Recombinant Human EGFL7, N-His

Reference: YHJ76201
Product nameRecombinant Human EGFL7, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight29.43 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeTyr24-Ser273
Aliases /SynonymsNOTCH4-like protein, Zneu1, Multiple EGF-like domains protein 7, Epidermal growth factor-like protein 7, MEGF7, EGFL7, VE-statin, EGF-like protein 7, Multiple epidermal growth factor-like domains protein 7, Vascular endothelial statin
ReferenceYHJ76201
NoteFor research use only.

Description of Recombinant Human EGFL7, N-His

Introduction to Recombinant Human EGFL7

Recombinant Human EGFL7, also known as Epidermal Growth Factor-Like Domain 7, is a protein that plays a crucial role in various biological processes such as angiogenesis, cell proliferation, and wound healing. It is a member of the epidermal growth factor (EGF) family and is encoded by the EGFL7 gene located on chromosome 9 in humans. In this article, we will delve into the structure, activity, and applications of Recombinant Human EGFL7.

Structure of Recombinant Human EGFL7

Recombinant Human EGFL7 is a small protein consisting of 118 amino acids with a molecular weight of approximately 13 kDa. It contains an EGF-like domain, which is a highly conserved motif found in many growth factors and cytokines. This domain is responsible for the binding of EGFL7 to its receptor, integrin αvβ3, which is present on the surface of endothelial cells.

In addition to the EGF-like domain, Recombinant Human EGFL7 also has a C-terminal domain that is rich in basic amino acids. This domain is essential for the binding of EGFL7 to heparin sulfate proteoglycans, which are found on the surface of cells and in the extracellular matrix. The basic amino acids in this domain also contribute to the overall stability of the protein.

Activity of Recombinant Human EGFL7

Recombinant Human EGFL7 is primarily known for its role in promoting angiogenesis, the formation of new blood vessels from pre-existing ones. It does so by binding to integrin αvβ3 on endothelial cells and activating the VEGF-A/VEGFR2 signaling pathway. This results in the proliferation and migration of endothelial cells, leading to the formation of new blood vessels.

In addition to angiogenesis, Recombinant Human EGFL7 has also been shown to promote cell proliferation and migration in various cell types, including cancer cells. It can also enhance the migration and adhesion of endothelial cells, which is crucial for the process of wound healing.

Applications of Recombinant Human EGFL7

Due to its role in angiogenesis and wound healing, Recombinant Human EGFL7 has potential applications in various fields of medicine. One of the most promising applications is in the treatment of cardiovascular diseases, such as ischemic heart disease and peripheral artery disease. By promoting angiogenesis, EGFL7 can help improve blood flow to damaged tissues and promote tissue repair.

Moreover, Recombinant Human EGFL7 has also shown potential in the treatment of cancer. By promoting cell proliferation and migration, EGFL7 can contribute to tumor growth and metastasis. Therefore, inhibiting EGFL7 activity could potentially be used as a therapeutic strategy for cancer treatment.

In addition, Recombinant Human EGFL7 has been studied for its potential in promoting wound healing. By enhancing the migration and adhesion of endothelial cells, EGFL7 can help with the formation of new blood vessels, which are crucial for wound healing. This makes it a promising candidate for the development of wound healing therapies.

Conclusion

Recombinant Human EGFL7 is a small protein with a crucial role in angiogenesis, cell proliferation, and wound healing. Its structure, consisting of an EGF-like domain and a C-terminal domain, allows it to interact with various receptors and contribute to its diverse activities. With its potential applications in cardiovascular diseases, cancer, and wound healing, Recombinant Human EGFL7 is a promising protein for further research and development in the field of medicine.

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