Recombinant Human MMP28 Protein, N-His

Description of Recombinant Human MMP28 Protein, N-His

Introduction

Recombinant Human MMP28 Protein, also known as Matrix Metalloproteinase 28, is a member of the Matrix Metalloproteinase (MMP) family. MMPs are a group of enzymes that play crucial roles in tissue remodeling, wound healing, and various pathological processes such as cancer and inflammation. MMP28 is a relatively new member of the MMP family, first identified in 2001. It has been found to have unique structural and functional properties, making it an intriguing target for research and potential therapeutic applications.

Structure of Recombinant Human MMP28 Protein

Recombinant Human MMP28 Protein is a 60 kDa glycoprotein that consists of 541 amino acids. It is composed of several distinct structural domains, including a signal peptide, a prodomain, a catalytic domain, a hinge region, a hemopexin-like domain, and a C-terminal domain. The signal peptide is responsible for the secretion of the protein, while the prodomain acts as an intramolecular chaperone, ensuring proper folding and activation of the enzyme. The catalytic domain contains the zinc-binding motif, which is essential for the proteolytic activity of MMPs. The hinge region connects the catalytic domain to the hemopexin-like domain, which is involved in substrate recognition and binding. The C-terminal domain is responsible for the homodimerization of MMP28 and its interaction with other proteins and extracellular matrix components.

Activity of Recombinant Human MMP28 Protein

Recombinant Human MMP28 Protein is a zinc-dependent endopeptidase that cleaves various extracellular matrix components, including collagens, proteoglycans, and fibronectin. Unlike other MMPs, it has a preference for type III collagen, a major component of the basement membrane. MMP28 also has a unique ability to cleave and activate other MMPs, such as MMP2 and MMP13, which further enhances its role in tissue remodeling and wound healing. Additionally, MMP28 has been found to have non-proteolytic functions, such as cell signaling and cell migration, which are mediated by its hemopexin-like domain.

Application of Recombinant Human MMP28 Protein

Recombinant Human MMP28 Protein has a wide range of potential applications in both research and clinical settings. Its role in tissue remodeling and wound healing makes it a promising target for the development of therapeutics for various diseases, such as cancer, fibrosis, and chronic wounds. In cancer, MMP28 has been found to promote tumor growth and metastasis by degrading the extracellular matrix and facilitating tumor cell migration. Therefore, inhibiting MMP28 activity could potentially slow down tumor progression and improve patient outcomes. In fibrosis, MMP28 has been shown to play a role in the excessive deposition of collagen, leading to tissue scarring and organ dysfunction. Inhibiting MMP28 could potentially prevent or reverse this process and improve organ function. Additionally, MMP28 has been found to be upregulated in chronic wounds, and inhibiting its activity could promote wound healing by reducing inflammation and promoting tissue repair.

In research, Recombinant Human MMP28 Protein is a valuable tool for studying the structure and function of MMPs and their role in various biological processes. It can be used to study the substrate specificity of MMP28 and its interactions with other proteins and extracellular matrix components. It can also be used to investigate the non-proteolytic functions of MMP28 and their contribution to disease processes. Furthermore, recombinant protein technology allows for the production of large quantities of pure and active MMP28, which is essential for biochemical and structural studies.

Conclusion

Recombinant Human MMP28 Protein is a unique member of the MMP family with distinct structural and functional properties. It has a crucial role in tissue remodeling, wound healing, and various pathological processes. Its potential as a therapeutic target and its utility in research make it an intriguing