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symmetric dimethylarginine sdma  (MedChemExpress)


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    Structured Review

    MedChemExpress symmetric dimethylarginine sdma
    ( A ) Schematic diagram depicting the Tudor affinity resin. SMN Tudor domain shown in surface representation (light gray) is immobilized onto the Halo-link agarose resin via an N-terminal Halo-tag. The box on the right illustrates the recognition of <t>sDMA</t> by the aromatic cage of SMN Tudor domain. ( B ) Workflow for the molecular affinity strategy for arginine methylation profiling. ( C ) The enrichment efficiencies of molecular affinity strategy in three biological replicate experiments. ( D ) The number of methylation peptides and different methylarginine sites (monomethyl or dimethyl) identified from three biological replicates. ( E ) The reproducibility of molecular affinity strategy by comparing identified methylarginine sites in three biological replicates.
    Symmetric Dimethylarginine Sdma, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/symmetric dimethylarginine sdma/product/MedChemExpress
    Average 93 stars, based on 3 article reviews
    symmetric dimethylarginine sdma - by Bioz Stars, 2026-03
    93/100 stars

    Images

    1) Product Images from "Tudor-based proteomic strategy pan-specifically enriches and identifies protein arginine methylation"

    Article Title: Tudor-based proteomic strategy pan-specifically enriches and identifies protein arginine methylation

    Journal: EMBO Reports

    doi: 10.1038/s44319-025-00599-y

    ( A ) Schematic diagram depicting the Tudor affinity resin. SMN Tudor domain shown in surface representation (light gray) is immobilized onto the Halo-link agarose resin via an N-terminal Halo-tag. The box on the right illustrates the recognition of sDMA by the aromatic cage of SMN Tudor domain. ( B ) Workflow for the molecular affinity strategy for arginine methylation profiling. ( C ) The enrichment efficiencies of molecular affinity strategy in three biological replicate experiments. ( D ) The number of methylation peptides and different methylarginine sites (monomethyl or dimethyl) identified from three biological replicates. ( E ) The reproducibility of molecular affinity strategy by comparing identified methylarginine sites in three biological replicates.
    Figure Legend Snippet: ( A ) Schematic diagram depicting the Tudor affinity resin. SMN Tudor domain shown in surface representation (light gray) is immobilized onto the Halo-link agarose resin via an N-terminal Halo-tag. The box on the right illustrates the recognition of sDMA by the aromatic cage of SMN Tudor domain. ( B ) Workflow for the molecular affinity strategy for arginine methylation profiling. ( C ) The enrichment efficiencies of molecular affinity strategy in three biological replicate experiments. ( D ) The number of methylation peptides and different methylarginine sites (monomethyl or dimethyl) identified from three biological replicates. ( E ) The reproducibility of molecular affinity strategy by comparing identified methylarginine sites in three biological replicates.

    Techniques Used: Methylation

    The lines represent data fitting curves using 1:1 binding model at a fixed stoichiometry (N) of 1. The peptides used were SmD1 (AGRGRGR), SmD1-sDMA (AGR me2s GRGR), SmD1 aDMA (AGR me2a GRGR).
    Figure Legend Snippet: The lines represent data fitting curves using 1:1 binding model at a fixed stoichiometry (N) of 1. The peptides used were SmD1 (AGRGRGR), SmD1-sDMA (AGR me2s GRGR), SmD1 aDMA (AGR me2a GRGR).

