Anti s nitrosocysteine

Immunofluorescence analyses were conducted using the protocol as described elsewhere 17, 18. To detect NFκB subcellular localization, we used anti‐NFκB (p65) (Santa Cruz) and anti‐α‐actinin (Sigma) as primary antibodies and detected using fluorescent‐labelled secondary antibodies (Jackson Lab, West Grove, PA, USA). DAPI was used to stain the nuclei. To examine S‐nitrosylation of RyR and SERCA2a, we used anti‐SERCA2a (Santa Cruz Biotechnology), anti‐RYR (Abcam) and anti‐S‐nitrosocysteine (Abcam).

The following antibodies were used. Anti-β-Galactosidase (Bioss, bs-4960R), anti-alkaline phosphatase (Novus Biologicals, NBP1-32948); anti-heterochromatin protein 1-γ (HP1-γ, phospho Ser 93, Bioss, bs-3221R); anti-p21 (Bioss, bs-10129R); anti-p27 (phospho Thr 187, Abcam, ab75908); anti-NOS-1, 2 (Thermo Fisher Scientific, PA1-033 and -036); anti-NOS-3 (Sigma-Aldrich, SAB-4300435); anti-ErbB2 (Thermo Fisher Scientific, PA5-16395); anti-pSMAD3 (Ser423/Ser425, Novous Biological, NBP1-77836); anti-CD24 (Novus Biologicals, NBP1-4639055); anti-CD44 (Bioss, bs-2507R); anti-S-Nitroso-Cysteine (Abcam, ab50185 or Alpha Diagnostics, NISC11-A); anti-Integrin α6 (BD Biosciences, 555734); anti-GM130 (Cell Signaling, 12480 S); anti-human CK 14 (ThermoFisher, MA511599); anti-human CK 18 (ThermoFisher, PA514263); anti-mouse CK 14 (BioLegend, 905301); anti-human CK 8/18 (DSHB, Troma-I); anti-Cleaved Caspase3 (Cell Signaling, #9664); anti-β-Actin (Sigma, A1978); anti-DYNLL1 (Abcam, ab51603); and anti-ADMA (EMD Millipore, 09-814).