Recombinant Mouse MMP7 Protein, N-His from ProteoGenix; catalogue ARO-P11017; research use only.
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Recombinant Mouse MMP7 Protein, also known as Matrix Metalloproteinase 7, is a member of the matrix metalloproteinase (MMP) family of enzymes. These enzymes play a crucial role in the degradation and remodeling of the extracellular matrix, which is essential for various physiological processes such as tissue growth, wound healing, and immune response. Recombinant Mouse MMP7 Protein is produced through recombinant DNA technology, making it a highly pure and biologically active protein.
Recombinant Mouse MMP7 Protein is a 28 kDa protein consisting of 267 amino acids. It contains a signal peptide, a propeptide, a catalytic domain, and a hemopexin-like domain. The catalytic domain is responsible for the proteolytic activity of the protein, while the hemopexin-like domain is involved in substrate recognition and binding.
The structure of Recombinant Mouse MMP7 Protein is similar to other members of the MMP family, with a conserved zinc-binding motif in the catalytic domain. This motif is essential for the enzymatic activity of the protein. The three-dimensional structure of Recombinant Mouse MMP7 Protein has been determined by X-ray crystallography, revealing its overall fold and the location of the active site.
Recombinant Mouse MMP7 Protein is a zinc-dependent endopeptidase that cleaves various components of the extracellular matrix, including collagen, elastin, fibronectin, and laminin. It is also capable of activating other MMPs, such as MMP2 and MMP9, through proteolytic processing of their propeptides. This activation cascade is essential for the regulation of MMP activity and the maintenance of tissue homeostasis.
The proteolytic activity of Recombinant Mouse MMP7 Protein is tightly regulated by endogenous inhibitors, such as tissue inhibitors of metalloproteinases (TIMPs) and alpha-2-macroglobulin. These inhibitors bind to the active site of the protein, preventing substrate binding and cleavage. Dysregulation of MMP activity has been linked to various diseases, including cancer, cardiovascular diseases, and inflammatory disorders.
Recombinant Mouse MMP7 Protein has been extensively studied for its role in various physiological and pathological processes. It is primarily involved in tissue remodeling and repair, making it a potential therapeutic target for conditions such as wound healing and tissue regeneration. Additionally, Recombinant Mouse MMP7 Protein has been implicated in cancer progression and metastasis, making it a promising target for cancer therapy.
Recombinant Mouse MMP7 Protein has also been used as a diagnostic tool for various diseases. Its elevated levels have been associated with various cancers, including breast, colon, and lung cancer. Measuring the levels of Recombinant Mouse MMP7 Protein in patient samples can aid in early detection and monitoring of these diseases.
Moreover, Recombinant Mouse MMP7 Protein has been used in research to study the role of MMPs in various processes, such as angiogenesis, inflammation, and tissue repair. It has also been used in drug development to screen for potential inhibitors or activators of MMP activity.
In summary, Recombinant Mouse MMP7 Protein is a biologically active protein with a crucial role in tissue remodeling and repair. Its structure, activity, and application have been extensively studied, making it a valuable tool in both basic research and clinical applications. Further studies on Recombinant Mouse MMP7 Protein may lead to a better understanding of its role in various diseases and the development of novel therapeutic strategies.
ProteoGenix catalogue number ARO-P11017. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 29.36 kDa; Fragment: Asp26-Leu264; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
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