Human Acetylcholinesterase
<strong>Human Acetylcholinesterase</strong>_x000D_ <strong>Catalog number:</strong> B2016594_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 5 ug_x000D_ <strong>Molecular Weight or Concentration:</strong> 64.6 kDa_x000D_ <strong>Supplied as:</strong> Powder_x000D_ <strong>Applications:</strong> a molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> −20°C_x000D_ <strong>Keywords:</strong> AChE, Acetylcholine acetylhydrolase_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: Richbart SD, Merritt JC, Nolan NA, Dasgupta P. Acetylcholinesterase and human cancers Adv Cancer Res. 2021;152:1-66._x000D_ 2: Patocka J, Kuca K, Jun D. Acetylcholinesterase and butyrylcholinesterase--important enzymes of human body Acta Medica (Hradec Kralove). 2004;47(4):215-28._x000D_ 3: García-Ayllón MS, Millán C, Serra-Basante C, Bataller R, Sáez-Valero J. Readthrough acetylcholinesterase is increased in human liver cirrhosis PLoS One. 2012;7(9):e44598._x000D_ 4: Silman I, Sussman JL. Recent developments in structural studies on acetylcholinesterase J Neurochem. 2017 Aug;142 Suppl 2:19-25._x000D_ 5: Alam A, Shaikh S, Ahmad SS, Ansari MA, Shakil S, Rizvi SM, Shakil S, Imran M, Haneef M, Abuzenadah AM, Kamal MA. Molecular interaction of human brain acetylcholinesterase with a natural inhibitor huperzine-B: an enzoinformatics approach CNS Neurol Disord Drug Targets. 2014 Apr;13(3):487-90._x000D_ 6: Soreq H, Zevin-Sonkin D, Avni A, Hall LM, Spierer P. A human acetylcholinesterase gene identified by homology to the Ace region of Drosophila Proc Natl Acad Sci U S A. 1985 Mar;82(6):1827-31._x000D_ 7: Bester SM, Adipietro KA, Funk VL, Myslinski JM, Keul ND, Cheung J, Wilder PT, Wood ZA, Weber DJ, Height JJ, Pegan SD. The structural and biochemical impacts of monomerizing human acetylcholinesterase Protein Sci. 2019 Jun;28(6):1106-1114._x000D_ 8: da Silva JAV, Pereira AF, LaPlante SR, Kuca K, Ramalho TC, França TCC. Reactivation of VX-Inhibited Human_Acetylcholinesterase by Deprotonated Pralidoxime. A Complementary Quantum Mechanical Study Biomolecules. 2020 Jan 27;10(2):192._x000D_ 9: Shaikh S, Verma A, Siddiqui S, Ahmad SS, Rizvi SM, Shakil S, Biswas D, Singh D, Siddiqui MH, Shakil S, Tabrez S, Kamal MA. Current acetylcholinesterase-inhibitors: a neuroinformatics perspective CNS Neurol Disord Drug Targets. 2014 Apr;13(3):391-401._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/24059296">10: Shaikh S, Verma A, Siddiqui S, Ahmad SS, Rizvi SM, Shakil S, Biswas D, Singh D, Siddiqui MH, Shakil S, Tabrez S, Kamal MA. Current acetylcholinesterase-inhibitors: a neuroinformatics perspective CNS Neurol Disord Drug Targets. 2014 Apr;13(3):391-401. </a>_x000D_ _x000D_ <strong>Products Related to Human Acetylcholinesterase can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>
Product Specifications
Short Description
Catalog Number: B2016594 (5 ug)
Weight
0.15
Length
2
Width
0.5
Height
0.5
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