|IP||1-4 μL/mg of lysate|
**********Please Note: Optimal concentrations/dilutions should be determined by the end user.**********
PRMT6 was immunoprecipitated using:
Lane A:0.5 mg MCF-7 Whole Cell Lysate
Lane B:0.5 mg 293T Whole Cell Lysate
Lane C:0.5 mg Hela Whole Cell Lysate2 µL anti-PRMT6 rabbit polyclonal antibody and 15 μl of 50 % Protein G agarose.Primary antibody:
Anti-PRMT6 rabbit polyclonal antibody,at 1:200 dilutionSecondary antibody:
Clean-Blotô IP Detection Reagent (HRP) at 1:500 dilutionDeveloped using the DAB staining technique.
Performed under reducing conditions.Predicted band size: 42 kDa
Observed band size: 42 kDa
Anti-PRMT6 rabbit polyclonal antibody at 1:500 dilution
Lane A: 293T Whole Cell Lysate
Lane B: MCF7 Whole Cell Lysate
Lane C: Hela Whole Cell LysateLysates/proteins at 30 μg per lane.
Goat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution.Developed using the Odyssey technique.
Performed under reducing conditions.Predicted band size:42 kDa
Observed band size:42 kDa
Protein arginine N-methyltransferase 6, also known as Histone-arginine N-methyltransferase PRMT6, PRMT6, and HRMT1L6, is a member of the protein arginine N-methyltransferase family and PRMT6 subfamily. PRMT6 is highly expressed in kidney and testes. PRMT6 is known to catalyze the generation of asymmetric dimethylarginine in polypeptides. It has been implicated in human immunodeficiency virus pathogenesis, DNA repair, and transcriptional regulation. PRMT6 is known to methylate histone H3 Arg-2 (H3R2), and this negatively regulates the lysine methylation of H3K4 resulting in gene repression. PRMT6 plays a key role in coupling process by functioning as a transcriptional coactivator that can regulate alternative splicing. PRMT6 coactivates the progesterone, glucocorticoid and oestrogen receptors in luciferase reporter assays in a hormone-dependent manner. Small interfering RNA (siRNA) oligonucleotide duplex knockdown of PRMT6 disrupts oestrogen-stimulated transcription of endogenous GREB1 and progesterone receptor in MCF-7 breast cancer cells. Neutralizing the activity of PRMT6 could inhibit tumor progression and may be of cancer therapeutic significance.