HPA018976

Sigma-Aldrich

Anti-PRMT2 antibody produced in rabbit

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):
Anti-Protein arginine N-methyltransferase 2
Human Protein Atlas Number:

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

mouse, human, rat

application(s)

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500

immunogen sequence

LRFDIRKAGTLHGFTAWFSVHFQSLQEGQPPQVLSTGPFHPTTHWKQTLFMMDDPVPVHTGDVVTGSVVLQRNPVWRRHMSVALSW

conjugate

unconjugated

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... PRMT2(3275)

General description

The gene PRMT2 (protein arginine N-methyltransferase 2) is mapped to human chromosome 21q22.3. It belongs to the arginine methyltransferase protein family. The protein shuttles between the cytoplasm and nucleus. PRMT2 is also referred as HRMT1L1 (histone-arginine N-methyltransferase).

Immunogen

Protein arginine N-methyltransferase 2 recombinant protein epitope signature tag (PrEST)

Biochem/physiol Actions

PRMT2 (protein arginine N-methyltransferase 2) methylates arginine residues within proteins using S-adenosyl-L-methionine. It methylates histone H4 and acts as a transcription co-activator. PRMT2 is a co-activator of the androgen receptor and ERα (Estrogen erceptor α). PRMT2 interacts with PRMT1 and promotes PRMT1 enzymatic activity.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST73894.

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Sigma-Aldrich Co. LLC

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Rene Meyer et al.
The Journal of steroid biochemistry and molecular biology, 107(1-2), 1-14 (2007-06-26)
The basal transcriptional activity of nuclear receptors (NRs) is regulated by interactions with additional comodulator proteins (coactivator/corepressor). Here, we describe a new androgen receptor (AR)-associated coactivator, PRMT2, which belongs to the arginine methyltransferase protein family. To search for AR-interacting proteins...
Lakshmanan Ganesh et al.
Molecular and cellular biology, 26(10), 3864-3874 (2006-05-02)
The protein arginine methyltransferases (PRMTs) include a family of proteins with related putative methyltransferase domains that modify chromatin and regulate cellular transcription. Although some family members, PRMT1 and PRMT4, have been implicated in transcriptional modulation or intracellular signaling, the roles...
Ted M Lakowski et al.
The Biochemical journal, 421(2), 253-261 (2009-05-02)
Protein arginine N-methyltransferases (PRMTs) methylate arginine residues within proteins using S-adenosyl-L-methionine (AdoMet) to form S-adenosyl-L-homocysteine and methylarginine residues. All PRMTs produce omega-NG-monomethylarginine (MMA) residues and either asymmetric omega-N(G),N(G)-dimethylarginine (aDMA) or symmetric omega-N(G),N'(G)-dimethylarginine (sDMA) residues, referred to as Type I or...
G Poelmans et al.
American journal of medical genetics. Part B, Neuropsychiatric genetics : the official publication of the International Society of Psychiatric Genetics, 150B(1), 140-147 (2008-06-04)
Dyslexia is the most common childhood learning disorder and it is a significantly heritable trait. At least nine chromosomal loci have been linked to dyslexia, and additional susceptibility loci on other chromosomes have been suggested. Within two of these loci...
Joyce Sayegh et al.
The Journal of biological chemistry, 282(50), 36444-36453 (2007-10-11)
Human protein arginine methyltransferase PRMT8 has been recently described as a type I enzyme in brain that is localized to the plasma membrane by N-terminal myristoylation. The amino acid sequence of human PRMT8 is almost 80% identical to human PRMT1...

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

MilliporeSigma

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.