Human Argininosuccinate Lyase
<strong>Human Argininosuccinate Lyase</strong>_x000D_ <strong>Catalog number:</strong> B2012516_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 100 ug_x000D_ <strong>Molecular Weight or Concentration:</strong> 79.5 kDa_x000D_ <strong>Supplied as:</strong> Lyophilized Powder_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20°C_x000D_ <strong>Keywords:</strong> Argininosuccinate lyase Protein, Human_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Du D, Liu C, Qin M, Zhang X, Xi T, Yuan S, Hao H, Xiong J. Metabolic dysregulation and emerging therapeutical targets for hepatocellular carcinoma Acta Pharm Sin B. 2022 Feb;12(2):558-580._x000D_ 2: Nagamani SCS, Erez A, Lee B. Argininosuccinate Lyase Deficiency 2011 Feb 3 [updated 2019 Mar 28]. In: Adam MP, Everman DB, Mirzaa GM, Pagon RA, Wallace SE, Bean LJH, Gripp KW, Amemiya A, editors. GeneReviews(®) [Internet]. Seattle (WA): University of Washington, Seattle; 1993–2022._x000D_ 3: Matsumoto S, Häberle J, Kido J, Mitsubuchi H, Endo F, Nakamura K. Urea cycle disorders-update J Hum Genet. 2019 Sep;64(9):833-847._x000D_ 4: Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL. Regulation of cellular metabolism by protein lysine acetylation Science. 2010 Feb 19;327(5968):1000-4._x000D_ 5: Nagamani SC, Erez A, Lee B. Argininosuccinate lyase deficiency Genet Med. 2012 May;14(5):501-7._x000D_ 6: Vande Voorde J, Ackermann T, Pfetzer N, Sumpton D, Mackay G, Kalna G, Nixon C, Blyth K, Gottlieb E, Tardito S. Improving the metabolic fidelity of cancer models with a physiological cell culture medium Sci Adv. 2019 Jan 2;5(1):eaau7314._x000D_ 7: O'Brien WE, Barr RH. Argininosuccinate lyase: purification and characterization from human liver Biochemistry. 1981 Mar 31;20(7):2056-60._x000D_ 8: Yu Y, Terada K, Nagasaki A, Takiguchi M, Mori M. Preparation of recombinant argininosuccinate synthetase and argininosuccinate lyase: expression of the enzymes in rat tissues J Biochem. 1995 May;117(5):952-7._x000D_ 9: Davidson JS, Baumgarten IM, Harley EH. Metabolic cooperation between argininosuccinate synthetase and argininosuccinate lyase deficient human fibroblasts Exp Cell Res. 1984 Feb;150(2):367-78._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/24166829">10: Balmer C, Pandey AV, Rüfenacht V, Nuoffer JM, Fang P, Wong LJ, Häberle J. Mutations and polymorphisms in the human argininosuccinate lyase (ASL) gene Hum Mutat. 2014 Jan;35(1):27-35. </a>_x000D_ _x000D_ <strong>Products Related to Human Argininosuccinate Lyase can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>
Product Specifications
Short Description
Catalog Number: B2012516 (100 ug)
Weight
0.15
Length
2
Width
0.5
Height
0.5
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