Anti lamin b1

Manufactured by Thermo Fisher Scientific

Sourced in United States

Anti-lamin B1 is a laboratory product used for the detection and analysis of lamin B1, a structural protein found in the cell nucleus. It is intended for research use only.

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Lab products found in correlation

Anti β actin, by Merck Group (2 mentions) Sc 47778, by Santa Cruz Biotechnology (1 mentions) Anti cd36, by Santa Cruz Biotechnology (1 mentions) Ab52866, by Abcam (1 mentions) Anti α tubulin, by Abcam (1 mentions) Anti β actin, by Santa Cruz Biotechnology (1 mentions) Bca protein assay kit, by Thermo Fisher Scientific (1 mentions) Protease inhibitor cocktail, by Roche (1 mentions) Enhanced ripa lysis buffer, by Boster Bio (1 mentions) Anti ampk 5832s, by Cell Signaling Technology (1 mentions) Anti nrf2 16396 1 ap, by Proteintech (1 mentions) Horseradish peroxidase hrp conjugated secondary antibody, by GE Healthcare (1 mentions) Azure imager c300, by Azure Biosystems (1 mentions) Nitrocellulose membrane, by Thermo Fisher Scientific (1 mentions) Radioimmunoprecipitation assay buffer, by Merck Group (1 mentions) Anti collagen 1, by Thermo Fisher Scientific (1 mentions) P akt, by Santa Cruz Biotechnology (1 mentions) Anti erα, by Thermo Fisher Scientific (1 mentions) Protease and phosphatase inhibitor cocktail, by Merck Group (1 mentions) 4 to 12 bis tris protein gradient gels, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Lamin B1 (18 citations) Anti-VprBP and anti-Lamin B1 antibodies (3 citations)

6 protocols using anti lamin b1

Immunoblot Analysis of AMPK and Nrf2 Signaling

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The ipsilateral striatum of the mouse brain and cultured cells were homogenized in enhanced RIPA lysis buffer (AR0101, Boster, China) and 10% protease inhibitor cocktail (04693132001, Roche, USA) by sonication. The protein concentration was determined with the BCA protein assay kit (23221, Thermo). The proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred onto polyvinylidene difluoride membranes (1620177, Bio-Rad, USA), which were blocked in 5% non-fat milk before being incubated with primary antibodies overnight at 4°C. The primary antibodies were anti-LRRC8A (sc-517113, Santa Cruz, USA), anti-AMPK (5832S, Cell Signaling Technology, USA), anti-phospho-AMPK (Thr172; 50081S, Cell Signaling Technology, USA), anti-Nrf2 (16396-1-AP, Proteintech, USA), anti-lamin B1 (MA1-06103, Invitrogen), anti-CD36 (sc-7309, Santa Cruz), anti-α-tubulin (ab52866, Abcam), and anti-β-actin (sc-47778, Santa Cruz). The membranes were washed with TBST buffer and then incubated with IgG HRP-conjugated secondary antibodies (anti-mouse, 7076S, Cell Signaling Technology, or anti-rabbit, 7074S, Cell Signaling Technology) for 1h at room temperature. Immunoreactive bands were visualized by using chemiluminescent HRP substrate (90719, Millipore, USA). The bands were scanned and analyzed with ImageJ software.

Liu J., Shen D., Wei C., Wu W., Luo Z., Hu L., Xiao Z., Hu T., Sun Q., Wang X., Ding Y., Liu M., Pang M., Gai K., Ma Y., Tian Y., Yu Y., Wang P., Guan Y., Xu M., Yang F, & Li Q. (2022). Inhibition of the LRRC8A channel promotes microglia/macrophage phagocytosis and improves outcomes after intracerebral hemorrhagic stroke. iScience, 25(12), 105527.

