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Sigma-Aldrich

Anti-dimethyl-Arginine Antibody, asymmetric (ASYM25)

serum, from rabbit

Synonyme(s) :

dimethyl-arginine, asymmetric

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About This Item

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

Source biologique

rabbit

Niveau de qualité

100

Forme d'anticorps

serum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Espèces réactives

mouse

Réactivité de l'espèce (prédite par homologie)

rat (based on 100% sequence homology), human (based on 100% sequence homology)

Technique(s)

western blot: suitable

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Description générale

Asymmetrical dimethlarginine (ADMA) is an endogenous, L-arginine metabolite arising from the proteolysis of methylated arginine containing proteins and is a known inhibitor of nitric oxide synthase (NOS). In various studies, ADMA has been observed as having a regulatory role in cell motility and the actin cytoskeleton. Elevated levels of ADMA are associated with sporadic FSGS, coronary artery disease, hypertension, peripheral arterial occlusive disease, obesity, stroke, preeclampsia, and cardiovascular mortality/morbidity in patients with diabetic nephropathy.

Spécificité

This antibody recognizes dimethylated arginines.

Immunogène

KLH-conjugated linear peptide containing asymmetric dimethyl-arginine-glycine repeats.

Application

Detect dimethyl-Arginine using this Anti-dimethyl-Arginine Antibody, asymmetric (ASYM25) validated for use in WB.

Qualité



µ

Description de la cible

Multiple. This antibody detects proteins containing asymmetrical dimethylated arginines.

Remarque sur l'analyse


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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

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Minghao Yang et al.
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Osteosarcoma (OS), the most common primary malignancy of the bone, has a poor prognosis due to its high mortality rate and high potential for metastasis. Thus, it is urgently necessary to explore functional molecular targets of therapeutic strategies for osteosarcoma.
Li-Ming Liu et al.
Cancer research, 79(11), 2865-2877 (2019-04-25)
C/EBPα is an essential transcription factor involved in regulating the expression or function of certain cell-cycle regulators, including in breast cancer cells. Although protein arginine methyltransferases have been shown to play oncogenic roles in a variety of cancers, little is
Yongtai Bai et al.
Molecular cell, 75(6), 1299-1314 (2019-07-30)
MRE11 nuclease forms a trimeric complex (MRN) with RAD50 and NBS1 and plays a central role in preventing genomic instability. When DNA double-strand breaks (DSBs) occur, MRN is quickly recruited to the damage site and initiates DNA end resection; accordingly
Olesya A Ulanovskaya et al.
Nature chemical biology, 9(5), 300-306 (2013-03-05)
Nicotinamide N-methyltransferase (NNMT) is overexpressed in a variety of human cancers, where it contributes to tumorigenesis by a mechanism that is still poorly understood. Here we show using metabolomics that NNMT impairs the methylation potential of cancer cells by consuming
Li-Ming Liu et al.
Life (Basel, Switzerland), 11(8) (2021-08-28)
The protein p53 is one of the most important tumor suppressors, responding to a variety of stress signals. Mutations in p53 occur in about half of human cancer cases, and dysregulation of the p53 function by epigenetic modifiers and modifications
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