Recombinant Human Sialidase-1 (NEU1)

The recombinant human Sialidase-1 (NEU1) is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered. NEU1 is an enzyme that catalyzes the removal of sialic acid residues from glycoproteins and glycolipids. This enzymatic activity is essential for various physiological processes, including cell differentiation, lysosomal catabolism, and the assembly of elastic fibers in tissues [1] [2] [3]. NEU1 regulates insulin signaling, energy metabolism, and glucose uptake [4]. Moreover, NEU1 has been identified as a potential pharmacological target, suggesting its importance in drug development [5]. Studies have shown that sialidases, including NEU1, play roles in modulating functional molecules involved in various biological processes [6]. NEU1 is part of a multiprotein complex that facilitates elastic fiber assembly, emphasizing its role in maintaining tissue structure and function [2]. NEU1 has been found to desialylate and functionally inactivate receptors interacting with growth factors, further underlining its involvement in cellular signaling pathways [3]. The distribution and activity of NEU1 are tightly regulated within cells. The internalization signal in the cytoplasmic tail of NEU1 controls its intracellular localization, ensuring its proper function in lysosomes for the degradation of sialylated glycoconjugates [1]. NEU1 activity has been visualized in mammalian tissues, demonstrating its potential utility in molecular imaging and cancer detection [7]. References:[1] K. Lukong, V. Seyrantepe, K. Landry, S. Trudel, A. Ahmad, W. Gahlet al., Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail, Journal of Biological Chemistry, vol. 276, no. 49, p. 46172-46181, 2001. https://doi.org/10.1074/jbc.m104547200[2] A. Hinek, A. Pshezhetsky, M. Itzstein, & B. Starcher, Lysosomal sialidase (neuraminidase-1) is targeted to the cell surface in a multiprotein complex that facilitates elastic fiber assembly, Journal of Biological Chemistry, vol. 281, no. 6, p. 3698-3710, 2006. https://doi.org/10.1074/jbc.m508736200[3] A. Hinek, T. Bodnaruk, S. Bunda, Y. Wang, & K. Liu, Neuraminidase-1, a subunit of the cell surface elastin receptor, desialylates and functionally inactivates adjacent receptors interacting with the mitogenic growth factors pdgf-bb and igf-2, American Journal of Pathology, vol. 173, no. 4, p. 1042-1056, 2008. https://doi.org/10.2353/ajpath.2008.071081[4] A. Minami, Y. Fujita, S. Shimba, M. Shiratori, Y. Kaneko, T. Sawataniet al., The sialidase inhibitor 2,3-dehydro-2-deoxy-n-acetylneuraminic acid is a glucose-dependent potentiator of insulin secretion, Scientific Reports, vol. 10, no. 1, 2020. https://doi.org/10.1038/s41598-020-62203-8[5] C. Albrecht, Z. Akissi, P. Yao-Kouassi, A. Magid, P. Maurice, L. Ducaet al., Identification and evaluation of new potential inhibitors of human neuraminidase 1 extracted from olyra latifolia l.: a preliminary study, Biomedicines, vol. 9, no. 4, p. 411, 2021. https://doi.org/10.3390/biomedicines9040411[6] K. Hata, K. Koseki, K. Yamaguchi, S. Moriya, Y. Suzuki, S. Yingsakmongkonet al., Limited inhibitory effects of oseltamivir and zanamivir on human sialidases, Antimicrobial Agents and Chemotherapy, vol. 52, no. 10, p. 3484-3491, 2008. https://doi.org/10.1128/aac.00344-08[7] A. Minami, T. Otsubo, D. Ieno, K. Ikeda, H. Kanazawa, K. Shimizuet al., Visualization of sialidase activity in mammalian tissues and cancer detection with a novel fluorescent sialidase substrate, Plos One, vol. 9, no. 1, p. e81941, 2014. https://doi.org/10.1371/journal.pone.0081941