PRMT6, Polyclonal Antibody

Anti -PRMT6 (Protein arginine N Methyltransferase 6)

For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 1; NC_000001.10 (107599267..107601916). Location: 1p13.3

Polyclonal

IgG

Rabbit

Recognizes Human PRMT6 and mouse cell line (RAW).

Affinity Purified
Purified by Protein G affinity chromatography.

Supplied as a liquid in PBS, 0.02% sodium azide, 0.1 mg/ml BSA.

May be stored at 4 degree C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and add glycerol (40-50%). Freeze at -20 degree C. Aliquots are stable for at least 12 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Small volumes of anti-PRMT6 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

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. PRMT6 was identified by searching the human genome for protein arginine N-methyltransferase

Antibodies; Abs to Enzymes, Methyltransferase

Western Blot (WB)

Suitable for use in Western Blot.
Dilution: Western Blot: 1:500-1,000

41,938 Da[Similar Products]

protein arginine methyltransferase 6

protein arginine N-methyltransferase 6; OTTHUMP00000012633; HMT1 hnRNP methyltransferase-like 6; histone-arginine N-methyltransferase PRMT6; heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 6

Protein arginine N-methyltransferase 6

HRMT1L6  [Similar Products]

ANM6_HUMAN

Protein arginine N-methyltransferases, such as PRMT6, catalyze the sequential transfer of a methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins to form methylated arginine derivatives and S-adenosyl-L-homocysteine.[supplied by OMIM]

PRMT6: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). It thereby acts as a transcription corepressor of various genes such as HOXA2. Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to stimulate the polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. May play a role in innate immunity against HIV-1 in case of infection by methylating and impairing the function of various HIV-1 proteins such as Tat, Rev and Nucleocapsid protein p7 (NC). Belongs to the protein arginine N-methyltransferase family. PRMT6 subfamily. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Methyltransferase, protein arginine; Methyltransferase; EC 2.1.1.125

Chromosomal Location of Human Ortholog: 1p13.3

Cellular Component: nucleoplasm; cytosol; nucleus

Molecular Function: histone methyltransferase activity; protein-arginine omega-N monomethyltransferase activity; protein-arginine omega-N asymmetric methyltransferase activity; protein binding; histone binding

Biological Process: histone methylation; establishment and/or maintenance of chromatin architecture; viral reproduction; transcription, DNA-dependent; base-excision repair; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; negative regulation of transcription, DNA-dependent

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