05-808
Anti-dimethyl-Histone H3 (Arg2) Antibody, rabbit monoclonal
Upstate®, from rabbit
Synonym(s):
H3R2me2, Histone H3 (di methyl R2)
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
monoclonal
species reactivity
human
manufacturer/tradename
Upstate®
technique(s)
dot blot: suitable
inhibition assay: suitable (peptide)
multiplexing: suitable
western blot: suitable
isotype
IgG
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
dimethylation (Arg2)
Gene Information
human ... H3C1(8350)
General description
Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the ′beads on a string′ structure.
The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine.
The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine.
Immunogen
peptide containing the sequence AdimRTKQ, corresponding to dimethyl-arginine 2 of human histone H3.
Application
Use Anti-dimethyl-Histone H3 (Arg2) Antibody (Rabbit Monoclonal Antibody) validated in DB, WB, PIA, Mplex to detect dimethyl-Histone H3 (Arg2) also known as H3R2me2, Histone H3 (di methyl R2).
Quality
routinely evaluated in acid-extracted proteins from HeLa cells
Target description
17kDa
Physical form
Format: Purified
Analysis Note
Control
Acid extracts from HeLa cells
Acid extracts from HeLa cells
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
Certificates of Analysis (COA)
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Lessly P Sepulveda-Rincon et al.
Biology of reproduction, 95(6), 123-123 (2016-10-21)
The first lineage specification during mammalian embryo development can be visually distinguished at the blastocyst stage. Two cell lineages are observed on the embryonic-abembryonic axis of the blastocyst: the inner cell mass and the trophectoderm. The timing and mechanisms driving
Zichuan Liu et al.
Developmental biology, 368(2), 304-311 (2012-06-05)
Several research groups have suggested that the embryonic-abembryonic (Em-Ab) axis in the mouse can be predicted by the first cleavage plane of the early embryo. Currently, it is not known whether this early patterning occurs in cloned embryos produced by
Sitaram Gayatri et al.
Scientific reports, 6, 28718-28718 (2016-06-25)
Signal transduction in response to stimuli relies on the generation of cascades of posttranslational modifications that promote protein-protein interactions and facilitate the assembly of distinct signaling complexes. Arginine methylation is one such modification, which is catalyzed by a family of
Alessandra Di Lorenzo et al.
Nucleic acids research, 42(13), 8297-8309 (2014-06-19)
Protein arginine methyltransferase 6 (PRMT6) is a nuclear enzyme that modifies histone tails. To help elucidate the biological function of PRMT6 in vivo, we generated transgenic mice that ubiquitously express PRMT6 fused to the hormone-binding portion of the estrogen receptor
Ayaz Ahmad et al.
PloS one, 6(8), e22664-e22664 (2011-08-20)
Post-translational methylation of arginine residues profoundly affects the structure and functions of protein and, hence, implicated in a myriad of essential cellular processes such as signal transduction, mRNA splicing and transcriptional regulation. Protein arginine methyltransferases (PRMTs), the enzymes catalyzing arginine
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