antibodies against lamin b1  (R&D Systems)

Journal: Stem Cells International

Article Title: Exosomes Derived From Mesenchymal Stem Cells Regulating Myotube Cell Atrophy via NF‐κB Signaling Pathway

doi: 10.1155/sci/3606738

Figure Lengend Snippet: Effects of BMSC‐Exos on the expression of MyoD in TNF‑α‑treated C2C12 myotubes. Western blot analysis was performed to detect the protein expression levels of MyoD in nuclear fractions of C2C12 myotubes. α‐Tubulin (cytosolic marker) was undetectable in the nuclear fractions, confirming the high purity of the isolated nuclear components, while Lamin B1 was used as the nuclear loading control. The relative expression of MyoD was normalized to Lamin B1. The data are presented as the means ± standard deviations of three independent experiments. ∗∗ p < 0.01 vs. untreated cells; # p < 0.05 vs. TNF‐α‐treated cells; △ p < 0.05 vs. BMSC‐Exos‐treated cells.

Article Snippet: Western blotting was used to detect the expression levels of Atrogin‐1 (1∶1000, Bioss, bsm‐54451R), MuRF‐1 (1∶1000, Affinity, DF7187), MyoD (1∶1000, Abmart, TA7733S), GAPDH (1∶50000, Proteintech, 60004‐1‐lg), α‐Tubulin (1∶10000, Proteintech, 66031‐1‐lg), and Lamin B1 (1∶10000, Bioss, bs‐55118R), as well as NF‐κB signaling pathway‐related proteins IκB‐α (1∶1000, ImmunoWay, YT2419), p‐IκB‐α (1∶1000, Abmart, TP56280F), NF‐κB p65 (1∶1000, ImmunoWay, YT3108), and β‐actin (1∶5000, BOSTER, BM3873) in cells.

Techniques: Expressing, Western Blot, Marker, Isolation, Control

Journal: Stem Cells International

Article Title: Exosomes Derived From Mesenchymal Stem Cells Regulating Myotube Cell Atrophy via NF‐κB Signaling Pathway

doi: 10.1155/sci/3606738

Figure Lengend Snippet: Western blot analysis was performed to detect the protein expression levels of NF‐κB p65 in nuclear fractions of C2C12 myotubes. α‐Tubulin (cytosolic marker) was undetectable in the nuclear fractions, confirming the high purity of the isolated nuclear components, while Lamin B1 was used as the nuclear loading control. The relative expression of NF‐κB p65 was normalized to Lamin B1. The data are presented as the means ± standard deviations of three independent experiments. ∗∗∗ p < 0.0001 vs. untreated cells; ## p < 0.01 vs. TNF‐α treated cells; △△ p < 0.01 vs. BMSC‐Exos‐treated cells.

Article Snippet: Western blotting was used to detect the expression levels of Atrogin‐1 (1∶1000, Bioss, bsm‐54451R), MuRF‐1 (1∶1000, Affinity, DF7187), MyoD (1∶1000, Abmart, TA7733S), GAPDH (1∶50000, Proteintech, 60004‐1‐lg), α‐Tubulin (1∶10000, Proteintech, 66031‐1‐lg), and Lamin B1 (1∶10000, Bioss, bs‐55118R), as well as NF‐κB signaling pathway‐related proteins IκB‐α (1∶1000, ImmunoWay, YT2419), p‐IκB‐α (1∶1000, Abmart, TP56280F), NF‐κB p65 (1∶1000, ImmunoWay, YT3108), and β‐actin (1∶5000, BOSTER, BM3873) in cells.

Techniques: Western Blot, Expressing, Marker, Isolation, Control

Journal: bioRxiv

Article Title: Selective autophagy of whole micronuclei suppresses chromosomal instability

