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Merck
모든 사진(1)

문서

AB2286

Sigma-Aldrich

Anti-Amyloid Fibrils OC Antibody

serum, Chemicon®

동의어(들):

Amyloid Fibrils, Amyloid Fibrils OC

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About This Item

UNSPSC 코드:
12352203
eCl@ss:
32160702
NACRES:
NA.41

생물학적 소스

rabbit

Quality Level

항체 형태

serum

항체 생산 유형

primary antibodies

클론

polyclonal

종 반응성

human

종 반응성(상동성에 의해 예측)

rat, mouse

제조업체/상표

Chemicon®

기술

ELISA: suitable
dot blot: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

동형

IgG

UniProt 수납 번호

배송 상태

wet ice

타겟 번역 후 변형

unmodified

유전자 정보

human ... APP(351)
mouse ... App(11820)

일반 설명

Amyloid monomeric proteins can sometimes oligomerize into destructive amyloid fibrils. Amyloidogenic conformations of non-disease related proteins can be created by partial protein misfolding or denaturation. In disease state oligomerization, extensive amyloid oligomerization creates plaques in neural tissue that correlates with Alzheimer’s symptomology.

특이성

This antibody recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrillar oligomers or natively folded proteins. It may also show weak reactivity against Aβ monomers while AB2287 does not.

면역원

Fibrils prepared from human Aß42 peptide.

애플리케이션

Anti-Amyloid Fibrils OC Antibody is an antibody against Amyloid Fibrils OC for use in IP, IC, IH, ELISA, WB, DB.
Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in monomers, oligos, and fibrils.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

품질

Evaluated by Dot Blot in monomers, oligos, and fibrils.

Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in monomers, oligos, and fibrils.

물리적 형태

Unpurified
Unpurified rabbit polyclonal antibody serum containing 0.05% sodium azide.

저장 및 안정성

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

분석 메모

Control
Alzheimer′s Brain tissue

법적 정보

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

면책조항

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1


시험 성적서(COA)

제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.

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문서 라이브러리 방문

Rosa Sánchez et al.
Scientific reports, 6, 32801-32801 (2016-09-07)
Amyloids are polymeric structural states formed from locally or totally unfolded protein chains that permit surface reorganizations, stability enhancements and interaction properties that are absent in the precursor monomers. β-Parvalbumin, the major allergen in fish allergy, forms amyloids that are
TGFbeta1 activates c-Jun and Erk1 via alphaVbeta6 integrin.
Luettich, K; Schmidt, C
Molecular Cancer null
Sofia B Carvalho et al.
PloS one, 8(10), e76629-e76629 (2013-10-08)
S100 proteins are small dimeric calcium-binding proteins which control cell cycle, growth and differentiation via interactions with different target proteins. Intrinsic disorder is a hallmark among many signaling proteins and S100 proteins have been proposed to contain disorder-prone regions. Interestingly
Peng Liu et al.
Cell reports, 11(11), 1760-1771 (2015-06-09)
The accumulation of amyloid-β (Aβ) as amyloid fibrils and toxic oligomers is an important step in the development of Alzheimer's disease (AD). However, there are numerous potentially toxic oligomers and little is known about their neurological effects when generated in
Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models.
Sontag, EM; Lotz, GP; Agrawal, N; Tran, A; Aron, R; Yang, G; Necula, M; Lau et al.
The Journal of Neuroscience null

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