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AB268889

Recombinant Human PRMT5 protein (Tagged)

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Recombinant Human PRMT5 protein (Tagged) is a Human Full Length protein, expressed in Baculovirus infected Sf9 cells, with >80%, suitable for SDS-PAGE.

View Alternative Names

HRMT1L5, IBP72, JBP1, SKB1, PRMT5, Protein arginine N-methyltransferase 5, 72 kDa ICln-binding protein, Histone-arginine N-methyltransferase PRMT5, Jak-binding protein 1, Shk1 kinase-binding protein 1 homolog, SKB1 homolog, SKB1Hs

1 Images
SDS-PAGE - Recombinant Human PRMT5 protein (Tagged) (AB268889)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human PRMT5 protein (Tagged) (AB268889)

SDS-PAGE analysis of ab268889.

Key facts

Purity

>80% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

O14744

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"O14744","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PRMT5 also known as Protein Arginine Methyltransferase 5 is an enzyme with molecular weight approximately 72 kDa. This protein catalyzes symmetric dimethylation of arginine residues on target proteins affecting gene expression and signal transduction. PRMT5 is expressed in various tissues with significant presence in the brain pancreas and lung. It enhances methyltransferase activity by interacting with other proteins and substrates.
Biological function summary

PRMT5 influences numerous cellular processes including RNA processing signal transduction and DNA repair. It functions as part of a protein complex often involving MEP50/WDR77 which modulates its methylating activity on histones and other proteins. This interaction dictates the cellular roles that are central to maintaining normal cellular function and regulation.

Pathways

PRMT5 operates within the Wnt/β-catenin signaling and mTOR pathways among others. As it modulates the methylation of transcription factors and regulators it contributes to transcriptional repression or activation which is important for cellular proliferation and differentiation. PRMT5 interacts with proteins such as Smad7 and cyclin D1 influencing these signaling pathways.

PRMT5 shows significant associations with cancer and neurological disorders. Elevated levels of PRMT5 correlate with the progression of various cancers including lung and breast cancers making it a potential target for therapeutic intervention. Additionally PRMT5's interaction with oncogenic proteins like MYC and MDM4 highlights its role in tumorigenesis. Furthermore PRMT5 dysregulation is linked to neurodegenerative diseases impacting the protein's target specificity and exacerbating disease symptoms.

Specifications

Form

Liquid

Additional notes

Affinity purified.

General info

Function

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed : 10531356, PubMed : 11152681, PubMed : 11747828, PubMed : 12411503, PubMed : 15737618, PubMed : 17709427, PubMed : 20159986, PubMed : 20810653, PubMed : 21081503, PubMed : 21258366, PubMed : 21917714, PubMed : 22269951). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles (PubMed : 11747828, PubMed : 12411503, PubMed : 17709427). Methylates SUPT5H and may regulate its transcriptional elongation properties (PubMed : 12718890). May methylate the N-terminal region of MBD2 (PubMed : 16428440). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development (By similarity). Methylates histone H3 'Arg-8', which may repress transcription (By similarity). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation (PubMed : 21258366, PubMed : 21917714). Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed : 21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9 (PubMed : 22269951). Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (PubMed : 20810653). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation (PubMed : 20421892). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed : 25284789). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed : 26700805). Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression (PubMed : 25092918). Symmetrically methylates NCL (PubMed : 21081503). Methylates p53/TP53; methylation might possibly affect p53/TP53 target gene specificity (PubMed : 19011621). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 (By similarity).

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.

Subcellular localisation

Nucleus

Product protocols

Target data

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed : 10531356, PubMed : 11152681, PubMed : 11747828, PubMed : 12411503, PubMed : 15737618, PubMed : 17709427, PubMed : 20159986, PubMed : 20810653, PubMed : 21081503, PubMed : 21258366, PubMed : 21917714, PubMed : 22269951). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles (PubMed : 11747828, PubMed : 12411503, PubMed : 17709427). Methylates SUPT5H and may regulate its transcriptional elongation properties (PubMed : 12718890). May methylate the N-terminal region of MBD2 (PubMed : 16428440). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development (By similarity). Methylates histone H3 'Arg-8', which may repress transcription (By similarity). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation (PubMed : 21258366, PubMed : 21917714). Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed : 21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9 (PubMed : 22269951). Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (PubMed : 20810653). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation (PubMed : 20421892). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed : 25284789). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed : 26700805). Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression (PubMed : 25092918). Symmetrically methylates NCL (PubMed : 21081503). Methylates p53/TP53; methylation might possibly affect p53/TP53 target gene specificity (PubMed : 19011621). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 (By similarity).
See full target information PRMT5

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