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AB271720

Recombinant Human PRMT5 + MEP50 protein (Tagged) (Biotin)

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Recombinant Human PRMT5 + MEP50 protein (Tagged) (Biotin) is a Human Full Length protein, in the 2 to 637 aa range, expressed in HEK 293 cells, with >90%, 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 + MEP50 protein (Tagged) (Biotin) (AB271720)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human PRMT5 + MEP50 protein (Tagged) (Biotin) (AB271720)

SDS-PAGE analysis of 4 μg ab271720.

Key facts

Purity

>90% SDS-PAGE

Expression system

HEK 293 cells

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Conjugation

Biotin

Excitation/Emission
Accession

O14744

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride

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>" } } }

Product details

Enzymatically biotin-labeled using Avi-tag™ technology

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"73 kDa","actualMolecularWeight":null,"aminoAcidEnd":637,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"O14744","tags":[{"tag":"DDDDK","terminus":"N-Terminus"},{"tag":"Avi","terminus":"N-Terminus"}]},{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"38 kDa","actualMolecularWeight":null,"aminoAcidEnd":342,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q9BQA1","tags":[{"tag":"His","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
Storage information
Avoid freeze / thaw cycle|Store in the dark
False

Supplementary information

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

PRMT5 also known as Protein Arginine Methyltransferase 5 and its cofactors like MEP50 (also called WDR77) regulate arginine methylation on histones and other proteins. PRMT5 is an enzyme weighing approximately 72 kDa and is expressed in various tissues including the brain heart and kidneys. MEP50 however acts as an important partner in forming the PRMT5-MEP50 complex enhancing its enzymatic activity. Together they play a significant role in symmetric dimethylation of arginine residues impacting gene expression regulation.
Biological function summary

The PRMT5 and MEP50 complex contributes to numerous cellular processes. The complex influences cellular processes by altering histone modifications which can affect chromatin structure and gene transcription. By methylating non-histone proteins it participates in RNA processing signal transduction and protein interactions. The activity of PRMT5-MEP50 is vital for maintaining cellular differentiation proliferation and apoptosis showing importance in normal developmental processes and stem cell maintenance.

Pathways

PRMT5 and MEP50 are involved in several key signaling pathways including the Wnt signaling and cell cycle regulation pathways. Within these PRMT5 collaborates with proteins like Cyclin D1 which aids in cell cycle progression. The enzyme also associates with proteins in the PI3K/AKT signaling pathway. These partnerships enable PRMT5 and MEP50 to influence important aspects of cell fate and functionality integrating signals that govern growth and division.

Aberrant PRMT5-MEP50 activity links to various cancers such as lung and breast cancer. Overexpression of PRMT5 contributes to tumorigenesis by promoting uncontrolled cell proliferation and survival. Furthermore altered methylation patterns driven by PRMT5 are involved in neurodegenerative disorders like amyotrophic lateral sclerosis (ALS). Through these conditions PRMT5 often works in tandem with proteins like p53 which regulates cell cycle and apoptosis further demonstrating the role of PRMT5 and MEP50 in disease progression and potential as therapeutic targets.

Specifications

Form

Liquid

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

Additional targets

WDR77

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