The recombinant human IgGFc-binding protein (FCGBP) 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.
FCGBP, also known as Fc gamma binding protein, is a protein that plays a crucial role in mucosal immunity and mucosal epithelial cell defense mechanisms. It is widely expressed on mucosal surfaces and in various body fluids, making it an essential component of the innate immune defense system [1][2]. FCGBP is associated with mucin-producing cells and body fluids, indicating its ubiquitous presence in vertebrates and cephalochordates [3]. Furthermore, FCGBP regulates the infiltration of immune cells into tumor microenvironments, suggesting its role in cancer immunity [4].
Studies have shown that FCGBP is a mucus protein that protects against tumors and metastasis, highlighting its immunological functions [5]. Additionally, FCGBP interacts with other proteins such as IgG Fc binding protein and MUC2 mucin, indicating its involvement in various molecular interactions within the mucosal environment [6][7]. The protein contains von Willebrand D domains similar to those found in gel-forming mucins, although its precise function is still under investigation [8].
References:
[1] E. Znalesniak, F. Salm, & W. Hoffmann, Molecular alterations in the stomach of tff1-deficient mice: early steps in antral carcinogenesis, International Journal of Molecular Sciences, vol. 21, no. 2, p. 644, 2020. https://doi.org/10.3390/ijms21020644
[2] P. Gómez-Garre, M. Periñán, S. Jesús, M. Bacalini, P. Garagnani, B. Mollenhaueret al., Transcriptomic analysis reveals an association of fcgbp with parkinson’s disease, NPJ Parkinson S Disease, vol. 8, no. 1, 2022. https://doi.org/10.1038/s41531-022-00415-7
[3] J. Heuer, F. Heuer, R. Stürmer, S. Harder, H. Schlüter, N. Emídioet al., The tumor suppressor tff1 occurs in different forms and interacts with multiple partners in the human gastric mucus barrier: indications for diverse protective functions, International Journal of Molecular Sciences, vol. 21, no. 7, p. 2508, 2020. https://doi.org/10.3390/ijms21072508
[4] Q. Li, X. Niu, Y. Li, J. Zhang, S. Zhu, Q. Yanget al., Role of the mucin-like glycoprotein fcgbp in mucosal immunity and cancer, Frontiers in Immunology, vol. 13, 2022. https://doi.org/10.3389/fimmu.2022.863317
[5] Q. Ding, Non-coding rna-related fcgbp downregulation in head and neck squamous cell carcinoma: a novel biomarker for predicting paclitaxel resistance and immunosuppressive microenvironment, Scientific Reports, vol. 14, no. 1, 2024. https://doi.org/10.1038/s41598-024-55210-6
[6] T. Houben, S. Harder, H. Schlüter, H. Kalbacher, & W. Hoffmann, Different forms of tff3 in the human saliva: heterodimerization with igg fc binding protein (fcgbp), International Journal of Molecular Sciences, vol. 20, no. 20, p. 5000, 2019. https://doi.org/10.3390/ijms20205000
[7] H. Gorman, F. Moreau, A. Dufour, & K. Chadee, Iggfc-binding protein and muc2 mucin produced by colonic goblet-like cells spatially interact non-covalently and regulate wound healing, Frontiers in Immunology, vol. 14, 2023. https://doi.org/10.3389/fimmu.2023.1211336
[8] J. Fernández-Blanco, D. Fakih, L. Arike, A. Rodríguez-Piñeiro, B. Martínez-Abad, E. Skanseboet al., Attached stratified mucus separates bacteria from the epithelial cells in copd lungs, Jci Insight, vol. 3, no. 17, 2018. https://doi.org/10.1172/jci.insight.120994
