Meanwhile, it has been reported that hyaluronan and proteoglycan link (HAPLN) protein among extracellular matrix proteins plays a role in stabilizing aggregates of hyaluronic acid and proteoglycan in the extracellular matrix and is involved in cell-to-cell adhesion. Therefore, to mass-produce extracellular matrix proteins using desired amino acid sequences, a necessity of having more appropriate and cost-effective production systems has been raised. Generally, proteins extracted from animal tissues are used, but the amounts of the extracted proteins are very small. Due to these structural features, studies regarding mass-production and functions through recombination of extracellular matrix proteins have faced numerous technical challenges. Among them, extracellular matrix proteins are self-assembled into a molecular scaffold by adjusting biomechanical properties and composition according to functions of the corresponding tissue, and most extracellular matrix proteins are expressed in a trace amount in the tissue, and function by forming multiple bonds in a modular form. Since each tissue and organ of a multicellular organism have independently evolved according to their characteristics, the components and functions of the extracellular matrix also vary depending on the type of tissue and cell.īasically, the extracellular matrix consists of water, proteins, and polysaccharides. The extracellular matrix performs various biological functions such as cell-to-cell adhesion and physical support, as well as cell differentiation and growth, and intercellular signaling and regulation, etc. The extracellular matrix (ECM) is a non-cellular component in living things, formed by various substances that are secreted out of cells, and is present within all tissues and organs of living organisms. The present disclosure relates to a medium composition for culturing animal cells for producing a recombinant extracellular matrix protein, a method of producing the recombinant extracellular matrix protein with high purity, and a method of assaying a monomer of the recombinant extracellular matrix protein. 30, 2020, both of which are incorporated herein by reference in their entirety. 29, 2021, which in turn claims the benefit of Korean Patent Application No. National Stage of International Application No. The method of claim 1, wherein, in the analyzing, ratios of the monomer of the recombinant extracellular matrix protein and other impurities are analyzed. The method of claim 1, wherein the mobile phase comprises hydrochloride at a concentration of more than 0.5 M.Ħ. The method of claim 1, wherein the hydrochloride is arginine hydrochloride, aniline hydrochloride, adenine hydrochloride, guanine hydrochloride, guanidine hydrochloride, histidine hydrochloride, or lysine hydrochloride.ĥ. The method of claim 2, wherein the recombinant HAPLN protein is any one protein selected from the group consisting of HAPLN1, HAPLN2, HAPLN3, and HAPLN4.Ĥ. The method of claim 1, wherein the recombinant extracellular matrix protein is collagen, elastin, fibronectin, laminin, vitronectin, tenascin, or hyaluronan and proteoglycan link (HAPLN) protein.ģ. A method of assaying a monomer of a recombinant extracellular matrix protein, the method comprising: performing size exclusion chromatography on a sample comprising the recombinant extracellular matrix protein using a mobile phase comprising hydrochloride and analyzing the monomer of the recombinant extracellular matrix protein in the sample, based on a result of the size exclusion chromatography.Ģ.
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