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Merck
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重要文件

MABS107-I

Sigma-Aldrich

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

clone 2A3/2E6, from rabbit

同義詞:

Ubiquitin K11 linkage, Lysine 11

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About This Item

分類程式碼代碼:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物源

rabbit

抗體表格

purified immunoglobulin

抗體產品種類

primary antibodies

無性繁殖

2A3/2E6, monoclonal

物種活性

human

物種活性(以同源性預測)

all (based on 100% sequence homology)

技術

immunocytochemistry: suitable
western blot: suitable

同型

IgG

運輸包裝

wet ice

目標翻譯後修改

unmodified

基因資訊

human ... UBAP2(55833)

一般說明

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.

免疫原

Recombinant protein corresponding to all in Ubiquitin K11 linkage.

應用

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.

品質

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.

標靶描述

Varies

外觀

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

儲存和穩定性

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

免責聲明

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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儲存類別代碼

12 - Non Combustible Liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


分析證明 (COA)

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存取文件庫

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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