Recombinant Human Cartilage matrix protein (MATN1)

Recombinant human cartilage matrix protein (MATN1) production begins synthesizing the human MATN1 (23-496aa)-encoding gene, which is fused with an N-terminal 6xHis-tag gene. This fused gene is cloned into an appropriate expression vector and introduced into E. coli cells, from which those containing the expression vector are selected. The positive cells are cultured to express the recombinant MATN1 protein, which is harvested from the cell lysate. The recombinant MATN1 protein is purified using affinity chromatography. Its purity is over 85% as determined by SDS-PAGE. Human cartilage matrix protein, also called Matrilin-1, is encoded by the MATN1 gene and is a crucial component of the cartilage extracellular matrix (ECM). Matrilin-1 acts as an adaptor protein that bridges the collagen II and proteoglycan networks within the cartilage [1]. It forms homotrimers in mature cartilage, with the potential to form homotetramers under certain conditions [2]. Matrilin-1 plays a significant role in collagen fibrillogenesis and organization within the cartilage ECM [1]. It has been associated with the development and aging of articular cartilage, aiding in distinguishing different cartilage types based on its distribution [3]. Furthermore, studies have shown that matrilin-1 is involved in skeletal development, as evidenced by the fact that mice lacking matrilin-1 exhibited alterations in type II collagen fibrillogenesis and organization [1]. References:[1] X. Huang, D. Birk, & P. Goetinck, Mice lacking matrilin-1 (cartilage matrix protein) have alterations in type ii collagen fibrillogenesis and fibril organization, Developmental Dynamics, vol. 216, no. 4/5, p. 434-441, 1999. https://doi.org/10.1002/(sici)1097-0177(199912)216:4/53.0.co;2-x[2] A. Klatt, D. Nitsche, B. Kobbe, M. M?rgelin, M. Paulsson, & R. Wagener, Molecular structure and tissue distribution of matrilin-3, a filament-forming extracellular matrix protein expressed during skeletal development, Journal of Biological Chemistry, vol. 275, no. 6, p. 3999-4006, 2000. https://doi.org/10.1074/jbc.275.6.3999[3] E. Kavanagh and D. Ashhurst, Development and aging of the articular cartilage of the rabbit knee joint: distribution of biglycan, decorin, and matrilin-1, Journal of Histochemistry & Cytochemistry, vol. 47, no. 12, p. 1603-1615, 1999. https://doi.org/10.1177/002215549904701212