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Merck
모든 사진(2)

주요 문서

MABS107-I

Sigma-Aldrich

Anti-Ubiquitin K11 linkage Antibody, clone 2A3/2E6

clone 2A3/2E6, from rabbit

동의어(들):

Ubiquitin K11 linkage, Lysine 11

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About This Item

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

생물학적 소스

rabbit

항체 형태

purified immunoglobulin

항체 생산 유형

primary antibodies

클론

2A3/2E6, monoclonal

종 반응성

human

종 반응성(상동성에 의해 예측)

all (based on 100% sequence homology)

기술

immunocytochemistry: suitable
western blot: suitable

동형

IgG

배송 상태

wet ice

타겟 번역 후 변형

unmodified

유전자 정보

human ... UBAP2(55833)

일반 설명

Recently, the lysine11 (K11) linkage of ubiquitin has been shown to be specifically targeted by the Anaphase-Promoting Complex (APC) E3 ubiquitin ligase for catalyzed ubiquitination for mitosis. Antibodies specific to the K11-linkage have shown that the formation of the K11 chains are greatly increased in mitotic human cells in the presence of APC substrate degradation. K11-linked ubiquitin chains seem to have essential regulatory control over mitotic protein degradation.

면역원

Recombinant protein corresponding to all in Ubiquitin K11 linkage.

애플리케이션

Immunocytochemistry Analysis: A 1:500 dilution from a representative lot detected Ubiquitin K11 linkage in A431 and HeLa cells.
Research Category
Signaling
Research Sub Category
Developmental Signaling
This Anti-Ubiquitin K11 linkage Antibody, clone 2A3/2E6 is validated for use in western blotting & ICC for the detection of Ubiquitin K11 linkage.

품질

Evaluated by Western Blotting in K11 recombinant protein.

Western Blotting Analysis: A 1:250 to 1:1,000 dilution of this antibody detected Ubiquitin K11 linkage in 10 µg of K11 recombinant protein.

표적 설명

Varies

물리적 형태

Format: Purified
Protein A purified
Purified rabbit monoclonal IgG in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

저장 및 안정성

Stable for 1 year at 2-8°C from date of receipt.

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

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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

Mingwei Min et al.
Molecular biology of the cell, 26(24), 4325-4332 (2015-10-09)
The ubiquitin proteasome system (UPS) directs programmed destruction of key cellular regulators via posttranslational modification of its targets with polyubiquitin chains. These commonly contain Lys-48 (K48)-directed ubiquitin linkages, but chains containing atypical Lys-11 (K11) linkages also target substrates to the
Rahul S Samant et al.
Nature, 563(7731), 407-411 (2018-11-16)
Protein misfolding is linked to a wide array of human disorders, including Alzheimer's disease, Parkinson's disease and type II diabetes1,2. Protective cellular protein quality control (PQC) mechanisms have evolved to selectively recognize misfolded proteins and limit their toxic effects3-9, thus
Michael E French et al.
The Journal of biological chemistry, 292(25), 10398-10413 (2017-05-04)
Homologous to E6AP C-terminal (HECT) ubiquitin (Ub) ligases (E3s) are a large class of enzymes that bind to their substrates and catalyze ubiquitination through the formation of a Ub thioester intermediate. The mechanisms by which these E3s assemble polyubiquitin chains
Swarna L Vijayaraj et al.
Nature communications, 12(1), 2713-2713 (2021-05-13)
Interleukin-1β (IL-1β) is activated by inflammasome-associated caspase-1 in rare autoinflammatory conditions and in a variety of other inflammatory diseases. Therefore, IL-1β activity must be fine-tuned to enable anti-microbial responses whilst limiting collateral damage. Here, we show that precursor IL-1β is
Animesh Dhara et al.
mSphere, 1(3) (2016-06-25)
The contribution of ubiquitin-mediated mechanisms in the regulation of the Toxoplasma gondii cell cycle has remained largely unexplored. Here, we describe the functional characterization of a T. gondii deubiquitinase (TGGT1_258780) of the ovarian-tumor domain-containing (OTU) family, which, based on its structural

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