doi: 10.64898/2026.04.03.716211

Figure Lengend Snippet: a, Montage showing BAF dissociation from the MN membrane before acidification and timecourse of BAF (cortical/inner) signal for MN populations with different fates (scale bar = 1μm). b, Fate of MN with sustained (≥ 3 consecutive frames) BAF dissociation (n≥50MN per experiment, 3 separate experiments). c, Fate of MN with sustained (≥ 3 consecutive frames) Lamin B1 dissociation (n≥50MN per experiment, 3 separate experiments). d, LC3 recruitment on MN after sustained BAF dissociation (n=22 MN from 2 individual experiments). e, Relation between initial import capacity and final BAF localization based on MN fate. f, Acidification rate of MN in cells treated with the MKLP2 inhibitor, paprotrain, from nocodazole washout (pre-anaphase) or in the next interphase (n≥100MN per experiment, 4 separate experiments). g, Acidification rate of MN from cells with or without Lamin B1 overexpression(n≥100MN per experiment, 4 separate experiments). h, Lamin B1 levels on lagging derived MN in cells treated with or without paprotrain from nocodazole washout (n=50 individual MN, 2 separate experiments). i, Acidification rate of MN in cells treated with the VRK1 inhibitor, VRK1-IN-1, from nocodazole washout (pre-anaphase) or in the next interphase (n≥100MN per experiment, 4 separate experiments). j, Timecourse of BAF localization in acidified MN in basal conditions or following VRK1-IN-1 treatment from nocodazole washout (n between 14 and 21 MN from n=2 experiments). k, Holotomography montage of adjacent MN (white arrow=acidification-fated; green arrow=stable) several hours (top) and shortly (bottom) before acidification, showing rapid changes in the morphology of the acidification-fated MN shortly before acidification (scale bar = 1μm). l, CLEM experiment showing deformed but intact NE of autophagy targeted MN (green = LC3 positive autophagosomal membrane; orange = intact NE) (scale bar = 2μm for immunofluorescence image and scale bar = 500nm for EM image). Data are shown as mean ± sem, and were analysed using a one-way ANOVA (b, g), unpaired t-test (c, h), one-sample t-test (d), two-way ANOVA (f, i) (ns = non-significant, * = p ≤ 0.05, ** = p ≤ 0.01, *** = p ≤ 0.001, **** = p ≤ 0.0001)

Article Snippet: To investigate the impact of suppression of Aurora B midzone localisation on MN fates and Lamin B1 levels Paprotrain (10μM, MedChemExpress, HY-101298) was added from nocodazole washout or after mitotic exit.

Techniques: Membrane, Over Expression, Derivative Assay, Immunofluorescence

Journal: bioRxiv

Article Title: ARID2 loss destabilizes PBAF and drives colorectal cancer

doi: 10.64898/2026.04.01.715786

Figure Lengend Snippet: A) Immunoblot analysis of SWI/SNF core and PBAF components in HT-29 and SW620 cells following shRNA-mediated ARID2 knockdown (SH3, SH4) compared to non-targeting (NT) controls. Lamin B1 was utilized as loading control. *, non-specific band. B) Visualization of PBAF subunit levels determined via immunofluorescence in the same cells as Panel A. Cells were probed for endogenous PBAF and Pan-BAF (ATPase) components (Alexa Fluor 568, red) and counterstained with DAPI (blue) to stain nuclei. Scale bar 5µm.

Article Snippet: Primary antibodies used for pulldown, immunoblotting and immunofluorescence (IF) were ARID2 (1:5000, Cat no. 82342, Cell Signaling Technology, Danvers, MA, USA), BRD7 (1:5000, Cat no. A302-304A, Bethyl Laboratories, Montgomery, TX, USA), PBRM1 (1:5000, Cat no. A301-591A, Bethyl Laboratories), PHF10 (1:5000, Cat no. PA5-30678, Invitrogen, Carlsbad, CA, USA), BAF155 (1:5000, Cat no. sc-32763, Santa Cruz Biotechnology, Dallas, TX, USA), BRG1 (1:5000, Cat no. sc-17796, Santa Cruz Biotechnology), SMARCD1 (1:5000, Cat no. HPA004101, Sigma-Aldrich), ARID1A (1:5000, Cat no. A19570, ABclonal Technology, Woburn, MA, USA), SS18 (1:5000, Cat no. A6990, ABclonal Technology), Lamin B1(1:5000, Cat no. 12586, Cell Signalling Technology), GAPDH (1:10000, Cat no.MAB932Hu22, Cloud-Clone Corp, Katy, TX, USA), Anti-Halo (1:10000; Cat no. G9211; Lot no. 0000348664; Promega, Madison, WI, USA), Anti-Flag (1: 10000; Cat no. F1804; Lot No. SLBW5142; Sigma-Aldrich).

Techniques: Western Blot, shRNA, Knockdown, Control, Immunofluorescence, Staining