P4995
Anti-PRMT4 antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous solution
别名:
Anti-CARM1, Anti-Protein-Arginine Methyl Transferase 4
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关于此项目
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ARR, IP, WB
Citations:
5
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~50 kDa
species reactivity
human
concentration
~1 mg/mL
technique(s)
immunoprecipitation (IP): 5-20 μg using PRMT4-fusion protein from extracts of transfected 293T cells., microarray: suitable, western blot: 0.5-1 μg/mL using nuclear extracts of the MCF7 breast carcinoma cell line.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CARM1(10498)
mouse ... Carm1(59035)
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.
Immunogen
synthetic peptide corresponding to amino acids 48-63 of human PRMT4 conjugated to KLH via a C-terminal added lysine residue. The sequence is conserved in mouse.
Application
Anti-PRMT4 antibody produced in rabbit has been used for Western Blotting and immunofluorescence.
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 Mi2α, 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.
Protein-arginine methyl transferase 4 (PRMT4) plays a central role in upregulation of transcription by nuclear hormone receptors (NRs).
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.
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.
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存储类别
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
新产品
此项目有
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 Iacobucci
Cancer Research, 68(9) (2008)
Coactivator-Associated Arginine Methyltransferase 1 Enhances Transcriptional Activity of the Human T-Cell Lymphotropic Virus Type 1 Long Terminal Repeat through Direct Interaction with Tax
Jeong SJ, et al.
Journal of Virology, 80, 10036-10044 (2006)
Mapping of Post-translational Modifications of Transition Proteins, TP1 and TP2, and Identification of Protein Arginine Methyltransferase 4 and Lysine Methyltransferase 7 as Methyltransferase for TP2*
Nikhil Gupta
The Journal of Biological Chemistry, 12101-12122 (2015)
CARM1 Preferentially Methylates H3R17 over H3R26 through a Random Kinetic Mechanism.
Jacques SL
Biochemistry, 55(11), 1635-1644 (2016)
Nikhil Gupta et al.
The Journal of biological chemistry, 290(19), 12101-12122 (2015-03-31)
In a unique global chromatin remodeling process during mammalian spermiogenesis, 90% of the nucleosomal histones are replaced by testis-specific transition proteins, TP1, TP2, and TP4. These proteins are further substituted by sperm-specific protamines, P1 and P2, to form a highly
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