aurkb (Cell Signaling Technology Inc)
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Cell Signaling Technology Inc
aurkb
Aurkb, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 143 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/aurkb/Aurora+B%2FAIM1+Antibody/pm41637535-69-23-25
Average 94 stars, based on 143 article reviews
Aurkb, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 143 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/aurkb/Aurora+B%2FAIM1+Antibody/pm41637535-69-23-25
Average 94 stars, based on 143 article reviews
aurkb - by Bioz Stars,
2026-09
94/100 stars
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other:Article Title: USP29 activation mediated by FUBP1 promotes AURKB stability and oncogenic functions in gastric cancer. Article Snippet: Primary antibodies for USP29 (Cat# AP2153c, Abcepta), SDS Page:Article Title: AURKB as a Therapeutic Target and Key Driver of Liver Cancer Growth and Metastasis. Article Snippet: Hepatocellular carcinoma (HCC) is a major cause of cancerrelated deaths worldwide.. Aurora kinase B (AURKB), a critical regulator of mitosis, has been implicated in cancer progression, though its precise role in HCC remains unclear.. In this study, AURKB expression was found to be significantly elevated in HCC tissues and cell lines compared to controls, as validated by GEPIA and ENCORI databases. Incubation:Article Title: AURKB as a Therapeutic Target and Key Driver of Liver Cancer Growth and Metastasis. Article Snippet: Hepatocellular carcinoma (HCC) is a major cause of cancerrelated deaths worldwide.. Aurora kinase B (AURKB), a critical regulator of mitosis, has been implicated in cancer progression, though its precise role in HCC remains unclear.. In this study, AURKB expression was found to be significantly elevated in HCC tissues and cell lines compared to controls, as validated by GEPIA and ENCORI databases. Article Title: Targeted Extracellular Vesicles Deliver Asiaticoside to Inhibit AURKB/DRP1-Mediated Mitochondrial Fission and Attenuate Hypertrophic Scar Formation. Article Snippet: Following denaturation, protein separation was achieved through SDS-PAGE (7.5% or 12.5% gels) and electrotransferred onto PVDF membranes (IPVH00010, Millipore). .. Membranes were incubated with primary antibodies specific to: DRP1 (4E11B11, Cell Signaling, 1:1000), phospho-DRP1 Ser616 (AF8470, Affinity, 1:1000), phospho-DRP1 Ser637 (DF2980, Affinity, 1:1000), Article Title: A novel combination of CDK4/6 and PI3K inhibitors exhibits highly synergistic activity and translational potential in Ewing sarcoma Article Snippet: .. Membranes were incubated with primary antibodies directed against AURKA (Cell Signaling Technology catalog No 3092S), Transduction:Article Title: Functional screening reveals genetic dependencies and diverging cell cycle control in atypical teratoid rhabdoid tumors Article Snippet: .. Primary antibodies used in this study for DigiWest were the following: β-actin (Sigma, A1978, AMBRA1 (Cell Signaling, 24907), ATM (Cell Signaling, 2873), ATR (Cell Signaling, 2790), AURKA (Cell Signaling, 4718), Article Title: Functional screening reveals genetic dependencies and diverging cell cycle control in atypical teratoid rhabdoid tumors. Article Snippet: .. Primary antibodies used in this study for DigiWest were the following: β-actin (Sigma, A1978, AMBRA1 (Cell Signaling, 24907), ATM (Cell Signaling, 2873), ATR (Cell Signaling, 2790), AURKA (Cell Signaling, 4718), Western Blot:Article Title: Functional screening reveals genetic dependencies and diverging cell cycle control in atypical teratoid rhabdoid tumors. Article Snippet: .. Primary antibodies used in this study for western blotting were the following: CDK4 (abcam, ab199728), CDK6 (Cell Signaling, 13331), cyclin D1 (Cell Signaling, 55506), cyclin D2 (Cell Signaling, 3741), cyclin D3 (Cell Signaling, 2936), cyclin E1 (Cell Signaling, 20808), cyclin E2 (Cell Signaling, 4132), GAPDH (Cell Signaling 2118), Vinculin (Cell Signaling, 13901), β-tubulin (Cell Signaling, 86298), AMBRA1 (Cell Signaling, 24907), AURKA (Cell Signaling, 14475), Article Title: Functional screening reveals genetic dependencies and diverging cell cycle control in atypical teratoid rhabdoid tumors Article Snippet: .. Primary antibodies used in this study for western blotting were the following: CDK4 (abcam, ab199728), CDK6 (Cell Signaling, 13331), cyclin D1 (Cell Signaling, 55506), cyclin D2 (Cell Signaling, 3741), cyclin D3 (Cell Signaling, 2936), cyclin E1 (Cell Signaling, 20808), cyclin E2 (Cell Signaling, 4132), GAPDH (Cell Signaling 2118), Vinculin (Cell Signaling, 13901), β-tubulin (Cell Signaling, 86298), AMBRA1 (Cell Signaling, 24907), AURKA (Cell Signaling, 14475), |
