N5411
Anti-S-Nitroso-Cysteine (SNO-Cys) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Sign Into View Organizational & Contract Pricing
Select a Size
About This Item
MDL number:
UNSPSC Code:
12352203
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.
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)
Biochem/physiol Actions
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.
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.
Not finding the right product?
Try our Product Selector Tool.
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
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Xinyan Zhu et al.
Acta biochimica et biophysica Sinica, 55(10), 1640-1649 (2023-09-13)
The mechanism of extracellular matrix metalloproteinase inducer (EMMPRIN) in the regulation of liver fibrosis has not been clarified. This study aims to investigate the role of EMMPRIN S-nitrosylation (SNO) in the regulation of hepatic stellate cell (HSC) migration and matrix
Michele Salanova et al.
Redox biology, 1, 514-526 (2013-11-20)
Activity-induced nitric oxide (NO) imbalance and "nitrosative stress" are proposed mechanisms of disrupted Ca(2+) homeostasis in atrophic skeletal muscle. We thus mapped S-nitrosylated (SNO) functional muscle proteins in healthy male subjects in a long-term bed rest study (BBR2-2 Study) without
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
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
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service