05-808
Anti-dimethyl-Histone H3 (Arg2) Antibody, rabbit monoclonal
Upstate®, from rabbit
Sinônimo(s):
H3R2me2, Histone H3 (di methyl R2)
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About This Item
Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Produtos recomendados
fonte biológica
rabbit
Nível de qualidade
forma do anticorpo
purified antibody
tipo de produto de anticorpo
primary antibodies
clone
monoclonal
reatividade de espécies
human
fabricante/nome comercial
Upstate®
técnica(s)
dot blot: suitable
inhibition assay: suitable (peptide)
multiplexing: suitable
western blot: suitable
Isotipo
IgG
nº de adesão NCBI
nº de adesão UniProt
Condições de expedição
wet ice
modificação pós-traducional do alvo
dimethylation (Arg2)
Informações sobre genes
human ... H3C1(8350)
Descrição geral
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.
Imunogênio
peptide containing the sequence AdimRTKQ, corresponding to dimethyl-arginine 2 of human histone H3.
Aplicação
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).
Qualidade
routinely evaluated in acid-extracted proteins from HeLa cells
Descrição-alvo
17kDa
forma física
Format: Purified
Nota de análise
Control
Acid extracts from HeLa cells
Acid extracts from HeLa cells
Informações legais
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 1
Certificados de análise (COA)
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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
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
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
Analysis of histones in Xenopus laevis. I. A distinct index of enriched variants and modifications exists in each cell type and is remodeled during developmental transitions.
Shechter, D; Nicklay, JJ; Chitta, RK; Shabanowitz, J; Hunt, DF; Allis, CD
The Journal of Biological Chemistry null
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