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Merck
CN

09-814

Anti-dimethyl-Arginine Antibody, asymmetric (ASYM25)

serum, from rabbit

Synonym(s):

dimethyl-arginine, asymmetric

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About This Item

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

Key Documents

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Product Name

Anti-dimethyl-Arginine Antibody, asymmetric (ASYM25), serum, from rabbit

biological source

rabbit

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

mouse

species reactivity (predicted by homology)

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

technique(s)

western blot: suitable

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

100

Analysis Note

Control
PRMT1 treated and untreated MEF cell lysates
Evaluated by Western Blot in PRMT1 treated and untreated MEF cell lysates.

Western Blot Analysis: 1:1,000 dilution of this antibody detected dimethyl-Arginine on 10 µg of PRMT1 treated and untreated MEF cell lysates.

Application

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

Biochem/physiol Actions

This antibody recognizes dimethylated arginines.

General description

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.
Multiple. This antibody detects proteins containing asymmetrical dimethylated arginines.

Immunogen

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

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Storage Class

10 - Combustible liquids

wgk

WGK 1

Certificates of Analysis (COA)

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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
Minghao Yang et al.
Cell death & disease, 13(9), 815-815 (2022-09-24)
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.
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
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
Gang Ren et al.
Scientific reports, 9(1), 6688-6688 (2019-05-02)
One third of newly diagnosed breast cancers in the US are early-stage lesions. The etiological understanding and treatment of these lesions have become major clinical challenges. Because breast cancer risk factors are often linked to aberrant nitric oxide (NO) production
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