|Tested species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Recombinant fragment corresponding to a region within amino acids 75 and 288 of PRMT7 (Uniprot ID#Q9NVM4)|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS, pH 7, with 1% BSA, 20% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:500-1:3000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
IHC notes, Requires antigen retrieval using heat mediated 10mM Citrate buffer (pH6.0) or Tris-EDTA buffer (pH8.0)
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.