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Sorbitol dehydrogenase (SORD; EC 184.108.40.206) catalyzes the interconversion of polyols and their corresponding ketoses, and together with aldose reductase (ALDR1; MIM 103880), makes up the sorbitol pathway that is believed to play an important role in the de. Zusätzlich bieten wir Ihnen Sorbitol Dehydrogenase Kits (35) und Sorbitol Dehydrogenase Proteine (27) und viele weitere Produktgruppen zu diesem Protein an.
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Mouse (Murine) Polyclonal SORD Primary Antibody für ELISA, WB - ABIN250334
Karacao?lan, Ozer: Steady-state kinetic properties of sorbitol dehydrogenase from chicken liver. in Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology 2005
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Mouse (Murine) Polyclonal SORD Primary Antibody für ELISA, WB - ABIN185332
Cao, Aghajanian, Haig-Ladewig, Gerton: Sorbitol can fuel mouse sperm motility and protein tyrosine phosphorylation via sorbitol dehydrogenase. in Biology of reproduction 2008
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Human Monoclonal SORD Primary Antibody für IHC (p), ELISA - ABIN562952
Szabó, Hämäläinen, Loikkanen, Moilanen, Hirvikoski, Väisänen, Paavonen, Vaarala: Sorbitol dehydrogenase expression is regulated by androgens in the human prostate. in Oncology reports 2010
Human Polyclonal SORD Primary Antibody für IHC, IHC (p) - ABIN4355163
Uzozie, Nanni, Staiano, Grossmann, Barkow-Oesterreicher, Shay, Tiwari, Buffoli, Laczko, Marra: Sorbitol dehydrogenase overexpression and other aspects of dysregulated protein expression in human precancerous colorectal neoplasms: a quantitative proteomics study. in Molecular & cellular proteomics : MCP 2014
Nicotine-induced reduced expression of Sord could be involved in impaired secretory functions of the epididymis.
Knockout mice had the highest sorbitol content among various genetic types including mice wwith human aldose reductase (zeige AKR1B1 Antikörper).
The zinc-finger protein ZAC1 (zeige PLAGL1 Antikörper) is up-regulated under hypertonic stress and negatively regulates expression of sorbitol dehydrogenase, allowing for accumulation of sorbitol as a compatible organic osmolyte.
SDH (zeige SARDH Antikörper) gene expression was increased by hypoxia and oxidative stress, but not extracellular hyperosmolarity. Hyperosmolarity and hypoxia did not alter the SDH (zeige SARDH Antikörper) protein level.
One of the most striking changes involved sorbitol dehydrogenase, a key enzyme in the polyol pathway. Validation studies revealed dramatically increased sorbitol dehydrogenase concentrations and activity in adenomas and cancer cell lines, along with important changes in the expression of other enzymes in the same (AKR1B1 (zeige AKR1B1 Antikörper)) and related (KHK (zeige KHK Antikörper)) pathways.
The SDH (zeige SARDH Antikörper) level was significantly decreased in patients with proliferative compared with non-proliferative retinopathy in both insulin (zeige INS Antikörper) and oral diabetic groups.
Thus, our findings suggest that the -888G > C polymorphism in the SORD gene is not involved in the pathogenesis of diabtic retinopathy in type 2 diabetes.
The expression of SORD is regulated by androgens in human prostate. In prostate cancer, increased immunostaining was associated with high Gleason patterns and high serum PSA concentrations.
crystals of sorbitol dehydrogenase belong to the monoclinic C2 space group, with unit-cell parameters a = 145.9, b = 52.3, c = 169.0 A, beta = 101.8 degrees
Sorbitol dehydrogenase (SDH), a member of the medium-chain dehydrogenase/reductase protein family and the second enzyme of the polyol pathway of glucose metabolism, converts sorbitol to fructose strictly using NAD(+) as coenzyme.
Results compare the catalytic mechanism of liver sorbitol dehydrogenase with wild-type and Glu154-->Cys (zeige DNAJC5 Antikörper) forms of yeast xylitol dehydrogenase.
Sorbitol dehydrogenase (SORD\; EC 220.127.116.11) catalyzes the interconversion of polyols and their corresponding ketoses, and together with aldose reductase (ALDR1\; MIM 103880), makes up the sorbitol pathway that is believed to play an important role in the development of diabetic complications (summarized by Carr and Markham, 1995
, L-iditol 2-dehydrogenase
, mammalian sorbitol dehydrogenase homolog
, sorbitol dehydrogenase 1