This recombinant mouse Beta-galactoside alpha-2,6-sialyltransferase 1 (St6gal1) 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.
ST6GAL1 is a sialyltransferase that catalyzes the transfer of sialic acid onto galactose-containing substrates, a process crucial for the glycosylation of proteins and lipids in the Golgi apparatus [1][2]. ST6GAL1 plays a significant role in various biological processes, including cell proliferation, metastasis, and modulation of cell signaling and behavior [3][4]. It regulates immunoglobulin production in B cells and has implications for B-cell development [5]. Upregulation of ST6GAL1 has been detected in many human malignancies. ST6GAL1 promotes cancer progression by modulating sialylation patterns on glycoproteins [6].
Research has shown that ST6GAL1 is associated with various diseases, such as bladder cancer, hepatocellular carcinoma, glioblastoma, IgA nephropathy, and pancreatic cancer [1][2][4][7][8][9]. ST6GAL1 dysregulation contributes to disease progression through chemotherapy evasion and liver inflammation, promoting tumor growth and metastasis [1][2][4][7][8]. ST6GAL1 has been demonstrated to control IgA nephropathy progression and protect against radiation-induced gastrointestinal damage [9][10].
References:
[1] P. Antony, M. Rose, A. Heidenreich, R. Knüchel, N. Gaisa, & E. Dahl, Epigenetic inactivation of st6gal1 in human bladder cancer, BMC Cancer, vol. 14, no. 1, 2014. https://doi.org/10.1186/1471-2407-14-901
[2] R. Liu, X. Cao, Y. Liang, X. Li, J. Qian, Y. Liuet al., Downregulation of st6gal1 promotes liver inflammation and predicts adverse prognosis in hepatocellular carcinoma, Journal of Inflammation Research, vol. Volume 15, p. 5801-5814, 2022. https://doi.org/10.2147/jir.s385491
[3] N. Dashzeveg, Dynamic glycoprotein hyposialylation promotes chemotherapy evasion and metastatic seeding of quiescent circulating tumor cell clusters in breast cancer, Cancer Discovery, vol. 13, no. 9, p. 2050-2071, 2023. https://doi.org/10.1158/2159-8290.cd-22-0644
[4] S. Gc, K. Tuy, L. Rickenbacker, R. Jones, A. Chakraborty, C. Milleret al., Α2,6 sialylation mediated by st6gal1 promotes glioblastoma growth, Jci Insight, vol. 7, no. 21, 2022. https://doi.org/10.1172/jci.insight.158799
[5] E. Irons, P. Punch, & J. Lau, Blood-borne st6gal1 regulates immunoglobulin production in b cells, Frontiers in Immunology, vol. 11, 2020. https://doi.org/10.3389/fimmu.2020.00617
[6] E. Scott, st6gal1‐mediated aberrant sialylation promotes prostate cancer progression, The Journal of Pathology, vol. 261, no. 1, p. 71-84, 2023. https://doi.org/10.1002/path.6152
[7] Y. Liu, F. Wang, Y. Zhang, J. Jia, & T. Yan, St6gal1 is up‐regulated and associated with aberrant iga1 glycosylation in iga nephropathy: an integrated analysis of the transcriptome, Journal of Cellular and Molecular Medicine, vol. 24, no. 18, p. 10493-10500, 2020. https://doi.org/10.1111/jcmm.15664
[8] N. Bhalerao, St6gal1 sialyltransferase promotes acinar to ductal metaplasia and pancreatic cancer progression, Jci Insight, vol. 8, no. 19, 2023. https://doi.org/10.1172/jci.insight.161563
[9] Y. Liu, H. Yu, S. Wu, X. Yang, C. Cao, F. Wanget al., Plasma st6gal1 regulates igg sialylation to control iga nephropathy progression, Therapeutic Advances in Chronic Disease, vol. 12, p. 204062232110486, 2021. https://doi.org/10.1177/20406223211048644
[10] P. Punch, E. Irons, C. Manhardt, H. Marathe, & J. Lau, The sialyltransferase st6gal1 protects against radiation-induced gastrointestinal damage, Glycobiology, vol. 30, no. 7, p. 446-453, 2020. https://doi.org/10.1093/glycob/cwz108
