07-413
Anti-dimethyl-Arginine Antibody, symmetric (SYM11)
Upstate®, from rabbit
Synonym(s):
Anti-SYM11, Anti-dimethyl-Arginine, Symmetric Dimethyl-Arginine Ab
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
polyclonal
species reactivity
human, mouse
manufacturer/tradename
Upstate®
technique(s)
western blot: suitable
isotype
IgG
shipped in
dry ice
target post-translational modification
unmodified
Related Categories
General description
Symmetrical dimethylated arginine (sDMA) is a product of the post-translational modification, arginine methylation. sDMA is a structural isomer of asymmetric dimethylarginine.
Specificity
SmD3 at ~16kDa, and other proteins that contain arginines that are symmetrically dimethylated
Immunogen
peptide corresponding to amino acids 99-119 of Small nuclear ribonucleoprotein SmD3.
Application
Anti-dimethyl-Arginine Antibody, symmetric (SYM11) has been used in:
- co-immunoprecipitation (co-IP)
- western blot analysis
- immunoprecipitation
Biochem/physiol Actions
Symmetrical dimethylarginine (sDMA) is a competitor of arginine transport and is eliminated through renal excretion. sDMA serves as a marker to indicate the estimated glomerular filtration rate (GFR) and the coronary artery disease (CAD) severity. Elevated sDMA is associated with the risk of cardiovascular disease and mortality. It might also help in the early detection of chronic kidney disease. sDMA acts as an endogenous marker of renal function. It is associated with tumorigenesis.
Quality
routinely evaluated by immunoblot in RIPA lysates from Jurkat cells
Target description
~16 kDa
Physical form
Format: Purified
Analysis Note
Control
Positive Antigen Control: Catalog #12-303, Jurkat cell lysate.
Positive Antigen Control: Catalog #12-303, Jurkat cell lysate.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Certificates of Analysis (COA)
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Zi Wang et al.
Communications biology, 7(1), 241-241 (2024-02-29)
PRMT5, a type II arginine methyltransferase, is involved in transcriptional regulation, RNA processing and other biological processes and signal transduction. Secondary metabolites are vital pharmacological compounds in Ganoderma lucidum, and their content is an important indicator for evaluating the quality
Jérémy Dufourt et al.
Nature communications, 8(1), 1305-1305 (2017-11-05)
Piwi-interacting RNAs (piRNAs) and PIWI proteins play a crucial role in germ cells by repressing transposable elements and regulating gene expression. In Drosophila, maternal piRNAs are loaded into the embryo mostly bound to the PIWI protein Aubergine (Aub). Aub targets
Rui Liu et al.
Microbiology spectrum, 11(6), e0290623-e0290623 (2023-10-26)
PRMT5 contributes to secondary metabolite biosynthesis in Ganoderma lucidum. However, the mechanism through which PRMT5 regulates the biosynthesis of secondary metabolites remains unclear. In the current study, PRMT5 silencing led to a significant decrease in the biosynthesis of polysaccharides from
Lars D Engstrom et al.
Cancer discovery, 13(11), 2412-2431 (2023-08-08)
Previous studies implicated protein arginine methyltransferase 5 (PRMT5) as a synthetic lethal target for MTAP-deleted (MTAP del) cancers; however, the pharmacologic characterization of small-molecule inhibitors that recapitulate the synthetic lethal phenotype has not been described. MRTX1719 selectively inhibited PRMT5 in
Christopher R Smith et al.
Journal of medicinal chemistry, 65(3), 1749-1766 (2022-01-19)
The PRMT5•MTA complex has recently emerged as a new synthetically lethal drug target for the treatment of MTAP-deleted cancers. Here, we report the discovery of development candidate MRTX1719. MRTX1719 is a potent and selective binder to the PRMT5•MTA complex and
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