Code | CSB-EP006240HU |
Abbreviation | Recombinant Human CXCL10 protein |
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Size | $224 |
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The recombinant human CXCL10 protein is expressed with an N-terminal 6xHis tag in an E. coli system. The CXCL10 gene fragment (22-98aa) is co-inserted into a vector with the 6xHis tag gene and then introduced into E. coli cells. Protein expression is initiated by adding IPTG, which induces the production of the recombinant CXCL10 protein. After lysis of the cells, affinity chromatography is used to purify the target protein. The recombinant CXCL10 protein is analyzed using SDS-PAGE, with the gel showing a purity of over 90%.
Human CXCL10 is a chemokine that plays a critical role in immune response and inflammation. It is primarily produced in response to IFN-γ and is involved in the recruitment and activation of immune cells, particularly T lymphocytes, monocytes, and NK cells, through its interaction with the CXCR3 [1][2]. CXCL10 is classified as a non-ELR (glutamic acid-leucine-arginine) CXC chemokine, which distinguishes it from other chemokines that promote angiogenesis [3].
The expression of CXCL10 is significantly upregulated in various pathological conditions, including viral infections, autoimmune diseases, and cancers. Elevated levels of CXCL10 have been observed in patients with COVID-19, where it serves as a potential biomarker for disease severity and prognosis [4]. CXCL10 has been shown to inhibit tumor growth and angiogenesis, suggesting its therapeutic potential in cancer treatment [5]. Moreover, its role in chronic inflammatory conditions, such as chronic obstructive pulmonary disease (COPD) and diabetes, highlights its involvement in the pathogenesis of these diseases [6][7]. CXCL10's mechanism of action involves the activation of various intracellular signaling pathways, including the ERK MAPK and PI3K pathways, which are crucial for cell proliferation and survival [8].
References:
[1] L. Yang, P. Chen, S. Luo, J. Li, K. Liu, H. Huo-zhen, et al. Cxc‐chemokine‐ligand‐10 gene therapy efficiently inhibits the growth of cervical carcinoma on the basis of its anti‐angiogenic and antiviral activity, Biotechnology and Applied Biochemistry, vol. 53, no. 3, p. 209-216, 2009. https://doi.org/10.1042/ba20090012
[2] E. Hermans, Cxcl10 is a crucial chemoattractant for efficient intranasal delivery of mesenchymal stem cells to the neonatal hypoxic-ischemic brain, Stem Cell Research & Therapy, vol. 15, no. 1, 2024. https://doi.org/10.1186/s13287-024-03747-8
[3] P. Hensbergen, E. Raaij-Helmer, R. Dijkman, R. Schors, G. Werner-Felmayer, D. Boorsma, et al. Processing of natural and recombinant cxcr3‐targeting chemokines and implications for biological activity, European Journal of Biochemistry, vol. 268, no. 18, p. 4992-4999, 2001. https://doi.org/10.1046/j.0014-2956.2001.02433.x
[4] D. Mikkelsen, Characterization of cxcl10 as a biomarker of respiratory tract infections detectable by open-source lateral flow immunoassay,, 2024. https://doi.org/10.1101/2024.01.12.24301261
[5] G. Li, L. Tian, J. Hou, Z. Ding, Q. He, P. Feng, et al., Improved therapeutic effectiveness by combining recombinant cxc chemokine ligand 10 with cisplatin in solid tumors, Clinical Cancer Research, vol. 11, no. 11, p. 4217-4224, 2005. https://doi.org/10.1158/1078-0432.ccr-04-2117
[6] E. Hardaker, A. Bacon, K. Carlson, A. Roshak, J. Foley, D. Schmidtet al., Regulation of tnf‐α and ifn‐γ induced cxcl10 expression: participation of the airway smooth muscle in the pulmonary inflammatory response in chronic obstructive pulmonary disease, The Faseb Journal, vol. 18, no. 1, p. 191-193, 2003. https://doi.org/10.1096/fj.03-0170fje
[7] F. Schulthess, F. Paroni, N. Sauter, L. Shu, P. Ribaux, L. Haataja, et al. Cxcl10 impairs β cell function and viability in diabetes through tlr4 signaling, Cell Metabolism, vol. 9, no. 2, p. 125-139, 2009. https://doi.org/10.1016/j.cmet.2009.01.003
[8] J. Gao, L. Wu, Y. Wang, S. Cui, S. Duan, Z. Dong, et al. Knockdown of cxcl10 inhibits mesangial cell proliferation in murine habu nephritis via erk signaling, Cellular Physiology and Biochemistry, vol. 42, no. 5, p. 2118-2129, 2017. https://doi.org/10.1159/000479914
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