Human AKR1B10 Protein (Highly Pure)

<strong>Human AKR1B10 Protein (Highly Pure)</strong>_x000D_ <strong>Catalog number:</strong> B2011563_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 100 µg_x000D_ <strong>Molecular Weight or Concentration:</strong> 1 mg/mL_x000D_ <strong>Supplied as:</strong> Solution_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20 °C_x000D_ <strong>Keywords:</strong> AKR1B10 protein, Purified recombinant Human AKR1B10 protein, AKRB0 1, AKR1B12 protein, member B10 protein, AKRB0-1 protein, AKR1B10 protein, HIS protein, SI reductase protein, HIS protein, Aldose reductase related protein , AKR1B10, AKRB0-1, ARL1 protein, Aldo-keto reductase family 1 protein, Small intestine_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Li J, Guo Y, Duan L, Hu X, Zhang X, Hu J, Huang L, He R, Hu Z, Luo W, Tan T, Huang R, Liao D, Zhu YS, Luo DX. AKR1B10 promotes breast cancer cell migration and invasion via activation of ERK signaling Oncotarget. 2017 May 16;8(20):33694-33703._x000D_ 2: Penning TM. The aldo-keto reductases (AKRs): Overview Chem Biol Interact. 2015 Jun 5;234:236-46._x000D_ 3: Govaere O, Cockell S, Tiniakos D, Queen R, Younes R, Vacca M, Alexander L, Ravaioli F, Palmer J, Petta S, Boursier J, Rosso C, Johnson K, Wonders K, Day CP, Ekstedt M, Orešič M, Darlay R, Cordell HJ, Marra F, Vidal-Puig A, Bedossa P, Schattenberg JM, Clément K, Allison M, Bugianesi E, Ratziu V, Daly AK, Anstee QM. Transcriptomic profiling across the nonalcoholic fatty liver disease spectrum reveals gene signatures for steatohepatitis and fibrosis Sci Transl Med. 2020 Dec 2;12(572):eaba4448._x000D_ 4: Endo S, Matsunaga T, Nishinaka T. The Role of AKR1B10 in Physiology and Pathophysiology Metabolites. 2021 May 21;11(6):332._x000D_ 5: Endo S, Matsunaga T, Mamiya H, Ohta C, Soda M, Kitade Y, Tajima K, Zhao HT, El-Kabbani O, Hara A. Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids Arch Biochem Biophys. 2009 Jul 1;487(1):1-9._x000D_ 6: Rohde K, Federbusch M, Horstmann A, Keller M, Villringer A, Stumvoll M, Tönjes A, Kovacs P, Böttcher Y. Genetic variants in AKR1B10 associate with human eating behavior BMC Genet. 2015 Mar 25;16:31._x000D_ 7: Luo D, Bu Y, Ma J, Rajput S, He Y, Cai G, Liao DF, Cao D. Heat shock protein 90-α mediates aldo-keto reductase 1B10 (AKR1B10) protein secretion through secretory lysosomes J Biol Chem. 2013 Dec 20;288(51):36733-40._x000D_ 8: Liu X, Hu Z, Qu J, Li J, Gong K, Wang L, Jiang J, Li X, He R, Duan L, Luo W, Xia C, Luo D. AKR1B10 confers resistance to radiotherapy via FFA/TLR4/NF-κB axis in nasopharyngeal carcinoma Int J Biol Sci. 2021 Feb 3;17(3):756-767._x000D_ 9: Soda M, Endo S, Matsunaga T, Zhao HT, El-Kabbani O, Iinuma M, Yamamura K, Hara A. Inhibition of human aldose reductase-like protein (AKR1B10) by α- and γ-mangostins, major components of pericarps of mangosteen Biol Pharm Bull. 2012;35(11):2075-80._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/28286104">10: Jung YJ, Lee EH, Lee CG, Rhee KJ, Jung WS, Choi Y, Pan CH, Kang K. AKR1B10-inhibitory Selaginella tamariscina extract and amentoflavone decrease the growth of A549 human lung cancer cells in vitro and in vivo J Ethnopharmacol. 2017 Apr 18;202:78-84. </a>_x000D_ _x000D_ <strong>Products Related to Human AKR1B10 Protein (Highly Pure) can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>