Protein arginine methylation is an important posttranslational modification in eukaryotic cells, which has been implicated in RNA processing and trafficking, receptor-mediated signaling, and transcription. The PRMT proteins are recruited by C-terminal activation domain-2 of the SRC (steroid receptor coactivator) GRIP-1, whereas p300 interacts with activation domain-1 in the C terminus. have identified a mammalian arginine N-methyltransferase, PRMT7, that can catalyze the formation of omega-NG-monomethylarginine in peptides. In contrast to the other members of the PRMT family, PRMT7 was not able to methylate GST-fibrillarin or myelin basic protein or histone H2A, in vitro. It is also structurally different from other PRMTS in containing two putative AdoMet-binding motifs. Both of these domains are required for enzymatic activity.
Immunogen
PRMT7 antibody was raised against amino acids 346 - 360 of PRMT7 (Human).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
IHCWB
PRMT7 antibody can be used in ELISA, Western Blot, immunohistochemistry starting at 5 μg/mL, and immunofluorescence starting at 10 μg/mL.:
The amino acid sequence used as immunogen can be found in five different human PRMT7 isoforms: CRA_a (692 amino acids), CRA_b (613 amino acids), CRA_c (465 amino acids), CRA_d (655 amino acids) and CRA_e (567 amino acids).