Anti-Ubiquitin monoclonal antibody (CABT-LM000160)

Specifications


Host Species
Mouse
Antibody Isotype
IgG1
Clone
2C4
Species Reactivity
Bovine
Immunogen
Bovine erythrocyte ubiquitin
Conjugate
Unconjugated

Citations


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References


Multifaceted HIV-1 Vif interactions with human E3 ubiquitin ligase and APOBEC3s

FEBS JOURNAL

Authors: Hu, Yingxia; Knecht, Kirsten M.; Shen, Qi; Xiong, Yong

APOBEC3 (A3) proteins are a family of host antiviral restriction factors that potently inhibit various retroviral infections, including human immunodeficiency virus (HIV)-1. To overcome this restriction, HIV-1 virion infectivity factor (Vif) recruits the cellular cofactor CBF beta to assist in targeting A3 proteins to a host E3 ligase complex for polyubiquitination and subsequent proteasomal degradation. Intervention of the Vif-A3 interactions could be a promising therapeutic strategy to facilitate A3-mediated suppression of HIV-1 in patients. In this structural snapshot, we review the structural features of the recently determined structure of human A3F in complex with HIV-1 Vif and its cofactor CBF beta, discuss insights into the molecular principles of Vif-A3 interplay during the arms race between the virus and host, and highlight the therapeutic implications.

SUMOylation enhances the activity of IDH2 under oxidative stress

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Authors: Yu, Yun; Chen, Yalan; Liu, Kexin; Cheng, Jinke; Tu, Jun

Mitochondria play a central role in biological oxidation that inevitably generates reactive oxygen species (ROS) as by-products. Maintenance of mitochondrial redox balance status requires NADPH, which is primarily generated by the mitochondrial matrix protein isocitrate dehydrogenase 2 (IDH2). The activity of IDH2 is regulated by post-translational modifications (PTMs). In this study, we found IDH2 is modified by small ubiquitin-like modifier 1 (SUMO1) at lysine 45. SUMO specific protease 1 (SENP1) is responsible for deSUMOylation of IDH2. SUMOylation of IDH2 is induced by oxidants and enhances the antioxidant activity of IDH2 to protect cells against oxidative stress. Mutation of the SUMOylation site impairs the enzymatic activity of IDH2 and hence decreases levels of alpha-ketoglutarate (alpha-KG), NADPH and GSH. Cells with SUMOylation deficient IDH2 suffer more apoptosis than that with wild type IDH2 under oxidative stress. These results indicate that SUMOylation is an important way to regulate IDH2 activity to maintain mitochondrial redox balance. (C) 2020 Elsevier Inc. All rights reserved.

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