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SRP0400

Sigma-Aldrich

PRMT4 peptide, biotin

≥90% (HPLC)

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

assay

≥90% (HPLC)

form

aqueous solution

packaging

pkg of 80 nmol

concentration

400 μM

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... CARM1(10498)

General description

Protein arginine methyltransferase 4 (PRMT4), which is also known as coactivator associated arginine methyltransferase 1 (CARM1), is part of the protein arginine methyltransferase (PRMT) family. The gene encoding this protein is localized on human chromosome 19p13.2.

Application

Study enzyme kinetics, and screen small molecular inhibitors of PRMT4 histone methyltransferase for drug discovery and HTS applications.

Biochem/physiol Actions

Protein arginine methyltransferase 4 (PRMT4) methylates arginine residues of histones and other proteins and thus has a role in modulation of gene expression. The protein also methylates histone acetyl transferases. It has been shown to associate with Mi2a, a chromatin remodeler. It also associates with nuclear factor-κB (NF-κB), estrogen receptor and tumor suppressor p53 and is recruited to specific target genes. PRMT4 has a role in pre-mRNA splicing and DNA damage response. The protein has been shown to be upregulated in liver, prostate and breast cancers.

Physical form

Supplied in a TRIS-buffered solution.

Other Notes

200 μL at 400 μM, or 80 nmol. Sold as 80 nmol

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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PRMT4 Is a Novel Coactivator of c-Myb-Dependent Transcription in Haematopoietic Cell Lines
Gundula Streubel
PLoS Genetics, 9(3), e1003343-e1003343 (2013)
High-resolution genomic profiling of Philadelphia chromosome-positive (Ph+) acute lymphoblastic leukemia (ALL) patients identified novel recurrent copy number variations involved in both pathogenesis and resistance to tyrosine kinase inhibitors
Ilaria Lacobucci
Cancer Research, 68(9) (2008)
CARM1 Preferentially Methylates H3R17 over H3R26 through a Random Kinetic Mechanism.
Jacques SL
Biochemistry, 55(11), 1635-1644 (2016)

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