产品名称
Anti-Ubiquitin K11 linkage Antibody, clone 2A3/2E6, clone 2A3/2E6, from rabbit
biological source
rabbit
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
2A3/2E6, monoclonal
species reactivity
human
species reactivity (predicted by homology)
all (based on 100% sequence homology)
technique(s)
immunocytochemistry: suitable
western blot: suitable
isotype
IgG
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... UBAP2(55833)
Analysis Note
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.
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.
Application
Immunocytochemistry Analysis: A 1:500 dilution from a representative lot detected Ubiquitin K11 linkage in A431 and HeLa cells.
Research Category
Signaling
Signaling
Research Sub Category
Developmental Signaling
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.
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.
General description
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.
Varies
Immunogen
Recombinant protein corresponding to all in Ubiquitin K11 linkage.
Physical form
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.
Preparation Note
Stable for 1 year at 2-8°C from date of receipt.
未找到合适的产品？
试试我们的产品选型工具.
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
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
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
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
我们的科学家团队拥有各种研究领域经验，包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.
联系客户支持