SRP0383
EHMT1 human
recombinant, expressed in E. coli, ≥63% (SDS-PAGE)
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Synonym(s):
EHMT1, KMT1D
UNSPSC Code:
12352200
NACRES:
NA.32
biological source
human
recombinant
expressed in E. coli
Assay
≥63% (SDS-PAGE)
form
aqueous solution
mol wt
72.4 kDa
packaging
pkg of 50 μg
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... EHMT1(79813)
General description
Human euchromatic histone-lysine N-methyltransferase (EHMT1), also known as G9a-like protein (GLP) or KMT1D, (GenBank Accession No. NM_024757), amino acids 894-1298 (end) with N-terminal GST-tag, MW= 72.4 kDa, expressed in an E. coli expression system.
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Bassant Orabi et al.
Heart failure reviews, 23(3), 363-376 (2018-04-24)
Glucagon-like peptide-1 (GLP-1) agonists and dipeptidyl peptidase-4 (DPP-4) inhibitors produce some beneficial and deleterious effects in diabetic patients not mediated by their glycemic lowering effects, and there is a need for better understanding of the molecular basis of these effects.
Yukihiro Itoh et al.
Scientific reports, 9(1), 767-767 (2019-01-27)
In the context of drug design, C-H···O hydrogen bonds have received little attention so far, mostly because they are considered weak relative to other noncovalent interactions such as O-H···O hydrogen bonds, π/π interactions, and van der Waals interactions. Herein, we
Levi Todd et al.
The Journal of comparative neurology, 524(1), 74-89 (2015-06-09)
Retinal progenitors in the circumferential marginal zone (CMZ) and Müller glia-derived progenitors have been well described for the eyes of fish, amphibians, and birds. However, there is no information regarding a CMZ and the nature of retinal glia in species
Jing Huang et al.
The Journal of biological chemistry, 285(13), 9636-9641 (2010-02-02)
The tumor suppressor p53 is regulated by numerous post-translational modifications. Lysine methylation has recently emerged as a key post-translational modification that alters the activity of p53. Here, we describe a novel lysine methylation site in p53 that is carried out
Jun Ueda et al.
The Journal of biological chemistry, 281(29), 20120-20128 (2006-05-17)
G9a is a SET-domain mammalian histone methyltransferase responsible for mono- and dimethylation of lysine 9 in histone H3 (H3K9) at euchromatic regions. Recently we reported that G9a forms a stoichiometric heteromeric complex with another SET-domain-containing molecule, GLP/Eu-HMTase1. Although G9a and
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