Recombinant human PRMT1 protein

Protein arginine N-methyltransferase 1 (PRMT1) is a type I methyltransferase that transfers a methyl group from S-adenosylmethionine to guanidino nitrogens of arginine residues to form monomethylarginine and asymmetric dimethylarginine. Functions of type I arginine methylation in proteins may include regulation of transcription, modulation of the affinity of nucleic acid-binding proteins, regulation of interferon signaling pathways, and targeting of nuclear proteins. Recombinant human PRMT1, fused to His-MBP tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

Product Specifications

Specifications

Specific activity is > 10 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group on histone H4 per minute at 37C.

Product Name Alternative

Protein arginine N-methyltransferase 1 isoform 3, HRMT1L2, HMT1 hnRNP methyltransferase-like 2 (S. cerevisiae), HCP1, ANM1, Histone-arginine N-methyltransferase PRMT1, Interferon receptor 1-bound protein 4, IR1B4, ANM1, highly conserved protein 1

Expression System

E.coli

Antigen Species

Human

Tag

His-MBP-Tag

Applications

SDS-PAGE, Enzyme Activity

Concentration

1 mg/mL (determined by Bradford assay)

Purity

> 90% by SDS-PAGE

Bioactivity

Specific activity is > 10 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group on histone H4 per minute at 37C.

Molecular Weight

84.2 kDa (750aa)

Additionnal Information

S. cerevisiae like 2, Protein arginine N methyltransferase1, Protein arginine N methyltransferase 1, protein arginine methyltransferase 1, PRMT1 isoform3, PRMT1, PRMT 1, Mrmt1, Mrmt 1, IR1B4, IR1B 4, IR1 B4, Interferon receptor 1bound protein 4, Interferon receptor 1 bound protein4, Interferon receptor 1 bound protein 4, Human mRNA for suppressor for yeast mutant complete cds, Human mRNA for suppressor for yeast mutant, HRMT1L2, HRMT1L 2, HRMT1 L2, HMT2, HMT1 hnRNP methyltransferase-like 2 isoform 3 ANM 1, HMT1 hnRNP methyltransferase-like 2 isoform 3, HMT1 hnRNP methyltransferase like 2 (S. cerevisiae), HMT1 hnRNP methyltransferase like 2, HMT1 hnRNP methyltransferase, HMT1 (hnRNP methyltransferase S. cerevisiae) like 2, HMT 2, Heterogeneous nuclear ribonucleoproteins methyltransferase like2, Heterogeneous nuclear ribonucleoproteins methyltransferase like 2, HCP1, HCP 1, ANM1, PRM0802-10 µg, PRM0802-20 µg, PRM0802-50 µg, PRM0802-100 µg, PRM0802-250 µg, PRM0802-500 µg, PRM0802-1 mg, PRM0802-0

References & Citations

Goulet I., et al. (2007) J Biol Chem. 282 (45) :33009-21.; ; Tang J., et al. (2000) J Biol Chem. 275 (11) :7723-30.;

Other References

Yamaguchi A, et al. The Effect of PRMT1-Mediated Arginine Methylation on the Subcellular Localization, Stress Granules, and Detergent-Insoluble Aggregates of FUS/TLS. (PLoS One. 2012) {https://pubmed.ncbi.nlm.nih.gov/23152885/}; ; Ryan VH, et al. Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation. (Mol Cell. 2018) {https://pubmed.ncbi.nlm.nih.gov/29358076/}; ; Dong R, et al. The translation initiating factor eIF4E and arginine methylation underlie G3BP1 function in dendritic spine development of neurons. (J Biol Chem. 2023) {https://pubmed.ncbi.nlm.nih.gov/37442236/}

Storage Conditions

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Formulation

Liquid in. 40 mM Tris-HCl buffer (pH 8.0) containing 100 mM NaCl, 4mM MgCl₂, 2mM DTT, 40% glycerol

Scientific Category

Histone Related

NCBI Accession Number

NP_938074.2

Uniprot Accession Number

Q99873

Species

Human

AA Sequence

MAA AEAANCIMEV SCGQAESSEK PNAEDMTSKD YYFDSYAHFG IHEEMLKDEV RTLTYRNSMF HNRHLFKDKV VLDVGSGTGI LCMFAAKAGA RKVIGIECSS ISDYAVKIVK ANKLDHVVTI IKGKVEEVEL PVEKVDIIIS EWMGYCLFYE SMLNTVLYAR DKWLAPDGLI FPDRATLYVT AIEDRQYKDY KIHWWENVYG FDMSCIKDVA IKEPLVDVVD PKQLVTNACL IKEVDIYTVK VEDLTFTSPF CLQVKRNDYV HALVAYFNIE FTRCHKRTGF STSPESPYTH WKQTVFYMED YLTVKTGEEI FGTIGMRPNA KNNRDLDFTI DLDFKGQLCE LSCSTDYRMR