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Lamin a c h 110

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Lamin A/C (H-110) is a primary antibody that binds to the Lamin A/C protein. Lamin A/C is a structural protein found in the cell nucleus and is involved in maintaining the nuclear envelope and chromatin organization.

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Lab products found in correlation

α tubulin, by Santa Cruz Biotechnology (3 mentions) Dc protein kit, by Bio-Rad (2 mentions) Ubf f 9, by Santa Cruz Biotechnology (2 mentions) Polr1a rpa194 c 1, by Santa Cruz Biotechnology (2 mentions) Taf1c, by Abcam (2 mentions) Polr1b rpa135 h 15, by Santa Cruz Biotechnology (2 mentions) Rpa43 hpa022416, by Merck Group (2 mentions) Gapdh, by Cell Signaling Technology (2 mentions) Protease inhibitor, by Roche (2 mentions) Enhanced chemi luminescence (ecl), by PerkinElmer (2 mentions) Cd45 clone 30 f11, by BD (1 mentions) Pan actin ab 5, by Thermo Fisher Scientific (1 mentions) Laminb1 ab16048, by Abcam (1 mentions) Sulforaphane, by Merck Group (1 mentions) Aesculin, by Merck Group (1 mentions) Lipopolysaccharide lps escherichia coli o55 b5, by Merck Group (1 mentions) Cellobiose, by Merck Group (1 mentions) Goat anti rabbit igg tritc, by Merck Group (1 mentions) Fl 393, by Santa Cruz Biotechnology (1 mentions)

5 protocols using lamin a c h 110

1

Quantitative Western Blot Analysis

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Cells were lysed in RIPA lysis buffer (50 mM Tris-HCl [pH 7.5], 150 mM NaCl, 1% NP-40, 0.1% SDS, and 1% sodium deoxycholate) supplemented with protease inhibitors (Roche), sonicated, and centrifuged at 13,200 rpm for 15 min. Protein concentrations were measured using the Dc-Protein Kit (Bio-Rad). Equal amounts of protein were separated on SDS-PAGE, blotted, probed for target proteins, and detected using ECL (Perkin Elmer). The primary antibodies used for detection were UBF (F-9; Santa Cruz Biotechnology), RRN3 (ab112052; Abcam), TAF1C (ab134394; Abcam), POLR1A/RPA194 (C-1; Santa Cruz Biotechnology), POLR1B/RPA135 (H-15; Santa Cruz Biotechnology), RPA43 (HPA022416; Sigma-Aldrich), α-tubulin (10D8; Santa Cruz Biotechnology), lamin A/C (H-110; Santa Cruz Biotechnology), and GAPDH (14C10; Cell Signaling Technology). Horseradish peroxidase (HRP)-conjugated secondary antibodies were from DAKO or Santa Cruz Biotechnology. Protein densitometry analysis was conducted using ImageJ software, and the mean value normalized with loading control was used as final protein band quantification.
Wei T., Najmi S.M., Liu H., Peltonen K., Kucerova A., Schneider D.A, & Laiho M. (2018). Small-Molecule Targeting of RNA Polymerase I Activates a Conserved Transcription Elongation Checkpoint. Cell reports, 23(2), 404-414.
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2

