SRP0146
PRMT5/MEP50 Active human
recombinant, expressed in baculovirus infected insect cells, ≥70% (SDS-PAGE)
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Synonym(s):
Arginine methyltransferase 5, HMT1 hnRNP methyltransferase-like 5(HRMT1L5), ICln-binding protein (IBP72) 72 kDa, Jak-binding protein 1 (JBP1), shk1 kinase-binding protein 1 homolog (SKB1)
UNSPSC Code:
12352200
NACRES:
NA.32
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biological source
human
recombinant
expressed in baculovirus infected insect cells
Assay
≥70% (SDS-PAGE)
form
aqueous solution
mol wt
73 kDa
packaging
pkg of 20 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
>0.02 mg/mL
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PRMT5(10419)
General description
Protein arginine methyltransferase 5 (PRMT5) also referred to as Janus kinase-binding protein 1, is encoded by the gene mapped to human chromosome 14q11.2. PRMT5 enzyme, containing 637 amino acids, belongs to type II enzymes, which is a subclass of PRMT family. PRMT5 is predominantly expressed at distinct level in various organs including heart, muscle and testis.
Human PRMT5 (GenBank Accession No. NM_006109), amino acids 2-end, with N-terminal DDDDK tag (FLAG), MW = 73kDa, expressed in a Baculovirus infected Sf9 cell expression system.
Human PRMT5 (GenBank Accession No. NM_006109), amino acids 2-end, with N-terminal DDDDK tag (FLAG), MW = 73kDa, expressed in a Baculovirus infected Sf9 cell expression system.
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Biochem/physiol Actions
Protein arginine methyltransferase 5 (PRMT5) catalyzes the symmetric dimethylation of arginine residues. It is implicated in various biological functions such as ribosome biogenesis, assembly of the Golgi apparatus, cellular differentiation, cellular proliferation, apoptosis, and germ cell specification. Irregular expression of PRMT5 leads to several type of cancers such as leukemia and lymphoma, gastric cancer, breast cancer and colorectal cancer. PRMT5 plays an important role in the regulation of cell growth, proliferation and apoptosis in epithelial ovarian cancer cell lines A2780 and SKOV3. PRMT5 enables nuclear factor-κB (NF-κB) activation via demethylating arginine 30 (R30) on the p65 subunit of NF-κB. PRMT5 participates in transcriptional regulation by methylating histones H2A, H3R8, and H4R3 as well as by inhibiting the expression of suppressor of tumorigenicity 7 (ST7), and nonmetastatic 23 (NM23) genes. PRMT5 enhances DNA damage response via methylation of tumor suppressor p53 on R333, R335, and R337 in the oligomerization domain.
Unit Definition
One unit is defined as the amount of enzyme required to methylate 1 pmol of substrate/min at 37°C.
Physical form
Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 10% glycerol and 3 mM DTT.
Preparation Note
Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Overexpression of PRMT5 promotes tumor cell growth and is associated with poor disease prognosis in epithelial ovarian cancer.
Bao X
The Journal of Histochemistry and Cytochemistry, 61(3), 206-217 (2013)
PRMT5 dimethylates R30 of the p65 subunit to activate NF-?B.
Wei H
Proceedings of the National Academy of Sciences of the USA, 110(33), 13516-13521 (2013)
Lei Huang et al.
Nature communications, 13(1), 3955-3955 (2022-07-09)
Protein arginine methyltransferase 5 (PRMT5) is the primary methyltransferase generating symmetric-dimethyl-arginine marks on histone and non-histone proteins. PRMT5 dysregulation is implicated in multiple oncogenic processes. Here, we report that PRMT5-mediated methylation of protein kinase B (AKT) is required for its
Ashok Kumar et al.
Cell reports, 32(13), 108172-108172 (2020-10-01)
Nuclear actin has been elusive due to the lack of knowledge about molecular mechanisms. From actin-containing chromatin remodeling complexes, we discovered an arginine mono-methylation mark on an evolutionarily conserved R256 residue of actin (R256me1). Actin R256 mutations in yeast affect nuclear
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