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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human MYDGF Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 17.72 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°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) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Thr36-Leu173 |
Aliases /Synonyms | MYDGF, C19orf10, Myeloid-derived growth factor |
Reference | YHK63901 |
Note | For research use only. |
Recombinant Human MYDGF Protein, also known as Myeloid-Derived Growth Factor, is a protein that plays a crucial role in the regulation of cell growth and differentiation. It is a member of the platelet-derived growth factor (PDGF) family and is essential for the development and maintenance of various tissues and organs in the human body. In this article, we will discuss the structure, activity, and applications of this recombinant protein.
The MYDGF gene is located on chromosome 19 and encodes for a protein of 128 amino acids. The recombinant form of MYDGF protein is produced by cloning and expressing the gene in a suitable host cell, such as E. coli or mammalian cells. The resulting protein has a molecular weight of approximately 15 kDa and contains a single PDGF domain, which is responsible for its biological activity.
The crystal structure of recombinant MYDGF protein has been determined, revealing a compact dimeric structure with two antiparallel β-sheets and a single α-helix. This structure is similar to other members of the PDGF family, such as PDGF-BB and PDGF-AB. The dimerization of MYDGF is essential for its biological activity, as it allows the protein to bind to its receptor and initiate downstream signaling pathways.
MYDGF protein is a potent mitogen, meaning it stimulates cell proliferation and growth. It exerts its activity by binding to its receptor, PDGFR-α, which is expressed on the surface of various cell types, including fibroblasts, smooth muscle cells, and endothelial cells. This binding leads to the activation of several signaling pathways, including the MAPK and PI3K pathways, which ultimately promote cell growth and survival.
In addition to its mitogenic activity, recombinant MYDGF protein has been shown to have angiogenic properties. It can induce the formation of new blood vessels, which is crucial for tissue repair and regeneration. This activity is mediated by the recruitment of endothelial cells and the stimulation of their proliferation and migration.
The unique properties of recombinant MYDGF protein make it a valuable tool for various research and clinical applications. One of its primary applications is in tissue engineering, where it is used to promote the growth and differentiation of stem cells into specific cell types. This is particularly useful in regenerative medicine, where MYDGF can aid in the repair of damaged tissues and organs.
Recombinant MYDGF protein has also been studied for its potential in wound healing. It has been shown to accelerate the healing process by promoting cell proliferation and angiogenesis. This makes it a promising candidate for the development of new wound healing therapies.
Furthermore, MYDGF has been implicated in various diseases, including cancer, cardiovascular diseases, and fibrotic disorders. Its overexpression has been observed in certain types of cancer, and it has been shown to promote tumor growth and metastasis. On the other hand, its deficiency has been linked to cardiovascular diseases and fibrosis. Therefore, MYDGF protein could be a potential target for the development of novel therapies for these diseases.
Recombinant Human MYDGF Protein is a versatile protein with various biological activities. Its unique structure and mitogenic and angiogenic properties make it a valuable tool for tissue engineering and wound healing applications. Furthermore, its involvement in various diseases makes it a potential target for the development of new therapies. Further research on this protein is necessary to fully understand its role in health and disease and to explore its potential in various fields of medicine.
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