SKP2 Antibody - C-terminal region (ARP30219_P050)
- Known as:
- SKP2 Antibody - C-terminal region (ARP30219_P050)
- Catalog number:
- arp30219_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- SKP2 Antibody - C-terminal region (ARP30219_P050)
Related genes to: SKP2 Antibody - C-terminal region (ARP30219_P050)
- Gene:
- SKP2 NIH gene
- Name:
- S-phase kinase associated protein 2
- Previous symbol:
- -
- Synonyms:
- FBXL1, FBL1, p45
- Chromosome:
- 5p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-12-18
- Date modifiied:
- 2016-10-05
Related products to: SKP2 Antibody - C-terminal region (ARP30219_P050)
Related articles to: SKP2 Antibody - C-terminal region (ARP30219_P050)
- Osteosarcoma (OS) is an aggressive bone malignancy with poor prognosis, characterized by high metastasis rates. Kinesin family member 18B (), a key protein in cell division and mitosis, has emerged as a potential diagnostic and therapeutic target in various cancers, including OS. This study investigates the role of in OS progression and its underlying mechanisms. We found that expression is significantly upregulated in OS tissues and correlates with lymph node metastasis (N-stage) and clinical stage. Knockdown of inhibited OS cell migration, invasion, proliferation, and tumorigenesis. Mechanistically, promotes OS survival through the ubiquitin-proteasome system (UPS) by regulating Skp2 protein degradation. knockdown accelerated Skp2 ubiquitination, leading to reduced Skp2 levels and inhibited OS cell viability and glycolytic metabolism. Overexpression of enhanced OS cell viability and glycolysis in an Skp2-dependent manner. These findings suggest that the -Skp2 axis plays a critical role in the metabolic reprogramming of OS cells and serves as a novel prognostic biomarker and therapeutic target in OS. - Source: PubMed
Publication date: 2026/04/02
Liu HaonanGuo XinLu ChaoxiangLu Daifeng - Cutaneous T-cell lymphoma (CTCL) is a skin-predominant form of non-Hodgkin lymphoma for which improved therapeutic options are needed. Here, we investigated the anti-lymphoma effects of pristimerin (PS) and defined its underlying mechanism in H9 and HH CTCL cell lines. PS strongly reduced cell growth and induced apoptosis, with hallmarks of mitochondrial (intrinsic) pathway activation, including caspase processing. PS also decreased basal AKT activity and downregulated pro-survival factors such as XIAP. In addition, PS reduced the abundance of S-phase kinase-associated protein 2 (SKP2) and was accompanied by increased levels of the cyclin-dependent kinase inhibitors p21 and p27. Genetic suppression of AKT intensified apoptosis-associated signaling, reflected by increased H2AX activation and PARP cleavage. Notably, PS elevated intracellular reactive oxygen species (ROS), and scavenging ROS with N-acetylcysteine (NAC) significantly attenuated PS-driven cytotoxicity, supporting a ROS-dependent mechanism. Finally, PS combined with the proteasome inhibitor bortezomib produced greater anti-CTCL activity than either agent alone, consistent with a synergistic interaction. Together, these findings show that PS promotes ROS-dependent, mitochondria-mediated apoptosis in CTCL and support further evaluation of PS-based strategies for this malignancy. - Source: PubMed
Publication date: 2026/04/03
Kuttikrishnan ShilpaAnver RasheedaAhmad FareedMariyam ZahwaHabeeba UmmuAkhtar SabahSalameh IsraaSiddiqui Shahid SPrabu Kirti SAnsari Abdul WBhat Ajaz AKhan Abdul QUddin Shahab - S-phase kinase-associated protein 2 (SKP2) is an oncogene and cell cycle regulator that mediates the ubiquitination of cell cycle regulators. Curcumol, a sesquiterpene natural product, has been reported to regulate SKP2-mediated ubiquitination degradation to overcome drug resistance in cancer cells. However, whether the cell cycle arrest effect of curcumol is related to SKP2's function in cancer cells and its mechanisms are still unclear. - Source: PubMed
