|Application ||WB, E|
|Reactivity||Human, Mouse, Rat|
|Description||Rabbit IgG polyclonal antibody for DPYD detection. Tested with WB, Direct ELISA in Human;Mouse;Rat.|
|Reconstitution||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Application Details||Western blot, 0.1-0.5 µg/ml|
Direct ELISA, 0.1-0.5 µg/ml
|Tissue Specificity||Found in most tissues with greatest activity found in liver and peripheral blood mononuclear cells.|
|Contents||Each vial contains 4mg Trehalose, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.|
|Immunogen||E. coli-derived human DPYD recombinant protein (Position: A356-Y511).|
|Cross Reactivity||No cross reactivity with other proteins.|
|Storage||At -20˚C; for one year. After r˚Constitution, at 4˚C; for one month. It˚Can also be aliquotted and stored frozen at -20˚C; for a longer time. Avoid repeated freezing and thawing.|
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Provided below are standard protocols that you may find useful for product applications.
DPYD (Dihydropyrimidine Dehydrogenase), also called DPD, is an enzyme that in humans is encoded by the DPYD gene. The protein encoded by this gene is a pyrimidine catabolic enzyme and the initial and rate-limiting factor in the pathway of uracil and thymidine catabolism. The structure of the DPYD gene contains 23 exons spanning about 950 kb. Using somatic cell hybrid strategies, the DPYD gene is mapped to the centromeric region of chromosome 1 between 1p22 and 1q21. By fluorescence in situ hybridization, the DPYD gene is mapped to 1p22. The highest level of DPD was found in monocytes followed by that in lymphocytes, granulocytes, and platelets, whereas no significant activity of DPD could be detected in erythrocytes. The activity of DPD in peripheral blood mononuclear cells was intermediate between that observed in monocytes and lymphocytes. By cDNA microarray, Western blot analysis, and luciferase reporter assay, the transcription factor LSF was identified as a positive regulator of DPYD.
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