tartalmaz

15 mM sodium azide

faj reaktivitás

human

fejlettebb validálás

independent
Learn more about Antibody Enhanced Validation

technika/technikák

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

izotípus

IgG1

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... APP(351) , APP(351)

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Általános leírás

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.

Egyediség

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.

Alkalmazás

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.

Biokémiai/fiziológiai hatások

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.

Fizikai forma

Monoclonal Anti-β-Amyloid Protein is provided as ascites fluid with 15mM sodium azide as a preservative.

Tárolás és stabilitás

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.

Jogi nyilatkozat

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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Tárolási osztály kódja

10 - Combustible liquids

WGK

nwg

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

Az ügyfelek ezeket is megtekintették

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)
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
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)
Effects of Folic Acid on Secretases Involved in Aβ Deposition in APP/PS1 Mice
Tian, T, et al.
Nutrients, 8(9), 556-556 (2016)

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