    Techniques Used: Binding Assay



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    ( A ) Schematic diagram depicting the Tudor affinity resin. SMN Tudor domain shown in surface representation (light gray) is immobilized onto the Halo-link agarose resin via an N-terminal Halo-tag. The box on the right illustrates the recognition of <t>sDMA</t> by the aromatic cage of SMN Tudor domain. ( B ) Workflow for the molecular affinity strategy for arginine methylation profiling. ( C ) The enrichment efficiencies of molecular affinity strategy in three biological replicate experiments. ( D ) The number of methylation peptides and different methylarginine sites (monomethyl or dimethyl) identified from three biological replicates. ( E ) The reproducibility of molecular affinity strategy by comparing identified methylarginine sites in three biological replicates.
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    ( A ) Schematic diagram depicting the Tudor affinity resin. SMN Tudor domain shown in surface representation (light gray) is immobilized onto the Halo-link agarose resin via an N-terminal Halo-tag. The box on the right illustrates the recognition of <t>sDMA</t> by the aromatic cage of SMN Tudor domain. ( B ) Workflow for the molecular affinity strategy for arginine methylation profiling. ( C ) The enrichment efficiencies of molecular affinity strategy in three biological replicate experiments. ( D ) The number of methylation peptides and different methylarginine sites (monomethyl or dimethyl) identified from three biological replicates. ( E ) The reproducibility of molecular affinity strategy by comparing identified methylarginine sites in three biological replicates.
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    ( A ) Schematic diagram depicting the Tudor affinity resin. SMN Tudor domain shown in surface representation (light gray) is immobilized onto the Halo-link agarose resin via an N-terminal Halo-tag. The box on the right illustrates the recognition of <t>sDMA</t> by the aromatic cage of SMN Tudor domain. ( B ) Workflow for the molecular affinity strategy for arginine methylation profiling. ( C ) The enrichment efficiencies of molecular affinity strategy in three biological replicate experiments. ( D ) The number of methylation peptides and different methylarginine sites (monomethyl or dimethyl) identified from three biological replicates. ( E ) The reproducibility of molecular affinity strategy by comparing identified methylarginine sites in three biological replicates.
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    Image Search Results


    ( A ) Schematic diagram depicting the Tudor affinity resin. SMN Tudor domain shown in surface representation (light gray) is immobilized onto the Halo-link agarose resin via an N-terminal Halo-tag. The box on the right illustrates the recognition of sDMA by the aromatic cage of SMN Tudor domain. ( B ) Workflow for the molecular affinity strategy for arginine methylation profiling. ( C ) The enrichment efficiencies of molecular affinity strategy in three biological replicate experiments. ( D ) The number of methylation peptides and different methylarginine sites (monomethyl or dimethyl) identified from three biological replicates. ( E ) The reproducibility of molecular affinity strategy by comparing identified methylarginine sites in three biological replicates.

    Journal: EMBO Reports

    Article Title: Tudor-based proteomic strategy pan-specifically enriches and identifies protein arginine methylation

    doi: 10.1038/s44319-025-00599-y

    Figure Lengend Snippet: ( A ) Schematic diagram depicting the Tudor affinity resin. SMN Tudor domain shown in surface representation (light gray) is immobilized onto the Halo-link agarose resin via an N-terminal Halo-tag. The box on the right illustrates the recognition of sDMA by the aromatic cage of SMN Tudor domain. ( B ) Workflow for the molecular affinity strategy for arginine methylation profiling. ( C ) The enrichment efficiencies of molecular affinity strategy in three biological replicate experiments. ( D ) The number of methylation peptides and different methylarginine sites (monomethyl or dimethyl) identified from three biological replicates. ( E ) The reproducibility of molecular affinity strategy by comparing identified methylarginine sites in three biological replicates.

    Article Snippet: Symmetric dimethylarginine (SDMA) , MedChemExpress , #HY-101410.

    Techniques: Methylation

    The lines represent data fitting curves using 1:1 binding model at a fixed stoichiometry (N) of 1. The peptides used were SmD1 (AGRGRGR), SmD1-sDMA (AGR me2s GRGR), SmD1 aDMA (AGR me2a GRGR).

    Journal: EMBO Reports

    Article Title: Tudor-based proteomic strategy pan-specifically enriches and identifies protein arginine methylation

    doi: 10.1038/s44319-025-00599-y

    Figure Lengend Snippet: The lines represent data fitting curves using 1:1 binding model at a fixed stoichiometry (N) of 1. The peptides used were SmD1 (AGRGRGR), SmD1-sDMA (AGR me2s GRGR), SmD1 aDMA (AGR me2a GRGR).

    Article Snippet: Symmetric dimethylarginine (SDMA) , MedChemExpress , #HY-101410.

    Techniques: Binding Assay