07-404
Anti-PRMT1 Antibody
Upstate®, from rabbit
Synonyme(s) :
Anti-ANM1, Anti-HCP1, Anti-HRMT1L2, Anti-IR1B4
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A propos de cet article
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
polyclonal
Application:
western blot
Species reactivity:
mouse, human
Citations:
68
Technique(s):
western blot: suitable
Uniprot accession no.:
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Laissez-nous vous aiderNom du produit
Anti-PRMT1 Antibody, Upstate®, from rabbit
biological source
rabbit
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
polyclonal
species reactivity
mouse, human
manufacturer/tradename
Upstate®
technique(s)
western blot: suitable
isotype
IgG
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... PRMT1(3276)
Analysis Note
routinely evaluated by immunoblot in lysates from Jurkat and 3T3/A31, NIH 3T3, HeLa, and mouse ES cells
Control
Positive Antigen Control: Catalog #12-303, Jurkat cell lysate.
Positive Antigen Control: Catalog #12-303, Jurkat cell lysate.
Application
Anti-PRMT1 Antibody is a high quality Rabbit Polyclonal Antibody for the detection of PRMT1 & has been validated in WB.
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
Histones
Histones
Biochem/physiol Actions
PRMT1 doublet
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.
General description
42-44 kDa
The methylation of arginine is mediated by the Protein Arginine Methyl Transferase (PRMT) family of enzymes. These enzymes transfer the methyl group from S-adenosyl-Lmethionine to the guanidino nitrogen atoms of an arginine residue. Arginine methylation was found to be an important modification in signal transduction, transcription, RNA transport, and splicing. PRMT1, also known as HRMT1L2 and IR1B4, was isolated through its interaction with BTG1 and TIS21, proteins that are important in cell quiescence. PRMT1 is a 361 amino acid protein; its splicing variants differ at the N-terminus, giving rise to three isoforms of 343, 361, and 347 amino acids (variants 1, 2, and 3 respectively). Proteins involved in the metabolism of RNA are substrates for PRMT1, among them Sam68.
Immunogen
Peptide corresponding to residues 298-318 of human protein arginine methyltransferase 1.
Physical form
0.1M Tris-glycine, pH 7.4, 0.15M NaCl,0.05% sodium azide before the addition of glycerol to 30%
Format: Purified
Protein A purified
Preparation Note
2 years at -20°C
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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Classe de stockage
10 - Combustible liquids
wgk
WGK 1
Certificats d'analyse (COA)
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Regulation of the EBNA1 Epstein-Barr virus protein by serine phosphorylation and arginine methylation.
Shire, K; Kapoor, P; Jiang, K; Hing, MN; Sivachandran, N; Nguyen, T; Frappier, L
Journal of virology null
Markus A Kleinschmidt et al.
Nucleic acids research, 36(10), 3202-3213 (2008-04-17)
Protein arginine methyltransferases (PRMT) have been implicated in the regulation of transcription. They are recruited to promoters via interaction with transcription factors and exert their coactivator function by methylating arginine residues in histones and other chromatin proteins. Here, we employ
Dynamics of human protein arginine methyltransferase 1(PRMT1) in vivo.
Herrmann, F; Lee, J; Bedford, MT; Fackelmayer, FO
The Journal of Biological Chemistry null
SET-mediated promoter hypoacetylation is a prerequisite for coactivation of the estrogen-responsive pS2 gene by PRMT1.
Wagner, S; Weber, S; Kleinschmidt, MA; Nagata, K; Bauer, UM
The Journal of Biological Chemistry null
Arginine methylation of scaffold attachment factor A by heterogeneous nuclear ribonucleoprotein particle-associated PRMT1.
Herrmann, F; Bossert, M; Schwander, A; Akgun, E; Fackelmayer, FO
The Journal of Biological Chemistry null
Numéro d'article de commerce international
| Référence | GTIN |
|---|---|
| 07-404 | 04053252675348 |
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