| Product Name | Histone H4 (1-20), PRMT7 Substrate, M1 |
| Product Quantity | 1 mg |
| Sequence | SGRGKGGKGLGKGGAKRHRK-NH2 |
| Molecular Weight | 1991.5 |
| Purity | ≥95% |
| Mechanism & Biological Significance | This amidated histone H4 N-terminal peptide is a defined protein arginine methyltransferase 7 (PRMT7) substrate. The GRG/RXR-rich H4 tail provides arginine sites that allow direct measurement of PRMT7-catalyzed methyl transfer and is useful for distinguishing PRMT7 substrate preferences from other PRMT family enzymes. |
| Published Research Context | The exact M1 sequence SGRGKGGKGLGKGGAKRHRK-amide has been used directly in PRMT7 enzymology. The original 2005 study reported methylation of the H4-derived M1 peptide by recombinant PRMT7. Later mechanistic work explicitly lists the same free-N-terminus, C-terminal-amide M1 peptide and showed that human PRMT7 produces monomethylarginine on this substrate, refining the enzyme's classification to a type III PRMT. |
| Research Applications | - PRMT7 activity and kinetic assays
- arginine-methylation mechanism studies
- PRMT substrate-specificity profiling
- PRMT inhibitor screening and assay controls
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| Experimental Considerations | The C-terminal amide is part of the exact reagent identity and should be retained. Historical literature initially classified PRMT7 as type II; later purified-enzyme work established type III monomethyltransferase activity, so the LifeTein description uses the updated mechanistic interpretation. |
| Selected Scientific References | - PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine
- Human Protein Arginine Methyltransferase 7 (PRMT7) Is a Type III Enzyme Forming ω-NG-Monomethylated Arginine Residues
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