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Western Blot Analysis of Statin and E2 Effects

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Cells were harvested after treatment with simvastatin (0.001, 0.01, 0.1, and 1 μM) and E₂ (10 nM), alone or in combination, at the specified time points. Cells were lysed in a lysis buffer (radioimmunoprecipitation assay buffer, Sigma-Aldrich) containing a protease and phosphatase inhibitor cocktail (Sigma-Aldrich). An equal amount of protein lysates was resolved using 4 to 12% Bis-Tris protein gradient gels (Thermo Fisher Scientific) and transferred to a nitrocellulose membrane (Thermo Fisher Scientific). Membranes were blocked using 5% nonfat milk in Tris-buffered saline with 0.1% Tween-20 (TBST, Thermo Fisher Scientific) for 1 h at room temperature and incubated with PCNA (CST, #13110), anti- ER-α (Invitrogen, PA5–16440), pERK1/2 (CST, #4695S), ERK1/2 (CST, #4370), pAKT (Santa Cruz; sc-7985), AKT (Santa Cruz; sc-8312), anti-collagen 1 (Thermo Fisher Scientific, PA5–29569), anti-β-actin (Sigma, A3854), anti-Na,K-ATPase (CST, 23565), or anti-lamin B1 (Invitrogen, PA5–19468) at 4 °C overnight on a rocker. Membranes were washed with TBST, co-incubated with appropriate horseradish peroxidase (HRP)-conjugated secondary antibodies (GE Healthcare, Chicago, IL) for 1 h at room temperature and visualized using an Azure Imager c300 (Azure Biosystems, Dublin, CA). Band signals were quantified using the NIH ImageJ software (version 1.52r, USA).

Afrin S., El Sabeh M., Islam M.S., Miyashita-Ishiwata M., Malik M., Catherino W.H., Akimzhanov A.M., Boehning D., Yang Q., Al-Hendy A., Segars J.H, & Borahay M.A. (2021). Simvastatin modulates estrogen signaling in uterine leiomyoma via regulating receptor palmitoylation, trafficking and degradation. Pharmacological research, 172, 105856.

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Immunoblotting of Cellular Proteins

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The whole-cell lysates were resolve on 10% denaturing SDS-PAGE and blotted onto a nitrocellulose membrane (Bio-Rad). Ponceau S staining was performed to con rm equal protein loading and transfer.
The membrane was blocked with 5% nonfat dry milk (NFDM) in PBS having 0.1% Tween-20 (PSBT) for 2 h. Membranes were then incubated with primary antibody for anti-Nrf-2 (Santa Cruz Biotechnology, 1:1000 dilution), anti-APE1 (Biogenuix, 1:1000 dilution), anti-LaminB1 (Invitrogen, 1:750 dilution) and anti-β-actin (Invitrogen, 1:5000 dilution) in 5% NFDM-PSBT for overnight at 4°C. After three washes with PBST membrane was further incubated with respective horseradish peroxidase (HRP) conjugated antimouse/rabbit IgG secondary antibody (GeNei™, 1:5000) in 5% NFDM-PSBT. Peroxidase activity was captured using enhanced chemiluminescence reagent of Bio-Rad, and images were visualized using Bio-Rad Chemi Doc™ MP system and densitometric analysis was done using Image Lab™ software of Bio-Rad version 5.2.

Gupta K.B., Mantha A.K., & Dhiman M. (2021). Curcumin Resuscitate Gliadin Induced Oxidative Damage And Altered Cellular Responses In Human Intestinal Cells Via Cross-Talk Between The Transcription Factor Nrf-2 And Multifunctional Protein APE1.

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Western Blot Analysis of DNA Repair Proteins

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Cells were collected by trypsinization and lysed in RIPA lysis buffer (150 mM NaCl, 1.0% IGEPAL CA-630, 0.5% sodium deoxycholate, 0.1% SDS, 50 mM Tris base, pH 8.0). Phosphatase and protease inhibitors (Gold Biotechnology) were added freshly to the lysis buffer. Following gel electrophoresis and transfer of cell extracts onto nitrocellulose, membranes were incubated for 1 hr or overnight in blocking buffer (5% milk in TBS + 0.1% tween). Membranes were subsequently incubated with primary antibodies diluted in antibody buffer (3% BSA in TBS + 0.1% tween) for 2 hrs at room temperature or overnight at 4°C. Detection was achieved using appropriate horseradish peroxidase (HRP)-conjugated secondary antibodies. Anti-ZRANB3 (1:5,000, Bethyl Laboratories), anti-SMARCAL1 (1:1,000, Santa Cruz Biotechnology), anti-BRCA1 (1:500, Bethyl Laboratories), anti-BRCA2 (1:1,000, Bethyl Laboratories), anti-vinculin (1:100,000, Sigma-Aldrich), anti-β-actin (1:100,000, Novus Biologicals), anti-GAPDH (1:5,000, Novus Biologicals), anti-HLTF (1:2,000, Abcam), anti-LAMIN B1 (Thermo Fisher Scientific), anti-FANCD2 (1:1,000, Novus Biologicals), anti-PCNA (1:100,000, Abcam), anti-NBS1 (GeneTex), anti-MRE11 (Cell Signaling Technology), anti-RPA2 (Bethyl Laboratories) antibodies were used in western blot experiments.

