Mouse Monoclonal dimethyl Arginine antibody. Suitable for IP, ChIP, WB and reacts with Modified Amino Acid samples. Cited in 11 publications.
Constituents: 2% Sucrose, 1.21% Tris, 0.75% Glycine
| IP | ChIP | WB | |
|---|---|---|---|
| Modified Amino Acid | Expected | Expected | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Modified Amino Acid | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Modified Amino Acid | Dilution info - | Notes Use 5µl for 4x106 cells. |
| Species | Dilution info | Notes |
|---|---|---|
Species Modified Amino Acid | Dilution info 1/50.00000 - 1/471.00000 | Notes - |
Di methyl Arginine
Mouse Monoclonal dimethyl Arginine antibody. Suitable for IP, ChIP, WB and reacts with Modified Amino Acid samples. Cited in 11 publications.
Constituents: 2% Sucrose, 1.21% Tris, 0.75% Glycine
This antibody reacts with free and bound asymmetric NG-NG-dimethyl arginine. It is not known whether the antibody reacts with symmetric dimethyl arginine.
This antibody will be of use in chromatin and transcription factor research to monitor methylation status. Since it is specific to dimethyl arginine it can be used in parallel with Anti-mono and dimethyl Arginine antibody [7E6] ab412 (detects monomethyl and dimethyl arginine) and Anti-mono methyl Arginine antibody [16B11] ab414 (detects monomethyl arginine only) to monitor the exact modification status.
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Dimethyl Arginine often referred to as asymmetric dimethylarginine (ADMA) is an endogenously produced molecule in the body. The molecular mass of dimethyl arginine usually depends on its specific dimethylated form with the molecule having different variants such as symmetric dimethylarginine (SDMA) and monomethylarginine (MMA). While dimethyl arginine is expressed in various tissues it predominantly arises as a byproduct of protein methylation processes. Protein arginine methyltransferases (PRMTs) enzymes responsible for these modifications mediate its formation influencing numerous physiological functions.
Dimethyl arginine modulates nitric oxide (NO) signaling by inhibiting nitric oxide synthase (NOS) enzymes which are vital for the production of NO—an important player in vasodilation and immune response. NO production requires L-arginine as a substrate and competition from dimethylated arginines reduces NO availability. This molecule though not a part of any large complex significantly impacts endothelial function and cell proliferation by affecting NO synthesis and cellular response to growth factors.
Dimethyl arginine plays an integral role in the regulation of the cardiovascular system and is involved in the urea cycle and polyamine pathways which are important for removing excess nitrogen and supporting cell growth respectively. The enzymes related to these pathways such as endothelial nitric oxide synthase (eNOS) and dimethylarginine dimethylaminohydrolase (DDAH) illustrate the interconnectedness of dimethyl arginine in maintaining vascular health and cellular homeostasis. The balance between dimethyl arginine and arginine levels affect the efficiency of the pathways indicating their influence on systemic health.
Dimethyl arginine links to cardiovascular diseases and chronic kidney disease. Its elevated levels often point to endothelial dysfunction contributing to the pathogenesis of atherosclerosis due to impaired NO-mediated vasodilation. Additionally kidney dysfunction can result in decreased dimethylarginine clearance exacerbating cardiovascular issues. Proteins such as eNOS and DDAH play pivotal roles in these conditions as they modulate the effects of dimethyl arginine on vascular and kidney health highlighting the importance of managing its levels in disease prevention and treatment.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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