Recombinant Human FBLN7, N-His

Description of Recombinant Human FBLN7, N-His

The Structure of Recombinant Human FBLN7

Recombinant Human FBLN7, also known as Fibulin-7, is a protein that plays a crucial role in the extracellular matrix (ECM). It is a member of the fibulin family, which consists of seven proteins that are involved in cell adhesion, migration, and signaling. The FBLN7 gene is located on chromosome 19 and is composed of 18 exons that encode a protein of 472 amino acids.

The primary structure of Recombinant Human FBLN7 consists of a signal peptide, an N-terminal domain, a tandem array of calcium-binding epidermal growth factor (EGF)-like repeats, and a C-terminal fibulin-type domain. The signal peptide is responsible for the secretion of the protein, while the N-terminal domain is involved in protein-protein interactions. The tandem array of calcium-binding EGF-like repeats is a unique feature of fibulin proteins and is essential for their structural stability. The C-terminal fibulin-type domain is responsible for binding to other ECM proteins, such as fibronectin and laminin.

The Activity of Recombinant Human FBLN7

Recombinant Human FBLN7 is a multifunctional protein with diverse activities. It is primarily involved in the assembly and maintenance of the ECM, which is a complex network of proteins and carbohydrates that provides structural support and regulates cell behavior. FBLN7 interacts with other ECM proteins, including fibronectin, laminin, and collagen, to form a stable network that is essential for tissue integrity.

In addition to its role in the ECM, Recombinant Human FBLN7 has been shown to have anti-angiogenic activity. Angiogenesis is the formation of new blood vessels, and it is a critical process in various physiological and pathological conditions, such as wound healing, tumor growth, and inflammation. FBLN7 inhibits angiogenesis by binding to vascular endothelial growth factor (VEGF) and preventing its interaction with its receptors on endothelial cells.

Furthermore, Recombinant Human FBLN7 has been reported to have anti-tumor activity. It has been shown to inhibit the proliferation and migration of cancer cells by disrupting their interaction with the ECM and inhibiting the activity of growth factors, such as VEGF and fibroblast growth factor (FGF). FBLN7 also promotes the apoptosis (cell death) of cancer cells by activating specific signaling pathways.

The Application of Recombinant Human FBLN7

Recombinant Human FBLN7 has numerous potential applications in the fields of medicine and biotechnology. Due to its anti-angiogenic and anti-tumor activities, FBLN7 has been studied as a potential therapeutic agent for various diseases, including cancer, diabetic retinopathy, and age-related macular degeneration. Its ability to inhibit angiogenesis and tumor growth makes it a promising candidate for the development of anti-cancer drugs.

Moreover, Recombinant Human FBLN7 has been investigated for its potential use in tissue engineering. The ECM plays a critical role in tissue development and regeneration, and FBLN7 is an essential component of the ECM. By incorporating FBLN7 into tissue scaffolds, it is possible to enhance the structural integrity and functionality of engineered tissues, making them more suitable for transplantation.

In conclusion, Recombinant Human FBLN7 is a versatile protein with various structural and functional properties. Its unique structure and diverse activities make it a crucial player in the ECM and a potential therapeutic agent for various diseases. Further research on FBLN7 and its interactions with other proteins in the ECM may lead to the development of novel treatments and therapies for various disorders.