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AKR1A1 产品

(Aldo-Keto Reductase Family 1, Member A1 (Aldehyde Reductase) (AKR1A1))

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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. [provided by RefSeq, Jan 2011].

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Featured AKR1A1 Categories

AKR1A1 抗体

High quality antibodies with extensive validation data.

AKR1A1 ELISA试剂盒

Reliable ELISA kits for a wide range of species.

AKR1A1 蛋白

Proteins for various applications incl. WB, ELISA, IF etc.

Recommended AKR1A1 抗体

Product
Reactivity
Application
Validations
Cat. No.
Quantity
Datasheet
Reactivity Human
Application WB, ELISA, IHC (p)
Validations
  • (3)
  • (5)
Cat. No. ABIN564487
Quantity 100 μg
Datasheet Datasheet
Reactivity Mouse, Rat
Application WB, ELISA, IHC (p), IF (cc), IF (p), IHC (fro)
Validations
  • (4)
Cat. No. ABIN872733
Quantity 100 μL
Datasheet Datasheet
Reactivity Human
Application WB, IHC, ELISA
Validations
  • (4)
Cat. No. ABIN184795
Quantity 100 μg
Datasheet Datasheet

Recommended AKR1A1 ELISA试剂盒

Product
Reactivity
Analytical Method
Validations
Cat. No.
Quantity
Datasheet
Reactivity Human
Analytical Method Quantitative Sandwich ELISA
Validations
Cat. No. ABIN6226317
Quantity 96 tests
Datasheet Datasheet

Recommended AKR1A1 蛋白

Product
Reactivity
Source
Validations
Cat. No.
Quantity
Datasheet
Reactivity Human
Source Wheat germ
Validations
  • (2)
  • (1)
Cat. No. ABIN1344742
Quantity 10 μg
Datasheet Datasheet
Reactivity Human
Source Escherichia coli (E. coli)
Validations
  • (1)
Cat. No. ABIN7121779
Quantity 50 μg
Datasheet Datasheet
Reactivity Mouse
Source Escherichia coli (E. coli)
Validations
  • (1)
Cat. No. ABIN3130069
Quantity 1 mg
Datasheet Datasheet

Latest Publications for our AKR1A1 Products

Atsriku, Hoffmann, Moghaddam, Kumar, Surapaneni: "In vitro metabolism of a novel JNK inhibitor tanzisertib: interspecies differences in oxido-reduction and characterization of enzymes involved in metabolism." in: Xenobiotica; the fate of foreign compounds in biological systems, Vol. 45, Issue 6, pp. 465-80, (2015) (PubMed).

Quiñones-Lombraña, Ferguson, Hageman Blair, Kalabus, Redzematovic, Blanco: "Interindividual variability in the cardiac expression of anthracycline reductases in donors with and without Down syndrome." in: Pharmaceutical research, Vol. 31, Issue 7, pp. 1644-55, (2014) (PubMed).

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." in: Biochemical and biophysical research communications, Vol. 367, Issue 2, pp. 318-22, (2008) (PubMed).

Bains, Takahashi, Pfeifer, Grigliatti, Reid, Riggs: "Two allelic variants of aldo-keto reductase 1A1 exhibit reduced in vitro metabolism of daunorubicin." in: Drug metabolism and disposition: the biological fate of chemicals, Vol. 36, Issue 5, pp. 904-10, (2008) (PubMed).

Takahashi, Bains, Pfeifer, Grigliatti, Reid, Riggs: "Aldo-keto reductase 1C2 fails to metabolize doxorubicin and daunorubicin in vitro." in: Drug metabolism and disposition: the biological fate of chemicals, Vol. 36, Issue 6, pp. 991-4, (2008) (PubMed).

Steuber, Heine, Podjarny, Klebe: "Merging the binding sites of aldose and aldehyde reductase for detection of inhibitor selectivity-determining features." in: Journal of molecular biology, Vol. 379, Issue 5, pp. 991-1016, (2008) (PubMed).

Gleissner, Sanders, Nadler, Ley: "Upregulation of aldose reductase during foam cell formation as possible link among diabetes, hyperlipidemia, and atherosclerosis." in: Arteriosclerosis, thrombosis, and vascular biology, Vol. 28, Issue 6, pp. 1137-43, (2008) (PubMed).

Kassner, Huse, Martin, Gödtel-Armbrust, Metzger, Meineke, Brockmöller, Klein, Zanger, Maser, Wojnowski: "Carbonyl reductase 1 is a predominant doxorubicin reductase in the human liver." in: Drug metabolism and disposition: the biological fate of chemicals, Vol. 36, Issue 10, pp. 2113-20, (2008) (PubMed).

Bohren, Brownlee, Milne, Gabbay, Harrison: "The structure of Apo R268A human aldose reductase: hinges and latches that control the kinetic mechanism." in: Biochimica et biophysica acta, Vol. 1748, Issue 2, pp. 201-12, (2005) (PubMed).

El-Kabbani, Green, Lin, Carson, Narayana, Moore, Flynn, DeLucas: "Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications." in: Acta crystallographica. Section D, Biological crystallography, Vol. 50, Issue Pt 6, pp. 859-68, (2004) (PubMed).

Synonyms and alternative names related to AKR1A1

aldo-keto reductase family 1, member A1a (aldehyde reductase) (akr1a1a), aldo-keto reductase family 1, member A1 (aldehyde reductase) (akr1a1), aldo-keto reductase family 1 member A1 (AKR1A1), aldo-keto reductase family 1, member A1b (aldehyde reductase) (akr1a1b), aldehyde reductase (AKR1A1), aldo-keto reductase family 1 member A1 (Akr1a1), aldo-keto reductase family 1, member A1 (aldehyde reductase) (Akr1a1), aldo-keto reductase family 1, member A1 (aldehyde reductase) L homeolog (akr1a1.L), 2610201A18Rik, akr1a1, AKR1A1, Akr1a4, aldr1, ALDR1, alr, ALR, Alr, ALR1, arm, ARM, dd3, DD3, zgc:100940, zgc:110225

Protein level used designations for AKR1A1

  • 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)
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