Publication date: 2026/03/16
Yang YizhuangZhang RiqiuDou TongLiu ZhangchiAi RuiZhao YueCui ZhiChen XuWang Juan - Programmed Death-Ligand 1 (PD-L1) promotes tumor progression through several mechanisms, including its intrinsic effect on breast cancer cell proliferation via the S-Phase Kinase-Associated Protein 2 (SKP2)-p21/p27 (SKP2-p21/p27) axis. However, the specific regulatory signaling through which PD-L1 influences the SKP2-p21/p27 axis to drive cell proliferation remains unclear. To investigate how PD-L1 mediates SKP2-dependent proliferation, proteomic analyses, gene-expression manipulation via knockdown or overexpression, Western blotting, quantitative immunofluorescence, colony-forming assays, real-time cell analysis, and Xenograft-derived cells were used. Proteomic data analysis identified several PD-L1 downstream targets as potential candidate regulators of the SKP2-p21/p27 axis and activators of the PI3K/AKT pathway. Candidate screening by gene knockdown, followed by analyses of SKP2, p21, and p27 protein expression, revealed Livin and Galectin-1 as upstream regulators of the SKP2-p21/p27 axis. Moreover, Western blotting and quantitative immunofluorescence in three breast cancer cell lines confirmed that PD-L1 is an upstream regulator of Livin, Galectin-1, and SKP2 protein expression. Mechanistically, Livin and Galectin-1 enhanced AKT phosphorylation (Ser473) to sustain PI3K/AKT pathway activation in a positive feedback loop to upregulate SKP2 expression. Functional assays, including colony-forming assays and real-time cell analyzer, demonstrated that Livin and Galectin-1 are critical for PD-L1-mediated, SKP2-dependent proliferation. These findings were corroborated in vivo using xenograft-derived cells. Overall, these findings delineate a tumor-intrinsic signaling axis in which PD-L1 upregulates Livin and Galectin-1 to sustain PI3K/AKT activity and drive SKP2-dependent cell proliferation. Targeting Livin and/or Galectin-1 may provide a rational strategy to disrupt PD-L1-associated proliferative signaling and improve combinatorial therapeutic approaches in breast cancer. - Source: PubMed
Publication date: 2026/03/17
Elfoly MarwaAlaiya AyodeleAl-Hazzani Amal AAl-Alwan MontherGhebeh Hazem - Vanadium compounds are promising metallodrug candidates, with well-documented antidiabetic, antitumor, and anti-Alzheimer's activities. In search for the long-term beneficial or adverse effects of antidiabetic vanadyl complexes, we serendipitously discovered that the vanadyl complexes VOp-dmada exerted pro-healthy aging effects across a diverse panel of model organisms, i.e., yeast, C. elegans, and SAMP8 mice. Furthermore, VOp-dmada attenuated replicative senescence in mouse embryonic fibroblasts and alleviated thymic epithelial cell aging while preserving thymic architecture and function in a mouse model of dexamethasone-induced acute thymic atrophy. Mechanistic investigations revealed that VOp-dmada improved the structural integrity and functional capacity of mitochondrial complex II. This effect was mediated by activation of the c-Myc/S-phase kinase-associated protein 2 (SKP2)/sirtuin 3 (SIRT3) signaling axis, which in turn upregulated succinate dehydrogenase subunit A (SDHA) expression. Thus, vanadyl complexes suppressed reactive oxygen species (ROS) generation at the source, disrupted the deleterious ROS-thioredoxin-interacting protein (TXNIP) vicious cycle, and ultimately decelerated the aging process. Our findings highlight the potential application of antidiabetic vanadium complexes in the treatment of other aging-related disorders and corroborate the chronic safety profile. Moreover, these results support the targeting of mitochondrial complex II function and integrity as a novel strategy for the discovery of pro-healthy aging agents. - Source: PubMed
Wang JiayuZhang BowenLiu LiwenLi XinXie ZhengweiYang Xiaoda