Anti lamin b c 20

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Anti-Lamin B (C-20) is a primary antibody that recognizes the C-terminus of Lamin B, a structural protein found in the cell nucleus. It is used for the detection and analysis of Lamin B in various cell and tissue samples.

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Close spelling variants of this product

Goat anti–lamin B (C-20; Lamin B (C-20) Anti-Lamin B Lamin B

5 protocols using anti lamin b c 20

Immunoblotting and Protein Isolation Protocols

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The immunoblotting, isolation of nuclear protein fractions, immunoprecipitation and mice protein extraction procedures were performed as previously described [22 (link)].
The primary antibodies used in this work are as follows: human anti-p53 (clone BP53-12, Novocastra Laboratories, Newcastle Upon Tyne, UK), mouse anti-p53 (clone 1C12, Cell Signaling Technology, Beverly, MA, USA), anti-RPL11 (clone 3A4A7, Invitrogen, Carlsbad, UK), anti-PARP-1 (Cell Signaling Technology), anti-RPS6 (clone C-8, Santa Cruz Biotechnology, CA, USA), anti-RPS14 (clone H-130, Santa Cruz Biotechnology), anti-Mdm2 (clone SMP14 and clone H-221, Santa Cruz Biotechnology), anti-Slug (clone C19G7, Cell Signaling Technology), anti-E-cadherin (clone 24E10, Cell Signaling Technology), anti-c-Myc (clone N-262, Santa Cruz Biotechnology), anti-β-actin (clone AC-74, Sigma-Aldrich), and anti-Lamin B (C-20, Santa Cruz Biotechnology). Horseradish peroxidase-conjugated secondary antibodies were from GE-Healthcare (Milan, Italy).

Brighenti E., Giannone F.A., Fornari F., Onofrillo C., Govoni M., Montanaro L., Treré D, & Derenzini M. (2016). Therapeutic dosages of aspirin counteract the IL-6 induced pro-tumorigenic effects by slowing down the ribosome biogenesis rate. Oncotarget, 7(39), 63226-63241.

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Nuclear and Cytosolic Protein Extraction

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Nuclear and cytosolic extracts were collected with the NE-PER nuclear and cytoplasmic extraction reagents (Pierce, Rockford, IL, USA). For Western blotting, protein bands were probed with the antibodies to anti-Phospho NFκB p65 (Ser536, 1:1,000; Cell Signaling Technology, Danvers, MA, USA), anti-IkBα (sc-1643, 1:500; Santa Cruz Biotechnology, Dallas, TX, USA) or anti-lamin B (C-20, 1:200; Santa Cruz Biotechnology) overnight at 4℃. HRP-conjugated rabbit anti-mouse immunoglobulin G (IgG) (1:5,000; Santa Cruz Biotechnology) were used for secondary antibodies. The protein bands were visualized by luminescence (LAS 3000, Fujifilm). Densitometric analyses were performed by using the Multi Gauge V3.0 software (Fujifilm). Expression levels were normalized to an endogenous control β-actin. All data represent three experiments.

Choi D.I., Park J.H., Choi J.Y., Piao M., Suh M.S., Lee J.B., Yun S.J, & Lee S.C. (2020). Keratinocytes-Derived Reactive Oxygen Species Play an Active Role to Induce Type 2 Inflammation of the Skin: A Pathogenic Role of Reactive Oxygen Species at the Early Phase of Atopic Dermatitis. Annals of Dermatology, 33(1), 26-36.

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Immunoblotting and Co-immunoprecipitation Protocol

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Cells were lysed in NP-40 buffer in the presence of protease inhibitor cocktail (Complete Mini, Roche Diagnostics). The following antibodies were used for immunoblotting and co-immuno-precipitation: Anti PU.1 (H-135, Santa Cruz), anti Id1 (C-20, Santa Cruz), anti Id2 (C-20, Santa Cruz), anti Id3 (C-20, Santa Cruz), anti E2A (N-649, Santa Cruz), anti Lamin B (C-20, Santa Cruz), anti Gfi1 (R&D systems) and anti β-Actin (Ac-15, Sigma-aldrich).

Fraszczak J., Helness A., Chen R., Vadnais C., Robert F., Khandanpour C, & Möröy T. (2016). Threshold Levels of Gfi1 Maintain E2A Activity for B Cell Commitment via Repression of Id1. PLoS ONE, 11(7), e0160344.

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Immunoblotting and Nuclear Protein Fractionation

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The immunoblotting, isolation of nuclear protein fractions and immunoprecipitation procedures were performed as previously described.^{11 (link)} Antibodies used in this work were as follows: anti-p53 (clone BP53-12, Novocastra), anti-β-actin (clone AC-74, Sigma-Aldrich), anti-MDM2 (clone SMP14 and clone H-221, Santa Cruz Biotechnology), anti-L11 (clone 3A4A7, Invitrogen), anti-SLUG (clone L40C6, Cell Signaling Technology), anti-E-cadherin (clone 32A8, Cell Signaling Technology), anti-c-Myc (Cell Signaling Technology) and anti-Lamin B (C-20, Santa Cruz Biotechnology).

Brighenti E., Calabrese C., Liguori G., Giannone F.A., Trerè D., Montanaro L, & Derenzini M. (2014). Interleukin 6 downregulates p53 expression and activity by stimulating ribosome biogenesis: a new pathway connecting inflammation to cancer. Oncogene, 33(35), 4396-4406.

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Immunoblot Analysis of Melanoma Cell Proteins

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Whole-cell lysates of melanoma cells and nuclear-enriched cell lysates were prepared and immunoblot analysis was performed as described previously^{22 (link)}. Fifteen μg protein of whole-cell lysate or 5 μg of nuclear-enriched lysates were used for the sodium dodecyl sulphate–polyacrylamide gel electrophoresis. The following primary antibodies were used: anti-Lamin-B (C-20, Santa Cruz Biotechnology, 1:250), anti-p53 (DO-I, Santa Cruz Technology), anti-Actin (D6A8, CST, 1:1000), anti-p73 (GC-15, BD Biosciences, 1:250; H-79, Santa Cruz, 1:250; 5B429, Novus Biologicals, 1:500), anti- pH2AX (JBW301, Abcam, 1:500), anti-Mdm2 (Abcam, 1: 100), anti-p21 (CST, 1:2000), and anti-HA (Santa Cruz, 1:250).

Makino E., Gutmann V., Kosnopfel C., Niessner H., Forschner A., Garbe C., Sinnberg T, & Schittek B. (2018). Melanoma cells resistant towards MAPK inhibitors exhibit reduced TAp73 expression mediating enhanced sensitivity to platinum-based drugs. Cell Death & Disease, 9(9), 930.

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