SRP0322
JMJD6 human
recombinant, expressed in baculovirus infected Sf9 cells, ≥80% (SDS-PAGE)
Synonym(s):
Jumonji domain-containing protein 6, PSR, PTDSR
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About This Item
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biological source
human
recombinant
expressed in baculovirus infected Sf9 cells
Assay
≥80% (SDS-PAGE)
form
aqueous solution
mol wt
74 kDa
packaging
pkg of 20 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
1.87 mg/mL
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... JMJD6(23210)
General description
Human JMJD6 (Jumonji domain containing 6), also known as PTDSR (GenBank Accession No. NM_001081461), amino-acids 2-414 (end) with an N-terminal GST-tag, MW=74 kDa, expressed in a Baculovirus-infected Sf9 cell expression system.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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PloS one, 5(10), e13769-e13769 (2010-11-10)
Methylation of residues in histone tails is part of a network that regulates gene expression. JmjC domain containing proteins catalyze the oxidative removal of methyl groups on histone lysine residues. Here, we report studies to test the involvement of Jumonji
Science (New York, N.Y.), 318(5849), 444-447 (2007-10-20)
Arginine methylation occurs on a number of proteins involved in a variety of cellular functions. Histone tails are known to be mono- and dimethylated on multiple arginine residues where they influence chromatin remodeling and gene expression. To date, no enzyme
Science (New York, N.Y.), 325(5936), 90-93 (2009-07-04)
The finding that the metazoan hypoxic response is regulated by oxygen-dependent posttranslational hydroxylations, which regulate the activity and lifetime of hypoxia-inducible factor (HIF), has raised the question of whether other hydroxylases are involved in the regulation of gene expression. We
Oncogene, 38(7), 980-997 (2018-09-07)
Overexpression of Jumonji domain-containing 6 (JMJD6) has been reported to be associated with more aggressive breast cancer characteristics. However, the precise role of JMJD6 in breast cancer development remains unclear. Here, we demonstrate that JMJD6 has intrinsic tyrosine kinase activity
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 31(12), 5356-5370 (2017-08-10)
JMJD6 is known to localize in the nucleus, exerting histone arginine demethylase and lysyl hydroxylase activities. A novel localization of JMJD6 in the extracellular matrix, resulting from its secretion as a soluble protein, was unveiled by a new anti-JMJD6 mAb
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