Bub3 antibody Polyclonal Antibodies Primary antibodies
- Known as:
- Bub3 (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb116210
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- Bub3 antibody Polyclonal Antibodies Primary antibodies
Related genes to: Bub3 antibody Polyclonal Antibodies Primary antibodies
- Gene:
- BUB3 NIH gene
- Name:
- BUB3 mitotic checkpoint protein
- Previous symbol:
- -
- Synonyms:
- BUB3L
- Chromosome:
- 10q26.13
- Locus Type:
- gene with protein product
- Date approved:
- 1999-02-17
- Date modifiied:
- 2019-01-18
Related products to: Bub3 antibody Polyclonal Antibodies Primary antibodies
Related articles to: Bub3 antibody Polyclonal Antibodies Primary antibodies
- Small cell lung cancer (SCLC) is marked by rapid tumor growth and poor outcomes and necessitates effective treatments. This paper explores the molecular mechanisms by which BCL11B affects immune escape in SCLC. - Source: PubMed
Publication date: 2026/07/15
Shao JiayueLiu ShuangqingQin LingFan NingningSun QiMeng Qingwei - The spindle assembly checkpoint (SAC) prevents sister chromatids separation until all chromosomes are properly attached to spindle microtubules and bi-oriented. SAC controls the metaphase-to-anaphase transition by inhibiting the anaphase promoting complex/cyclosome (APC/C). A critical step in this process is the recruitment of the Mad1-Mad2 complex to unattached kinetochores mediated by the KBB pathway (KNL1-Bub3-Bub1) and the RZZ pathway (Rod-Zw10-Zwilch). Here, we show that hSpindly contributes to the regulation of Mad1-Mad2 recruitment through the RZZ pathway. We demonstrate that hSpindly is a dynamic protein that oligomerizes at unattached kinetochores, and we identify threonine 552 as a key residue controlling its mobility and function. A non-phosphorylatable mutant (T552A) displays reduced dynamics at kinetochores, impairs SAC signaling, and increases cellular resistance to antimitotic drugs. Altogether, our findings identify hSpindly as a dynamic regulator of SAC signaling and potential therapeutic target for overcoming resistance to mitotic inhibitors. - Source: PubMed
Publication date: 2026/06/16
Mora-Santos MarHerrero-Ruiz JoaquínFennema-Galparsoro DirkBelmonte-Fernández AlejandroFerrandiz NuriaRomero Francisco - BACKGROUND: Lung adenocarcinoma (LUAD) is the most common form of lung cancer and is often diagnosed at advanced stages. NUF2, a key component of the NDC80 kinetochore complex, is highly expressed in several malignancies, but its function and regulatory mechanism in LUAD remain unclear. METHODS: Expression profiling using TCGA, GEO datasets, and LUAD tissue microarrays revealed NUF2 dysregulation in LUAD. Functional assays (CCK-8, EdU, colony formation, Transwell, and xenograft models) were performed to assess the effects of NUF2 gain- or loss-of-function. Protein interactions were examined using immunoprecipitation and mass spectrometry. Transcriptomic sequencing and Western blotting were used to evaluate downstream signaling pathways. RESULTS: NUF2 expression was significantly elevated in LUAD tissues and cell lines and was positively associated with tumor stage and poor overall survival. NUF2 knockdown inhibited LUAD cell proliferation, migration, and tumor growth, whereas NUF2 overexpression enhanced malignant behaviors. Mechanistically, NUF2 interacted with and stabilized the spindle checkpoint protein BUB3 by preventing proteasomal degradation. Additionally, NUF2 activated the NF-κB signaling pathway, and BUB3 was required for this activation. CONCLUSIONS: NUF2 promotes LUAD progression by stabilizing BUB3 and activating NF-κB signaling. Targeting the NUF2–BUB3 axis may represent a novel therapeutic strategy for LUAD. - Source: PubMed
Publication date: 2026/04/06
Zhu DingqiangLiang JinghuiLi JiachengYu WenhaoMa LuyuanTang ZhanpengLi RongyangQu ChenghaoHan JingyiWang DingxinLi LinTian Hui - The spindle assembly checkpoint (SAC) is vital for preventing oocyte aneuploidy, a leading cause of female infertility, miscarriages, and trisomy syndromes. However, whether deubiquitination participates in SAC regulation remains unknown. Here, we reveal that the deubiquitinase USP8 acts as a SAC regulator to prevent aneuploid egg formation. Mechanistically, depletion of USP8 inactivates the SAC, accelerates meiotic progression, and causes abnormal spindle assembly and chromosome alignment, ultimately leading to aneuploidy. Intriguingly, we identify USP8 in oocytes as a previously unidentified interaction partner of BUB3, a key component of the SAC, and demonstrate that USP8 stabilizes BUB3 through its deubiquitinating activity. Moreover, exogenous BUB3 rescues the defects observed in USP8-depleted oocytes. Together, our findings not only clarify that deubiquitination participates in regulating the SAC in oocytes but also uncover a unique role for USP8 in controlling the SAC via its interaction with BUB3. - Source: PubMed
Publication date: 2026/03/13
Zhou 周长银 ChangyinZhang 张雪 XueXu 许根露 GenluWang 王慧 HuiRan 冉宇婷 YutingLi 李昂 AngSun 孙青原 Qing-YuanOu 欧湘红 Xiang-Hong - Acrylamide is a synthetic material which is widely used in water treatment and paper manufacturing, and it is also generated from food formation, which shows neurological effects, skin irritation, or reproductive toxicity. Several studies focused on the effects of acrylamide on mitochondria and apoptosis in oocytes. In present study, we reported that acrylamide disturbed cell cycle progression of mouse oocyte meiosis. Our data showed that acrylamide caused both germinal vesicle (GV) breakdown and polar body extrusion defects. Further analysis indicated that acrylamide induced DNA damage in the GV oocytes, showing with increased γ-H2A.X expression, which active CHK2 for G2/M transition. This could be confirmed by the altered Cyclin B1 and CDK1 expression in oocytes. Besides, we found kinetochore-microtubule attachment was aberrant in metaphase I (MI) oocytes, which active spindle assembly checkpoint (SAC) for polar body extrusion, and this was confirmed by the consistent presentence of BubR1 and Bub3. This was due to the reduced tubulin acetylation-based microtubule stability, since HDAC6 and NAT10 expression was changed and cold treatment reduced the tubulin polymerization. Taken together, our study reported that acrylamide exposure disrupted cell cycle progression through DNA damage-based MPF activity and tubulin acetylation-based SAC activation in oocytes. - Source: PubMed
Publication date: 2026/01/30
Chen ShanshanWang Peng-XiaWang Yan-TingKe Xing-HeOu MinminSun Shao-ChenLiao Bi-YunChen Xuanyi