Code | CSB-YP013826HU |
Abbreviation | Recombinant Human MIF protein |
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Size | $250 |
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Producing the recombinant human macrophage migration inhibitory factor (MIF) with an N-terminal 6xHis-tag in yeast involves cloning the desired gene, along with the N-terminal His-tag sequence, into a suitable vector and transforming yeast cells. The desired gene encodes the full length of the human mature MIF (2-115aa). After inducing protein expression, the positive yeast cells are lysed to release the recombinant MIF protein, which is purified using affinity chromatography. The purity is checked by SDS-PAGE, greater than 85%.
Human MIF is an evolutionarily conserved protein with both extracellular immune-modulating and intracellular cell-regulatory functions [1]. It is constitutively expressed and stored in preformed cytoplasmic pools in immune cells such as monocytes, macrophages, T and B lymphocytes, eosinophils, neutrophils, and dendritic cells, and is rapidly released in response to stimuli [2]. MIF is involved in various functions such as chemotaxis, leukocyte recruitment, and immune modulation [2].
Genetic studies have shown significant relationships between high-expression MIF alleles and host inflammatory responses, as well as improved clinical outcomes from infections [3]. Furthermore, MIF has been linked to inflammation, autoimmune diseases, and stress responses, promoting the pro-inflammatory functions of immune cells [4]. It plays a role in regulating the NLRP3 inflammasome activation and downstream IL-1β production in human monocytes [5]. MIF is up-regulated in atherosclerotic lesions and correlates with coronary artery disease [6].
References:
[1] D. Sinitski, K. Grüner, M. Brandhofer, C. Kontos, P. Winkler, A. Reinstädleret al., Cross-kingdom mimicry of the receptor signaling and leukocyte recruitment activity of a human cytokine by its plant orthologs, Journal of Biological Chemistry, vol. 295, no. 3, p. 850-867, 2019. https://doi.org/10.1074/jbc.ra119.009716
[2] M. Tarasuk, O. Poungpair, D. Ungsupravate, K. Bangphoomi, W. Chaicumpa, & P. Yenchitsomanus, Human single-chain variable fragment antibody inhibits macrophage migration inhibitory factor tautomerase activity, International Journal of Molecular Medicine, vol. 33, no. 3, p. 515-522, 2014. https://doi.org/10.3892/ijmm.2014.1622
[3] R. Bucala, Mif, mif alleles, and prospects for therapeutic intervention in autoimmunity, Journal of Clinical Immunology, vol. 33, no. S1, p. 72-78, 2012. https://doi.org/10.1007/s10875-012-9781-1
[4] T. Calandra and T. Roger, Macrophage migration inhibitory factor: a regulator of innate immunity, Nature Reviews Immunology, vol. 3, no. 10, p. 791-800, 2003. https://doi.org/10.1038/nri1200
[5] M. Shin, Y. Kang, E. Wahl, H. Park, R. Lazova, L. Lenget al., Macrophage migration inhibitory factor regulates u1 small nuclear rnp immune complex–mediated activation of the nlrp3 inflammasome, Arthritis & Rheumatology, vol. 71, no. 1, p. 109-120, 2018. https://doi.org/10.1002/art.40672
[6] D. Sinitski, C. Kontos, C. Krammer, Y. Asare, A. Kapurniotu, & J. Bernhagen, Macrophage migration inhibitory factor (mif)-based therapeutic concepts in atherosclerosis and inflammation, Thrombosis and Haemostasis, vol. 119, no. 04, p. 553-566, 2019. https://doi.org/10.1055/s-0039-1677803
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