N5411
Anti-S-Nitroso-Cysteine (SNO-Cys) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
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About This Item
MDL number:
UNSPSC Code:
12352203
Recommended Products
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
General description
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.
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.
Specificity
Anti-S-Nitroso-Cysteine (SNO-Cys) antibody recognizes S-nitrosylated proteins. The antibody specifically recognizes S-nitroso-cysteine-BSA in immunoblotting and ELISA, but does not recognize unmodified BSA.
The antibody recognizes S-nitroso-cysteine-BSA, but does not recognize unmodified BSA.
Immunogen
S-nitrosylated cysteine-KLH.
Application
Anti-S-Nitroso-Cysteine may be used for applications such s immunoblotting, ELISA, and immunocytochemistry.
Immunoblotting: a minimum working antibody dilution of 1:2000- 1:4000 is recommended using S-nitrosylated cysteine-BSA.
ELISA: a minimum working antibody dilution of 1:500 is recommended using S-nitrosylated cysteine-BSA.
Immunocytochemistry: a minimum working antibody dilution of 1:100 is recommended using bovine endothelial cells treated with Ca2+ ionophore A23187.
Immunoblotting: a minimum working antibody dilution of 1:2000- 1:4000 is recommended using S-nitrosylated cysteine-BSA.
ELISA: a minimum working antibody dilution of 1:500 is recommended using S-nitrosylated cysteine-BSA.
Immunocytochemistry: a minimum working antibody dilution of 1:100 is recommended using bovine endothelial cells treated with Ca2+ ionophore A23187.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western blotting following immunoprecipitation (1 paper)
Western blotting following immunoprecipitation (1 paper)
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Jeffrey R Erickson et al.
The Journal of biological chemistry, 290(42), 25646-25656 (2015-09-01)
NO is known to modulate calcium handling and cellular signaling in the myocardium, but key targets for NO in the heart remain unidentified. Recent reports have implied that NO can activate calcium/calmodulin (Ca(2+)/CaM)-dependent protein kinase II (CaMKII) in neurons and
Jing Li et al.
Redox biology, 17, 386-399 (2018-06-04)
The adaptive immune system plays a critical role in hyperhomocysteinemia (HHcy)-accelerated atherosclerosis. Recent studies suggest that HHcy aggravates atherosclerosis with elevated oxidative stress and reduced S-nitrosylation level of redox-sensitive protein residues in the vasculature. However, whether and how S-nitrosylation contributes
Rivi Hertz et al.
Eukaryotic cell, 13(4), 494-503 (2014-02-25)
Nitric oxide (NO) has antimicrobial properties against many pathogens due to its reactivity as an S-nitrosylating agent. It inhibits many of the key enzymes that are involved in the metabolism and virulence of the parasite Entamoeba histolytica through S-nitrosylation of
Samson Jamesdaniel et al.
Antioxidants & redox signaling, 17(7), 929-933 (2012-04-25)
S-nitrosylation is a redox-sensitive protein modification, which is a highly specific, but reversible mechanism that regulates several signal transduction cascades. Oxidative stress plays a causal role in the ototoxic effects of an anti-neoplastic drug, cisplatin. Despite emerging evidence implicating nitroxidative
Suvendu Giri et al.
Clinical and experimental pharmacology & physiology, 47(1), 7-15 (2019-09-25)
Cardiovascular side effects of broadly used chemotherapeutic drugs such as Tamoxifen citrate (TC), Capecitabine (CP) and Epirubicin (EP) among cancer survivors are well established. Nitric oxide (NO) is known to protect cardiovascular tissues under conditions of stress. NO can act
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