Taglialatela A., Alvarez S., Leuzzi G., Sannino V., Ranjha L., Huang J.W., Madubata C., Anand R., Levy B., Rabadan R., Cejka P., Costanzo V, & Ciccia A. (2017). Restoration of replication fork stability in BRCA1- and BRCA2-deficient cells by inactivation of SNF2-family fork remodelers. Molecular cell, 68(2), 414-430.e8.

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Western Blot Analysis of Cellular Proteins

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Cells were harvested, washed twice with cold PBS, and lysed using a lysis buffer consisting of 25 mM Tris HCl (pH 8.0), 1 mM EDTA, 150 mM NaCl, and 0.5% NP40. After a 10-min incubation on ice, the cell lysate was centrifuged at 13,000 rpm at 4°C for 10 min. Equal amounts of protein from extracts were separated using SDS-PAGE and transferred to nitrocellulose membranes. The blots were blocked with 5% skim milk and incubated with primary antibodies, which were diluted in the range of 1:1,000 to 1:5,000. After washing with TBS-T (5 mM Tris HCl [pH 7.4], 150 mM NaCl, and 0.01% Tween 20), secondary antibodies were added at a dilution of 1:10,000 for a 1-h incubation at room temperature. Protein signals were detected using a western blot detection kit (AbFrontier, Korea). The following primary antibodies were used in this study: anti-β-actin (Merck Millipore, USA), anti-α-tubulin (AbFrontier), anti-menin (Bethyl Laboratories, USA), anti-cleaved-PARP (Cell Signaling Technology, USA), anti-AR (Santa Cruz Biotechnology, USA), and anti-Lamin B1 (Thermo Fisher Scientific).

Kim T., Jeong K., Kim E., Yoon K., Choi J., Park J.H., Kim J.H., Kim H.S., Youn H.D, & Cho E.J. (2022). Menin Enhances Androgen Receptor-Independent Proliferation and Migration of Prostate Cancer Cells. Molecules and Cells, 45(4), 202-215.

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Analyzing Nuclear and Cytoplasmic IDO1 Signaling

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Nuclear and cytoplasmic extracts from Ido1^−/− pDCs, transfected with WT and ITIM‐mutated Ido1 mRNA and incubated for 48 hr at 37°C, were prepared according the manufacturer's protocol for the TransAM Flexi NF‐κB Family Kit (Active Motif). Analysis of p52 and RelB expression was performed on normalized samples of pDCs using rabbit polyclonal anti‐p100/p52 (Cell Signaling Technology, MA, USA), anti‐RelB (Santa Cruz Biotechnology) antibodies. Anti–β‐tubulin and anti‐Lamin B1 (Thermo Fisher Scientific, Massachusetts, USA) were used as normalizers of the cytoplasmic and nuclear extracts respectively. TGF‐β production in culture supernatants from those cells was measured by means of TGF beta 1 Emax Immuno Assay System (Promega, Madison, WI 53711 USA).

Albini E., Rosini V., Gargaro M., Mondanelli G., Belladonna M.L., Pallotta M.T., Volpi C., Fallarino F., Macchiarulo A., Antognelli C., Bianchi R., Vacca C., Puccetti P., Grohmann U, & Orabona C. (2016). Distinct roles of immunoreceptor tyrosine‐based motifs in immunosuppressive indoleamine 2,3‐dioxygenase 1. Journal of Cellular and Molecular Medicine, 21(1), 165-176.

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