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Since many substrates are shared among AKR, it is generally accepted that these enzymes can functionally compensate each other in response to oxidative stress. Their overall abundances are the important factor that partially reflects the capacity of antioxidant and detoxification in tissues. In this study, the strategy was proposed for generation of Pan\u2010AKR antibodies to recognize most AKR proteins in mouse tissues. Derived from bioinformatic analysis, several consensus peptides with different potential antigenicities were synthesized, conjugated to hemocyanin from keyhole limpets and further delivered to rabbits to generate polyclonal antibodies. Three Pan\u2010AKR antibodies exhibited the immune specificities and immune sensitivities, Pan\u2010AKR\u2010P1 for AKR1B and AKR1C, Pan\u2010AKR\u2010P3 for AKR1C and Pan\u2010AKR\u2010P4 for all the AKR proteins. Pan\u2010AKR\u2010P4 antibody was employed to 2\u2010DE Western blot to examine the AKR abundances in mouse liver and kidney, resulting in seven immune\u2010reactive spots from each tissue. Protein identification with MS revealed that most immune\u2010positive spots were the members of AKR superfamily. Furthermore, Pan\u2010AKR\u2010P4 antibody was implemented to compare the different abundances of the AKR proteins in liver and kidney between normal and diabetic mice, suggesting that diabetes did cause some abnormal changes in the AKR protein abundances.<\/jats:p>","DOI":"10.1002\/pmic.200900256","type":"journal-article","created":{"date-parts":[[2009,9,21]],"date-time":"2009-09-21T08:53:18Z","timestamp":1253523198000},"page":"5090-5100","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["A new approach to monitor expression of aldo\u2013keto reductase proteins in mouse tissues"],"prefix":"10.1002","volume":"9","author":[{"given":"Shuyang","family":"Tu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yan","family":"Ren","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wei","family":"Tong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shirong","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ningzhi","family":"Xu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aruni","family":"Bhatnagar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Siqi","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2009,11,17]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj3260625"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.pharmtox.47.120505.105337"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tips.2004.03.001"},{"key":"e_1_2_6_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0891-5849(91)90192-6"},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.1002\/ijc.22933"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1002\/path.2039"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0009-2797(02)00193-X"},{"key":"e_1_2_6_9_2","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1042\/bj3430487","article-title":"Major differences exist in the function and tissue\u2010specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo\u2010keto reductase AKR1 family members","volume":"343","author":"O'Connor T.","year":"1999","journal-title":"Biochem. 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