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Key Documents

SRP0145

Sigma-Aldrich

PRMT5/MEP50 Active human

recombinant, expressed in FreeStyle 293-F cells, ≥60% (SDS-PAGE)

Sinônimo(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)

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About This Item

Código UNSPSC:
12352200
NACRES:
NA.32

fonte biológica

human

recombinante

expressed in FreeStyle 293-F cells

Ensaio

≥60% (SDS-PAGE)

forma

aqueous solution

peso molecular

37.5 kDa (MEP50)
73 kDa (PRMT5)

embalagem

pkg of 20 μg

fabricante/nome comercial

Sigma-Aldrich

condição de armazenamento

avoid repeated freeze/thaw cycles

concentração

>0.02 mg/mL

técnica(s)

inhibition assay: suitable

solubilidade

water: soluble

nº de adesão UniProt

aplicação(ões)

life science and biopharma

Condições de expedição

dry ice

temperatura de armazenamento

−70°C

Informações sobre genes

human ... PRMT5(10419)

Descrição geral

Research area: Cell signaling. Protein arginine methyltransferase 5 (PRMT5) and WD repeat-containing protein (WDR77) or methylosome protein- 50 (MEP-50) are part of the methylosome. PRMT5 is a type II PRMT enzyme. The gene encoding it is localized to human chromosome 14q11.2.Complex of human PRMT5 (GenBank Accession No. NM_006109), amino acid 2-end, with N-terminal FLAG®-tag, MW=73 kDa, and human MEP50 (GenBank Accession No. NM_024102), amino acid 2-end, with N-terminal His tag, MW=37.5 kDa, expressed in FreeStyle 293-F cells.

Aplicação

Recombinant PRMT5/MEP50 has been used in the detection of arginine methylation in in vitro methyltransferase assay.
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Ações bioquímicas/fisiológicas

Methylosome protein 50 (MEP50) binds to the oncogenic protein arginine methyltransferase 5 (PRMT5) and forms a complex called methylosome. This complex is involved in mono- and symmetric dimethylation of arginine, which is necessary for various biological processes. MEP50 acts as a coactivator for androgen receptor (AR) and estrogen receptor (ER). PRMT5 also methylates histones and other proteins involved in genome organization, transcription, stem cells, primordial germ cells, differentiation, the cell cycle, and spliceosome assembly. The two proteins have been associated with cancer tumorigenesis and are marked as potential oncogenes.A boost in MEP50 levels is observed in several human cancers such asastrocytoma, ovarian cancer, lung cancer, glioblastoma, breast cancer,testicular tumor, and prostate cancer.

Definição da unidade

One unit is defined as the amount of enzyme required to methylate 1 pmol of substrate/min at 37°C.

forma física

Formulated in 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 3 mM DTT, 80 μg/ml FLAG® peptide, and 20% glycerol.

Nota de preparo

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.

Informações legais

FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
FreeStyle is a trademark of Invitrogen Corp.

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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PRMT5 Is Upregulated in HTLV-1-Mediated T-Cell Transformation and Selective Inhibition Alters Viral Gene Expression and Infected Cell Survival.
Panfil AR
Viruses, 8(1), pii E7-pii E7 (2015)
MTAP deletion confers enhanced dependency on the PRMT5 arginine methyltransferase in cancer cells.
Kryukov GV
Science, 351(6278), 1214-1218 (2016)
Protein arginine methyltransferase 5 is a potential oncoprotein that upregulates G1 cyclins/cyclin-dependent kinases and the phosphoinositide 3-kinase/AKT signaling cascade.
Wei TY
Cancer Science, 103(9), 1640-1650 (2012)
The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond.
Stopa N
Cellular and Molecular Life Sciences, 72, 2041-2059 (2015)
Wen-Hsin Chang et al.
EMBO reports, 23(8), e54265-e54265 (2022-06-30)
The aggressive nature and poor prognosis of lung cancer led us to explore the mechanisms driving disease progression. Utilizing our invasive cell-based model, we identified methylthioadenosine phosphorylase (MTAP) and confirmed its suppressive effects on tumorigenesis and metastasis. Patients with low

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