Shkbp1 antibody - N-terminal region (ARP35400_P050)
- Known as:
- Shkbp1 (anti-) - N-terminal region (ARP35400_P050)
- Catalog number:
- arp35400_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- Shkbp1 antibody - N-terminal region (ARP35400_P050)
Related genes to: Shkbp1 antibody - N-terminal region (ARP35400_P050)
- Gene:
- SHKBP1 NIH gene
- Name:
- SH3KBP1 binding protein 1
- Previous symbol:
- -
- Synonyms:
- PP203, Sb1
- Chromosome:
- 19q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-12
- Date modifiied:
- 2013-01-10
Related products to: Shkbp1 antibody - N-terminal region (ARP35400_P050)
Related articles to: Shkbp1 antibody - N-terminal region (ARP35400_P050)
- [This retracts the article DOI: 10.1016/j.omtn.2017.12.014.]. - Source: PubMed
Publication date: 2026/03/16
He QianruZhao LiniLiu YunhuiLiu XiaobaiZheng JianYu HaiCai HengMa JunLiu LiboWang PingLi ZhenXue Yixue - SQSTM1/p62 is a master regulator of the autophagic and ubiquitination pathways of protein degradation and the antioxidant response. p62 functions in these pathways via reversible assembly and sequestration of additional factors into cytoplasmic phase-separated structures termed p62 bodies. The physiological roles of p62 in these various pathways depend on numerous mechanisms for regulating p62 body formation and dynamics that are incompletely understood. Here, we identify a new mechanism for regulation of p62 oligomerization and incorporation into p62 bodies by SHKBP1, a cullin-3 E3 ubiquitin ligase adaptor, that is independent of its potential functions in ubiquitination. We map an SHKBP1-p62 protein-protein interaction outside of p62 bodies that limits p62 assembly into p62 bodies and affects the antioxidant response involving sequestration of Keap1 and nuclear translocation of Nrf2. These studies provide a non-ubiquitination-based mechanism for an E3 ligase adaptor in regulating p62 body formation and cellular responses to oxidative stress. - Source: PubMed
Publication date: 2026/02/06
Luan LinCao XiaofuXia ZijunVaid ShivanshiLeonetti Manuel DBaskin Jeremy M - Identifying novel biomarkers for sepsis is essential for improving patient outcomes. Cuproptosis, a recently discovered form of cell death associated with various diseases, has an unclear relationship with sepsis. This study aimed to elucidate the expression patterns of cuproptosis-related genes(CRGs) in sepsis, identifying potential biomarkers and therapeutic targets. - Source: PubMed
Publication date: 2025/12/08
Wu FanLu JunlinLiu YiZhou RunquanLi WenjuanWang MingxingXu ShanSheng YuanhuiZhang Dan - SQSTM1/p62 is a master regulator of the autophagic and ubiquitination pathways of protein degradation and the antioxidant response. p62 functions in these pathways via reversible assembly and sequestration of additional factors into cytoplasmic phase-separated structures termed p62 bodies. The physiological roles of p62 in these various pathways depends on numerous mechanisms for regulating p62 body formation and dynamics that are incompletely understood. Here, we identify a new mechanism for regulation of p62 oligomerization and incorporation into p62 bodies by SHKBP1, a Cullin-3 E3 ubiquitin ligase adaptor, that is independent of its potential functions in ubiquitination. We map a SHKBP1-p62 protein-protein interaction outside of p62 bodies that limits p62 assembly into p62 bodies and affects the antioxidant response by preventing sequestration and degradation of Keap1. These studies provide a non-ubiquitination-based mechanism for an E3 ligase adaptor in regulating p62 phase separation and cellular responses to oxidative stress. - Source: PubMed
Publication date: 2025/01/22
Luan LinCao XiaofuBaskin Jeremy M - CD8 + effector cells are highly skilled in immune surveillance and contribute to adaptive immunity against cancer cells. An increasing number of molecular factors affecting T-cell differentiation may alter T-cell function by increasing or decreasing the capacity of the immune system to kill cancer cells. Here, Sh3kbp1 binding protein 1 (Shkbp1), known as CIN85 binding protein or SETA binding protein, was found to be expressed in immune organs and immune cells. Shkbp1 knockout mice presented abnormal red and white pulp structures in spleen. Shkbp1 knockout increased CD8 + T cell number in spleen and enhanced the function of isolated CD8 + T cells from Shkbp1 knockout mice. The subcutaneous melanoma model in Shkbp1 knockout mice showed that tumor growth was inhibited, and the infiltration of CD8 + T cells in tumor tissue was increased. Furthermore, adenoviral therapy targeting Shkbp1 indicated that knockout of Shkbp1 increased CD8 + T cells and inhibited tumor growth. This study provides new insights into the role of Shkbp1 in CD8 differentiation and functions, suggesting that Shkbp1 may be a new, potential target in cancer immunotherapy. - Source: PubMed
Publication date: 2023/06/19
Guo XiaolanLi HaobinMeng XiuqiongZhao ZhiBinZhang RongxinWang LijingLi Jiangchao