Human 3-ketodihydrosphingosine Reductase (KDSR)

<strong>Human 3-ketodihydrosphingosine Reductase (KDSR)</strong>_x000D_ <strong>Catalog number:</strong> B2015533_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 10 ug_x000D_ <strong>Molecular Weight or Concentration:</strong> 29 kDa (266 aa)_x000D_ <strong>Supplied as:</strong> Solution_x000D_ <strong>Applications:</strong> a molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20°C_x000D_ <strong>Keywords:</strong> KDS reductase, 3-dehydrosphinganine reductase, Follicular variant translocation protein 1, FVT-1, FVT1, DHSR, SDR35C1, KDSR_HUMAN_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: Liu Q, Chan AKN, Chang WH, Yang L, Pokharel SP, Miyashita K, Mattson N, Xu X, Li M, Lu W, Lin RJ, Wang SY, Chen CW. 3-Ketodihydrosphingosine reductase maintains ER homeostasis and unfolded protein response in leukemia Leukemia. 2022 Jan;36(1):100-110._x000D_ 2: Park KH, Ye ZW, Zhang J, Hammad SM, Townsend DM, Rockey DC, Kim SH. 3-ketodihydrosphingosine reductase mutation induces steatosis and hepatic injury in zebrafish Sci Rep. 2019 Feb 4;9(1):1138._x000D_ 3: Kihara A, Igarashi Y. FVT-1 is a mammalian 3-ketodihydrosphingosine reductase with an active site that faces the cytosolic side of the endoplasmic reticulum membrane J Biol Chem. 2004 Nov 19;279(47):49243-50._x000D_ 4: Krebs S, Medugorac I, Röther S, Strässer K, Förster M. A missense mutation in the 3-ketodihydrosphingosine reductase FVT1 as candidate causal mutation for bovine spinal muscular atrophy Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6746-51._x000D_ 5: Harrison PJ, Dunn TM, Campopiano DJ. Sphingolipid biosynthesis in man and microbes Nat Prod Rep. 2018 Sep 19;35(9):921-954._x000D_ 6: Boyden LM, Vincent NG, Zhou J, Hu R, Craiglow BG, Bayliss SJ, Rosman IS, Lucky AW, Diaz LA, Goldsmith LA, Paller AS, Lifton RP, Baserga SJ, Choate KA. Mutations in KDSR Cause Recessive Progressive Symmetric Erythrokeratoderma Am J Hum Genet. 2017 Jun 1;100(6):978-984._x000D_ 7: Kihara A. Synthesis and degradation pathways, functions, and pathology of ceramides and epidermal acylceramides Prog Lipid Res. 2016 Jul;63:50-69._x000D_ 8: Huber M, Chiticariu E, Bachmann D, Flatz L, Hohl D. Palmoplantar Keratoderma with Leukokeratosis Anogenitalis Caused by KDSR Mutations J Invest Dermatol. 2020 Aug;140(8):1662-1665.e1._x000D_ 9: Gupta SD, Gable K, Han G, Borovitskaya A, Selby L, Dunn TM, Harmon JM. Tsc10p and FVT1: topologically distinct short-chain reductases required for long-chain base synthesis in yeast and mammals J Lipid Res. 2009 Aug;50(8):1630-40._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/30467204">10: Bariana TK, Labarque V, Heremans J, Thys C, De Reys M, Greene D, Jenkins B, Grassi L, Seyres D, Burden F, Whitehorn D, Shamardina O, Papadia S, Gomez K, BioResource N, Van Geet C, Koulman A, Ouwehand WH, Ghevaert C, Frontini M, Turro E, Freson K. Sphingolipid dysregulation due to lack of functional KDSR impairs proplatelet formation causing thrombocytopenia Haematologica. 2019 May;104(5):1036-1045. </a>_x000D_ _x000D_ <strong>Products Related to Human 3-ketodihydrosphingosine Reductase (KDSR) can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>