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Merck
CN

16-227

Anti-Nitrotyrosine Antibody, clone 1A6, Alexa Fluor 555 conjugate

clone 1A6, Upstate®, from mouse

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
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biological source

mouse

Quality Level

conjugate

ALEXA FLUOR 555

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

1A6, monoclonal

species reactivity

vertebrates

manufacturer/tradename

Upstate®

technique(s)

flow cytometry: suitable
western blot: suitable

isotype

IgG2bκ

shipped in

wet ice

target post-translational modification

nitration (Tyr)

Gene Information

human ... NOS1(4842)

Related Categories

General description

The molecular weight is related to the nitrated protein

Immunogen

Nitrated KLH

Application

Anti-Nitrotyrosine Antibody, clone 1A6, Alexa Fluor 555 conjugate is an antibody against Nitrotyrosine for use in FC & WB.
Research Category
Neuroscience
Research Sub Category
Oxidative Stress

Biochem/physiol Actions

recognizes nitrated protein

Physical form

Protein G Purified

Preparation Note

1 year at 4°C from date of shipment

Analysis Note

Routinely evaluated by immunoblot.

Legal Information

ALEXA FLUOR is a trademark of Life Technologies
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

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.

Alexa Fluor is a registered trademark of Molecular Probes, Inc.

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Storage Class Code

10 - Combustible liquids

Regulatory Information

新产品
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Certificates of Analysis (COA)

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Biological significance of nitric oxide-mediated protein modifications.
Gow, Andrew J, et al.
American Journal of Physiology. Lung Cellular and Molecular Physiology, 287, L262-L268 (2004)
C Ayata et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 17(18), 6908-6917 (1997-09-15)
We investigated the role of neuronal (type I) nitric oxide synthase (nNOS) in NMDA-mediated excitotoxicity in wild-type (SV129 and C57BL/6J) and type I NOS knock-out (nNOS-/-) mice and examined its relationship to apoptosis. Excitotoxic lesions were produced by intrastriatal stereotactic
J Torreilles et al.
BMC immunology, 2, 1-1 (2001-03-07)
Peroxynitrite is increasingly proposed as a contributor to defence system in marine bivalve. It can be formed by combination of superoxide and nitric oxide, and can react with tyrosine residues of proteins giving rise to 3-nitrotyrosine. The present article describes
Zarema Balafanova et al.
The Journal of biological chemistry, 277(17), 15021-15027 (2002-02-13)
Activation of protein kinase C (PKC) epsilon by nitric oxide (NO) has been implicated in the development of cardioprotection. However, the cellular mechanisms underlying the activation of PKCepsilon by NO remain largely unknown. Nitration of protein tyrosine residues has been
Ming-Hui Zou et al.
The Journal of clinical investigation, 109(6), 817-826 (2002-03-20)
Nitric oxide (NO) is produced by NO synthase (NOS) in many cells and plays important roles in the neuronal, muscular, cardiovascular, and immune systems. In various disease conditions, all three types of NOS (neuronal, inducible, and endothelial) are reported to

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"Redox reactions are powerful chemical processes that involve the reduction and oxidation of proteins and metabolites found in living things. The mechanisms that regulate them are key to maintaining homeostasis and the balance between good health and disease pathology. Oxidative stress is the state where the delicate balance of redox biology is upset, and the pathology of oxidative stress are the cellular consequences to such an imbalance."

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