Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
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 de. Additionally we are shipping Sorbitol Dehydrogenase Proteins (27) and Sorbitol Dehydrogenase Kits (25) and many more products for this protein.
Showing 10 out of 129 products:
Human Polyclonal SORD Primary Antibody for EIA, WB - ABIN954884
Szabó, Hämäläinen, Loikkanen, Moilanen, Hirvikoski, Väisänen, Paavonen, Vaarala: Sorbitol dehydrogenase expression is regulated by androgens in the human prostate. in Oncology reports 2010
Show all 3 references for ABIN954884
Mouse (Murine) Polyclonal SORD Primary Antibody for 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
Show all 2 references for ABIN250334
Mouse (Murine) Polyclonal SORD Primary Antibody for 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
Show all 2 references for ABIN185332
Mouse (Murine) Polyclonal SORD Primary Antibody for IHC, WB - ABIN3022962
Pauly, Ekstrom, Beebe, Chrunyk, Cunningham, Griffor, Kamath, Lee, Madura, Mcguire, Subashi, Wasilko, Watts, Mylari, Oates, Adams, Rath: X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase. in Structure (London, England : 1993) 2003
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 (show AKR1B1 Antibodies).
The zinc-finger protein ZAC1 (show PLAGL1 Antibodies) is up-regulated under hypertonic stress and negatively regulates expression of sorbitol dehydrogenase, allowing for accumulation of sorbitol as a compatible organic osmolyte.
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 (show AKR1B1 Antibodies)) and related (KHK (show KHK Antibodies)) pathways.
The SDH (show SARDH Antibodies) level was significantly decreased in patients with proliferative compared with non-proliferative retinopathy in both insulin (show INS Antibodies) 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 (show PLAG1 Antibodies) 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 (show DNAJC5 Antibodies) forms of yeast xylitol dehydrogenase.
Sorbitol dehydrogenase (SORD\; EC 18.104.22.168) 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