![Dissolution of CIZ1–Xi assemblies in mitosis. ( A ) Model of CIZ1–RNA assemblies surrounding and protecting the modification status of underlying chromatin [ , ]. ( B ) Illustrative immunofluorescence images of female murine D3T3 cells stained for CIZ1 via N-terminal epitopes (CIZ1-N, red, detected with pAb 1794), revealing large protein assemblies at the inactive X chromosome (white arrows) that are not detected in mitosis. DNA is shown in blue, bar is 5 µm. ( C ) Diagram illustrating loss in mitosis and the early G1 phase window during which reformation of CIZ1–Xi assemblies takes place, determined previously using cells that were synchronized in G1 phase by release from arrest with nocodazole . ( D ) Map showing conserved putative <t>AURKB</t> phosphorylation sites between murine and human CIZ1 (circles) displayed on full-length murine CIZ1 ( NP_082688.1 .) The location of epitopes of CIZ1 antibodies used throughout is shown above. Conserved prion-like domains (PLD1 and PLD2) are in red , zinc fingers 1–3 in cyan (ZnF_C2H2 SM00355, ZF_C2H2 sd00020, and ZF_C2H2 sd00020), acidic region (Ac) in yellow, matrin-3 homology domain (MH3) in orange (ZnF_U1, smart00451), and h37/m38 amino-acid C-terminal tail in blue. The sequence context and identity of three conserved AURKB phosphorylation sites in the extreme C-terminus are shown. ( E ) Frequency of cells with CIZ1–Xi assemblies (red) or nucleus-wide SAFA (blue) in cells passing through the stages of mitosis indicated, for D3T3 cells and female primary embryonic fibroblasts (PEFs at p3), in the presence and absence of the AURKB kinase inhibitor barasertib at 0.1 and 1 µM. Results show the average of 3–4 independent replicates within one experiment for each line, with SEM. n indicates the number of nuclei inspected (PEF grey, 3T3 black). Statistical analysis of CIZ1–Xi frequency in anaphase cells shows one-way ANOVA with Tukey post hoc test within each cell type, where * <.05, ** <.01, *** <.001. Below, example immunofluorescence images of D3T3 cells through mitosis, with and without 1 µM barasertib. Cells were stained for the N-terminal domains of CIZ1 (CIZ1-N, red) and SAFA (green). DNA is shown in blue, bar is 5 microns. ( F ) Upper histogram shows the proportion of cells with CIZ1-marked Xi in cycling populations of female D3T3 cells after the indicated times exposed to 300 nM Okadaic acid, visualized via CIZ1-N (red). Lower, histograms show the effect of the indicated concentrations of tautomycin for 15 h, stained for CIZ1-N or the ‘tail’ epitope in the C-terminal end of CIZ1 (CIZ1-C, rabbit pAb). Comparison of technical replicates is by t-test, where * <.05, ** <.01, *** <.001. Error bars show SEM. Below, example images showing H3K27me3-marked Xi chromatin in cells stained for CIZ1-N or CIZ1-C at 15 h with or without tautomycin. Bar is 5 microns.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_2363/pmc12862363/pmc12862363__gkag018fig1.jpg)
![Interaction between CIZ1 dimer and RNA is regulated by AURKB sites in the C-terminal tail. ( A ) Schematic of h/m CIZ1 showing conserved domains, in yellow (acidic domain), orange (MH3 dimerization domain), and blue (unstructured tail h37/m38 C-terminal amino acids). Below, human C-terminal (C179) fragments, and derived mutants used as bait fragments in interaction studies, including C179 Δtail and phosphomimic C179 DDD . Below, C-terminal fragment encompassing the Zn finger motifs used for modelling (green, C305). Left, SDS–PAGE gels showing purified protein preparations stained with Coomassie Blue, or probed with anti-CIZ1 mAb 87, which recognizes all three proteins, or anti-CIZ1 tail pAb, which recognizes an epitope deleted in C179 Δtail and mutated in C179 DDD . ( B ) SEC-MALLS, showing normalized UV absorbance at 280 nm and molar mass (dotted line) for human CIZ1-C179 (blue), and human CIZ1-C179 Δtail (orange). ( C ) SEC-MALLS chromatogram showing normalized UV absorbance at 280 nm and molar mass (dotted line) for equivalent murine fragment C181 (black), and derived deletion mutant lacking the matrin 3 homology domain (C181 ΔMH3 , yellow). ( D ) Summary of measured molecular masses, indicating that the C-terminal fragment forms a stable dimer that is dependent on the MH3 domain but not the tail region. ( E ) AlphaFold dimer structure predictions of MH3 domain, showing human CIZ1 aa 779–838 uniprot Q9ULV3-1 (blue) and murine CIZ1 aa 725–785 uniprot Q8VEH2 (cyan). The domain forms a tight dimer with monomer–monomer interactions involving main chain hydrogen bonding between β-strands of the two MH3-type Zn finger motifs. ( F ) Example electrophoretic mobility shift assays (EMSA) showing the effect of C179, C179 Δtail , and C179 DDD on the mobility of digoxygenin (DIG)-labelled Xist repeat E RNA probe (left, 0.66 nM) or GAPDH RNA (right, 0.65 nM). Below, immunoblots of EMSA membranes using CIZ1 anti-MH3 domain antibody. Above, murine Xist structure and the derived Xist repeat E RNA probe used in EMSAs. Right, quantification of binding based on the fraction of shifted probe, derived from three replicate experiments (see also ). Graphs show means ± SEM. ( G ) AlphaFold-Multimer [ , ] structure prediction of human C-terminal aa 592–898 (hC306), showing the highest-ranking prediction, in which the acidic domains (yellow) are exposed and the unstructured tails (blue) extend from the core. ( H ) Model, depicting CIZ1 homodimers interacting with chromosome-associated RNAs via its C-terminal tails, with N-terminal PLD domains available for association with other proteins or other RNAs (left). Right, shows AURKB-mediated phosphorylation driving release from chromosome-associated RNA. In vitro in interphase this results in PLD-driven CIZ1 aggregation.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_2363/pmc12862363/pmc12862363__gkag018fig6.jpg)