The following antibodies were used for western blot analysis: anti-MDC1 rabbit polyclonal antibody (R2, manufactured in our lab) [1 (link)], anti-KPNA2 mouse monoclonal antibody (sc-55538, Santa cruz, Dallas, TX, USA), anti-HA mouse monoclonal antibody (sc-7392, Santa Cruz), anti-GFP mouse monoclonal antibody (sc-5286, Santa Cruz), anti-Histone3 rabbit polyclonal antibody (ab1791, Abcam, Cambridge, UK), and anti-α-Tubulin mouse monoclonal antibody (sc-5286, Santa Cruz). For immunoprecipitation assay, anti-HA rabbit polyclonal antibody (F-7, Santa Cruz), anti-GFP mouse monoclonal antibody (sc-5286, Santa Cruz), anti-MDC1 rabbit polyclonal antibody (R2, manufactured in our lab), and anti-KPNA2 mouse monoclonal antibody (sc-55538, Santa cruz) were used. The following antibodies were used for immunofluorescence staining: anti-MDC1 rabbit polyclonal antibody (R2), anti-HA mouse monoclonal antibody (sc-7392, Santa Cruz), anti-RNF8 goat polyclonal antibody (ab15850, Abcam), anti-53BP1 rabbit polyclonal antibody (sc-22760, Santa Cruz), anti-BRCA1 mouse monoclonal antibody (sc-6954, Santa cruz), anti-γH2AX mouse monoclonal antibody (05-636-1, Millipore, Burlington, MA, USA), and anti-RNF168 rabbit polyclonal antibody (ABE367, Millipore).
Sc 55538
Manufactured by Santa Cruz Biotechnology
Sourced in United States
Sc-55538 is a laboratory equipment product offered by Santa Cruz Biotechnology. It is designed for specific technical functions, but a detailed unbiased description cannot be provided while maintaining conciseness.
Automatically generated - may contain errors
3 protocols using sc 55538
1
Western Blot and Immunoprecipitation Antibodies
2
Immunohistochemical Analysis of KPNA2 in Bone Tissue
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All bone tissue samples were fixed in formalin (pH 7.4) and decalcified using standard procedures with 16–20 h incubation in 5% aqueous hydrochloric acid (HCl). Immunohistochemistry was performed on 4-μm-thick paraffin-embedded whole tissue sections with standard techniques. Briefly, following deparaffinization and rehydration, charged slides with 4-μm-thick sections of tissue were treated with 3% hydrogen peroxide to eliminate endogenous peroxidase activity and then processed for antigen retrieval with 10 mm citrate buffer (pH 6.0) for 15 min at 95 °C, followed by incubation in 5% bovine serum albumin (BSA) for 20 min at room temperature. All sections were rinsed with phosphate-buffered saline (PBS) and incubated overnight at 4 °C with a monoclonal mouse anti-human antibody against KPNA2 (sc-55,538, 1:100 dilution, Santa Cruz Biotechnology, Santa Cruz, USA). The slides were washed with PBS and then incubated at room temperature with the appropriate secondary antibody for 20 min. Diaminobenzidine (DAB) staining was then performed. Cervical cancer samples were used as positive controls. Negative control sections were prepared by substituting a nonimmune IgG antibody for the primary antibody.
3
Immunohistochemical Analysis of KPNA2 in Bone Tissue
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All bone tissue samples were xed in formalin (pH 7.4) and decalci ed using standard procedures with 16-20 h incubation in 5% aqueous hydrochloric acid (HCl). Immunohistochemistry was performed on 4μm-thick para n-embedded whole tissue sections with standard techniques. Brie y, following depara nization and rehydration, charged slides with 4-μm-thick sections of tissue were treated with 3% hydrogen peroxide to eliminate endogenous peroxidase activity and then processed for antigen retrieval with 10 mm citrate buffer (pH 6.0) for 15 min at 95 °C, followed by incubation in 5% bovine serum albumin (BSA) for 20 min at room temperature. All sections were rinsed with phosphate-buffered saline (PBS) and incubated overnight at 4 °C with a monoclonal mouse anti-human antibody against KPNA2 (sc-55538, 1:100 dilution, Santa Cruz Biotechnology, Santa Cruz, USA). The slides were washed with PBS and then incubated at room temperature with the appropriate secondary antibody for 20 min. Diaminobenzidine (DAB) staining was then performed. Cervical cancer samples were used as positive controls. Negative control sections were prepared by substituting a nonimmune IgG antibody for the primary antibody.
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