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Human Polyclonal AKR1A1 Primary Antibody pour ELISA, WB - ABIN543542
Steuber, Heine, Podjarny, Klebe: Merging the binding sites of aldose and aldehyde reductase for detection of inhibitor selectivity-determining features. dans Journal of molecular biology 2008
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Human Monoclonal AKR1A1 Primary Antibody pour IHC (p), ELISA - ABIN564487
Singer, Herth, Kuhlmann, Holland-Nell, Beck-Sickinger, Hoffmann: Mapping of phosphorylation-dependent anti-tau monoclonal antibodies in immunoblots using human tau-constructs synthesized by native chemical ligation. dans Biochemical and biophysical research communications 2008
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Data (including data from studies in knockout and transgenic mice) suggest that AKR1A1 in liver is involved in bioactivation of xenobiotic/carcinogen thioacetamide (TAA); Akr1a-/- knockout mice are resistant to TAA-induced liver injury/hepatotoxicity.
prostaglandin F synthase activity of human and bovine aldo-keto reductases
AKR1A1 could be involved in the metabolism of 4-hydroxynonenal and play a role in the resistance to oxidative stress
AKR1A1 has little effect on the production of gamma-hydroxybutyrate
structure of Apo R268A human aldose reductase reveals hinges and latches that control the kinetic mechanism
the binding site residues deviating between ALR1 and ALR2 influence ligand affinity in a complex interplay, presumably involving changes of dynamic properties and differences of the solvation/desolvation balance upon ligand binding
Data (including data from studies in knockout and transgenic mice) suggest that Akr1a1 in liver is involved in bioactivation of xenobiotic/carcinogen thioacetamide (TAA); Akr1a-/- knockout mice are resistant to TAA-induced liver injury/hepatotoxicity.
Akr1A1 gene knockout mice exhibit insufficient serum ascorbic acid levels, abnormal bone development and osteoporosis.
These results suggest that Akr1a might be involved in the metabolism of steroids and other carbonyl-containing compounds.
Aldehyde reductase exerts a protective effect against carbon tetrachloride-induced hepatic steatosis by replenishing ascorbic acid via its antioxidative properties.
The crystal structure of AKR1a4 in its apo form at high resolution.
A novel mechanism of regulation of oxidative stress by ATM through modulation of SMAR1-AKR1a4 complex, is proposed.
Structure of ALR1 in ternary complex with NADPH and 3,5-dichlorosalicylic acid is reported as well as the implications for inhibitor binding and selectivity.
This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Multiple alternatively spliced transcript variants of this gene exist, all encoding the same protein.
alcohol dehydrogenase [NADP(+)] A
, alcohol dehydrogenase [NADP+] A
, aldehyde reductase-A
, aldo-keto reductase family 1 member A1-A
, aldo-keto reductase family 1, member A1 (aldehyde reductase)
, Alcohol dehydrogenase
, Aldehyde reductase
, Aldo-keto reductase family 1 member A1
, alcohol dehydrogenase [NADP(+)]
, alcohol dehydrogenase
, alcohol dehydrogenase [NADP(+)] B
, alcohol dehydrogenase [NADP+] B
, aldehyde reductase-B
, aldo-keto reductase family 1 member A1-B
, aldo-keto reductase family 1, member A1
, aldehyde reductase
, aldo-keto reductase family 1 member A1
, dihydrodiol dehydrogenase 3
, 3-DG-reducing enzyme
, alcohol dehydrogenase (NADP+)-like protein
, aldo-keto reductase family 1, member A4 (aldehyde reductase)