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  • Rabbit Anti-S-Nitroso-Cysteine (SNO-Cys)

    • Rabbit Anti-S-Nitroso-Cysteine (SNO-Cys) | 15-NISC11-A

    NULL340.00

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    SKU:
    15-NISC11-A
    Availability:
    IN STOCK
    Size:
    100 µL
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    Product Description

    Rabbit Anti-S-Nitroso-Cysteine (SNO-Cys) | 15-NISC11-A

    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.

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