biological source
rabbit
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
human, mouse, rat
technique(s)
dot blot: suitable, immunocytochemistry: suitable, western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
dimethylation (Arg3)
Quality Level
Gene Information
human ... H4C1(8359)
mouse ... H4C1(326619)
General description
Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Histones are modified post-translationally by the actions of enzymes in both the nucleus and cytoplasm. These modifications, which include acetylation, phosphorylation, methylation, and ubiquitin-ation, occur predominantly on the N-terminal and C-terminal tails that extend beyond the nucleosome core particle. Arginine modifications of histones proteins are mediated by two classes of protein arginine methyltransferases (PRMTs), class I and II. Class I PRMTs place two methyl groups on the one nitrogen atom of the arginine guanidino group, resulting in an asymmetric modification. In contrast class II PRMTs place two methyl groups on two nitrogen atoms of the guanidino group producing a symmetric dimethylation. Although there are exceptions, asymmetric modifications are typically associated with transcription activation while symmetric modifications are most commonly associated with transcriptional repression.
~13 kDa observed. Crossreacting band at ~58 kDa has been observed in some lysates.
Immunogen
Epitope: Symmetrically dimethylated Arg3
KLH-conjugated linear peptide corresponding to human Histone H4 when symmetrically dimethylated at Arg3.
Application
Immunocytochemistry Analysis: 1:500 dilution from a representative lot detected Histone H4 in HeLa and A431 cells.
Peptide Dot Blot Analysis: 0.5 µg/mL of this antibody detected Histone H4 dimethyl Arg3 (symmetric) peptides, but did not detect Histone H4 dimethyl Arg3 (assymmetric) peptide, other modified peptides, or non-methyated histone H4 peptides.
Peptide Dot Blot Analysis: 0.5 µg/mL of this antibody detected Histone H4 dimethyl Arg3 (symmetric) peptides, but did not detect Histone H4 dimethyl Arg3 (assymmetric) peptide, other modified peptides, or non-methyated histone H4 peptides.
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
Histones
Histones
Use Anti-dimethyl-Histone H4 (Arg3) Symmetric Antibody (rabbit polyclonal antibody) validated in WB, ICC, DB to detect dimethyl-Histone H4 (Arg3) Symmetric also known as histone H4, histone cluster 4 H4.
Biochem/physiol Actions
Broad species cross-reactivity expected based on sequence similarity.
This antibody recognizes Histone H4 symmetrically dimethylated at Arg3.
Physical form
Affinity purified
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Preparation Note
Stable for 1 year at 2-8°C from date of receipt.
Analysis Note
Control
HeLa acid extract
HeLa acid extract
Evaluated by Western Blot in HeLa acid extract.
Western Blot Analysis: 0.1 µg/mL of this antibody detected Histone H4 on 10 µg of HeLa acid extract.
Western Blot Analysis: 0.1 µg/mL of this antibody detected Histone H4 on 10 µg of HeLa acid extract.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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.
未找到合适的产品?
试试我们的产品选型工具.
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity.
Ho, MC; Wilczek, C; Bonanno, JB; Xing, L; Seznec, J; Matsui, T; Carter, LG; Onikubo et al.
Testing null
Amuza Byaruhanga Lucky et al.
Communications biology, 6(1), 659-659 (2023-06-23)
Protein arginine methyltransferases (PRMTs) regulate many important cellular processes, such as transcription and RNA processing in model organisms but their functions in human malaria parasites are not elucidated. Here, we characterize PfPRMT5 in Plasmodium falciparum, which catalyzes symmetric dimethylation of
我们的科学家团队拥有各种研究领域经验,包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.
联系客户支持