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.
Positive Control: HeLa or NIH 3T3 cell lysate.
Applications:Suitable for use in Western Blot.
Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Aliquots are stable for 12 months after receipt.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：100ug
Host：rabbit
Source Antibody：human
Grade：Affinity Purified
Purity：Purified by Protein G affinity chromatography.
Form：Supplied as a liquid in PBS, 0.05% BSA, 0.05% sodium azide.
Specificity：Recognizes human PRMT7. Species Crossreactivity: mouse. 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).