Antibody Characterization for Cell Signaling

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The antibodies used were as follows: lamin A/C (H-110; Santa Cruz Biotechnology, Santa Cruz, CA); lamin B1 (ab16048; Abcam, Cambridge, UK); phosphorylated Stat5 (9314S), total Stat5 (9363S), phosphorylated Jak2 (3771S), total Erk (clone L34F12), phosphorylated Erk (4370P), total Akt (clone 40D4), total Jak2 (clone D2E12), phosphorylated Akt (4058S), total Stat1 (clone D1K9Y), and phosphorylated Stat1 (clones D4A7 and 58D6) (Cell Signaling Technology, Danvers, MA); pan-actin (Ab-5, 1:2500 dilution; ThermoFisher Scientific, Wayne, MI); and CD45 (clone 30-F11, 1:200 dilution; BD Biosciences, San Jose, CA). All antibodies were used at a 1:1000 dilution unless specified otherwise.
Kwan R., Brady G.F., Brzozowski M., Weerasinghe S.V., Martin H., Park M.J., Brunt M.J., Menon R.K., Tong X., Yin L., Stewart C.L, & Omary M.B. (2017). Hepatocyte-Specific Deletion of Mouse Lamin A/C Leads to Male-Selective Steatohepatitis. Cellular and Molecular Gastroenterology and Hepatology, 4(3), 365-383.
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3

Quantitative Western Blot Analysis

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Cells were lysed in RIPA lysis buffer (50 mM Tris-HCl [pH 7.5], 150 mM NaCl, 1% NP-40, 0.1% SDS, and 1% sodium deoxycholate) supplemented with protease inhibitors (Roche), sonicated, and centrifuged at 13,200 rpm for 15 min. Protein concentrations were measured using the Dc-Protein Kit (Bio-Rad). Equal amounts of protein were separated on SDS-PAGE, blotted, probed for target proteins, and detected using ECL (Perkin Elmer). The primary antibodies used for detection were UBF (F-9; Santa Cruz Biotechnology), RRN3 (ab112052; Abcam), TAF1C (ab134394; Abcam), POLR1A/RPA194 (C-1; Santa Cruz Biotechnology), POLR1B/RPA135 (H-15; Santa Cruz Biotechnology), RPA43 (HPA022416; Sigma-Aldrich), α-tubulin (10D8; Santa Cruz Biotechnology), lamin A/C (H-110; Santa Cruz Biotechnology), and GAPDH (14C10; Cell Signaling Technology). Horseradish peroxidase (HRP)-conjugated secondary antibodies were from DAKO or Santa Cruz Biotechnology. Protein densitometry analysis was conducted using ImageJ software, and the mean value normalized with loading control was used as final protein band quantification.
Wei T., Najmi S.M., Liu H., Peltonen K., Kucerova A., Schneider D.A, & Laiho M. (2018). Small-Molecule Targeting of RNA Polymerase I Activates a Conserved Transcription Elongation Checkpoint. Cell reports, 23(2), 404-414.
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4

Nrf2 Activation by Modified β-Glucosidase

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Aesculin, cellobiose, sulforaphane, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium-bromide (MTT), lipopolysaccharide (LPS; Escherichia coli O55:B5), and α-HA antibody (H3663) were obtained from Sigma-Aldrich (St. Louis, MO, USA). Water and methanol in high-performance liquid chromatography (HPLC)-grade were purchased from Burdick & Jackson (USA). Antibodies against Nrf2 (H-300), β-actin (C-4), and lamin A/C (H-110) were from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Modified β-glucosidase (N291T) from T. neapolitana (BglA) was purified using Ni-NTA affinity chromatography and heat treatment29 (link).
Kim K.H., Park H., Park H.J., Choi K.H., Sadikot R.T., Cha J, & Joo M. (2016). Glycosylation enables aesculin to activate Nrf2. Scientific Reports, 6, 29956.
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5

Immunofluorescence Staining of Lamin A/C, Tubulin, and p53

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The following antibodies were used: rabbit polyclonal Lamin A/C (H-110 Santa Cruz), mouse monoclonal α-Tubulin (Santa Cruz), rabbit polyclonal p53 (FL-393 Santa Cruz). Goat anti-rabbit IgG-TRITC (Sigma-Aldrich) was used as secondary antibody.
Borkosky S.S., Fassolari M., Campos-León K., Rossi A.H., Salgueiro M., Pascuale C.A., Martínez R.P., Gaston K., & Gay G. (2022). The guardian of the genome meets a viral master gene regulator at a biomolecular condensate.
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