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A rapid divergent evolution (zeige DHRS4 Proteine) brought the human DHRS2 gene, duplicated form of the DHRS4 one, to code a SDR (zeige DHRS4 Proteine)enzyme having subcellular localization, synthesis regulation and specialized cellular functions very different from those o (zeige DHRS4 Proteine)f the human DHRS4 enzyme.
Complete genomic organization of DHRS2, including two alternative promoter regions: a hepatocyte-specific promoter and a monocyte-derived dendritic cell-specific promoter
c-Myb proto-oncogene (zeige MYB Proteine) has a tumor suppressor role in breast cancer via c-Myb (zeige MYB Proteine) controlled DHRS2 (HEP27) expression.
Hep27 is regulated at the transcriptional level by the proto-oncogene c-Myb (zeige MYB Proteine) and is required for c-Myb (zeige MYB Proteine)-induced p53 (zeige TP53 Proteine) stabilization.
Molecular cloning, sequence and Chr 14 localization of the DHRS2 gene. Nuclear and cytoplasmic localization and normal tissue distribution of the DHRS2-encoded Hep27 protein.
The synthesis of the nuclear protein (zeige RDBP Proteine) D (Hep27 protein old name) is up-regulated in growth-inhibited HepG2 cells and is inhibited during DNA synthesis.
In human endometrial carcinoma cells, the Hep27 protein encoded by DHRS2 is specifically upregulated in mitochondria by the ERM/ETV5 (zeige ETV5 Proteine) transcription factor and Hep27 has a protective role against apoptosis induced by oxidative stress.
Hep27 a cell-cycle regulated protein belongs to the SDR family (short-chain dehydrogenase/reductase family).
Hep27 is a NADPH-dependent dicarbonyl reductase enzyme active on xenobiotics.
M. musculus DHRS2 and DHRS4 (zeige DHRS4 Proteine) genes are syntenic outparalogs that originated from a duplication of the DHRS4 (zeige DHRS4 Proteine) gene that took place before the formation of the mammalian clade. M. musculus genes are orthologs of human DHRS2 and DHRS4 (zeige DHRS4 Proteine) genes respectively.
Functional analysis of the human Dhrs2 ortholog.
Displays NADPH-dependent dicarbonyl reductase activity in vitro with 3,4-Hexanedione, 2,3-Heptanedione and 1-Phenyl-1,2- propanedione as substrates. No reductase activity is displayed in vitro with steroids, retinoids and sugars as substrates. May inhibit cell replication.
dehydrogenase/reductase SDR family member 4
, dehydrogenase/reductase SDR family member 2, mitochondrial
, dehydrogenase/reductase member 2
, dicarbonyl reductase HEP27
, protein D
, short chain dehydrogenase/reductase family 25C, member 1
, short-chain alcohol dehydrogenase family member
, SDR family member