biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

wide range

technique(s)

immunocytochemistry: 1:100 using paraformaldehyde-fixed, cultured bovine endothelial cell line treated with calcium ionophore A23187

indirect ELISA: 1:500 using S-nitrosylated cysteine-KLH

microarray: suitable

western blot: 1:2,000-1:4,000 using S-nitrosylated cysteine-BSA

shipped in

dry ice

storage temp.

−20°C

S-nitrosylation of cysteine thiols in proteins by the highly labile NO radical has been identified as a important effector of NO-related bioactivity both in NOS-containing cells and intercellular signaling, regulating NO-derived signal transduction pathways.
S-nitrosylation of proteins serves as a ubiquitous post-translational modification that dynamically regulates a broad functional spectrum of proteins.

S-nitrosylation of cysteine thiols has been shown to contribute to the cGMP-independent effects of NO. NO-sensitive ion channels, including the cardiac and skeletal muscle ryanodine receptor (RyR1), N-methyl-D-aspartate receptor (NMDAR) complex, and cyclic-nucleotide gated ion channel, are modulated by S-nitrosylation of critical cysteine residues.

S-nitrosylation of capsase-3 inhibits apoptosis signaling. S-nitrosylation activates matrix metalloproteinase-9 (MMP-9) and induces neuronal apoptosis.The small G-protein p21Ras and Jun kinases are regulated by S-nitrosylation. The activity of transcription factors such as NFkB, c-jun, and c-fos is modulated by S-nitrosylation.