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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
biological source
rabbit
Quality Level
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
mouse, human
manufacturer/tradename
Upstate®
technique(s)
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG
shipped in
dry ice
target post-translational modification
dimethylation (Arg)
General description
Arginine methylation is a post-translational modification that results in the formation of asymmetrical and symmetrical dimethylated arginines (a- and sDMA).
Does not recognize non-methylated peptides, peptides containing asymmetrically dimethylated arginines, or a peptide containing a single symmetric dimethylarginine.
varies
Immunogen
peptide containing four symmetrical dimethyl-arginine-glycine repeats
Application
Anti-dimethyl-Arginine Antibody, symmetric (SYM10) is a high quality Rabbit Polyclonal Antibody for the detection of dimethyl-Arginine & has been validated in ICC, IP & WB.
Research Category
Signaling
Signaling
Research Sub Category
Chromatin Biology
Chromatin Biology
Biochem/physiol Actions
Recognizes proteins that contain multiple symmetrically dimethylated arginines, including p80-Coilin and the Sm protein B, B′ and D.
Physical form
Whole rabbit antiserum containing 0.05% sodium azide and 30% glycerol. Liquid at -20°C.
Preparation Note
Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Analysis Note
Control
Positive Antigen Control: Catalog #12-303, Jurkat cell lysate.
Positive Antigen Control: Catalog #12-303, Jurkat cell lysate.
routinely evaluated by immunoblot in RIPA lysates from Jurkat cells
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Legal Information
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.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
Lindsay M Webb et al.
Frontiers in immunology, 10, 524-524 (2019-04-04)
Multiple sclerosis is an autoimmune disease of the central nervous system (CNS) mediated by CD4+ T cells and modeled via experimental autoimmune encephalomyelitis (EAE). Inhibition of PRMT5, the major Type II arginine methyltransferase, suppresses pathogenic T cell responses and EAE.
Joris Paris et al.
Retrovirology, 15(1), 48-48 (2018-07-13)
Nuclear localization of Gag is a property shared by many retroviruses and retrotransposons. The importance of this stage for retroviral replication is still unknown, but studies on the Rous Sarcoma virus indicate that Gag might select the viral RNA genome
Arginine methylation mediated by the Arabidopsis homolog of PRMT5 is essential for proper pre-mRNA splicing.
Deng, X; Gu, L; Liu, C; Lu, T; Lu, F; Lu, Z; Cui, P; Pei, Y; Wang, B; Hu, S; Cao, X
Proceedings of the National Academy of Sciences of the USA null
Hironari Tamiya et al.
The Journal of clinical investigation, 128(1), 517-530 (2017-12-12)
SHARPIN, an adaptor for the linear ubiquitin chain assembly complex (LUBAC), plays important roles in NF-κB signaling and inflammation. Here, we have demonstrated a LUBAC-independent role for SHARPIN in regulating melanoma growth. We observed that SHARPIN interacted with PRMT5, a
Madhumitha Rengasamy et al.
Nucleic acids research, 45(19), 11106-11120 (2017-10-05)
We observed overexpression and increased intra-nuclear accumulation of the PRMT5/WDR77 in breast cancer cell lines relative to immortalized breast epithelial cells. Utilizing mass spectrometry and biochemistry approaches we identified the Zn-finger protein ZNF326, as a novel interaction partner and substrate
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