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| Size | 100ug |
|---|---|
| Brand | ProteoGenix |
| Product type | Recombinant Proteins |
| Product name | Recombinant Mouse GPC3/Glypican 3 Protein, N-His-SUMO |
|---|---|
| Origin species | Mouse |
| Expression system | Prokaryotic expression |
| Molecular weight | 36.42 kDa |
| Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| 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 | ProteoGenix |
| Host species | Escherichia coli (E.coli) |
| Fragment Type | Ile344-Ser553 |
| Aliases /Synonyms | Glypican-3, Glypican-3 alpha subunit, Glypican-3 beta subunit, Gpc3 |
| Reference | ARO-P11481 |
| Note | For research use only. |
Recombinant Mouse GPC3/Glypican 3 Protein (rGPC3) is a genetically engineered protein that is produced in a laboratory setting. It is a member of the Glypican family of proteins, which are found on the surface of cells and play important roles in cell signaling and development. rGPC3 is a modified version of the native mouse Glypican 3 protein, with specific structural modifications that enhance its activity and stability. In this article, we will delve into the structure, activity, and applications of rGPC3.
rGPC3 is a glycosylphosphatidylinositol (GPI)-anchored protein, meaning it is attached to the cell membrane by a GPI anchor. It consists of a core protein of 580 amino acids, with a molecular weight of approximately 65 kDa. The protein is composed of a globular N-terminal domain and a long C-terminal domain, which contains multiple heparan sulfate attachment sites. The heparan sulfate chains are important for the binding of rGPC3 to its ligands.
The structure of rGPC3 has been extensively studied using X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. These studies have revealed that rGPC3 has a highly conserved structure, with a unique arrangement of cysteine residues that form disulfide bonds. These disulfide bonds are important for maintaining the overall structure and stability of the protein.
rGPC3 is a multifunctional protein that has been shown to play important roles in cell growth, differentiation, and migration. It is known to interact with a variety of growth factors, cytokines, and extracellular matrix proteins, and is involved in various signaling pathways. One of the key functions of rGPC3 is to regulate the activity of the Wnt signaling pathway, which plays a critical role in embryonic development and tissue homeostasis.
Studies have also shown that rGPC3 has pro-angiogenic properties, meaning it promotes the growth of new blood vessels. This activity is mediated by the interaction of rGPC3 with vascular endothelial growth factor (VEGF), a key regulator of angiogenesis. Additionally, rGPC3 has been shown to enhance the proliferation and migration of cancer cells, making it a potential target for cancer therapy.
Due to its diverse functions, rGPC3 has potential applications in various fields, including cancer research, regenerative medicine, and drug development. One of the most promising applications of rGPC3 is in cancer therapy. It has been found to be overexpressed in several types of cancer, including hepatocellular carcinoma, ovarian cancer, and lung cancer. This makes it a potential target for cancer immunotherapy, where the immune system is stimulated to recognize and attack cancer cells.
In addition, rGPC3 has been studied for its potential role in tissue regeneration. Studies have shown that it can promote the growth and differentiation of stem cells, making it a potential candidate for tissue engineering and regenerative medicine. Furthermore, rGPC3 has been shown to have anti-inflammatory properties, making it a potential therapeutic agent for inflammatory diseases.
In summary, rGPC3 is a recombinant protein that has a unique structure and diverse functions. Its activity is mediated by its interactions with various ligands, and it has potential applications in cancer therapy, tissue regeneration, and drug development. Further research on rGPC3 is needed to fully understand its role in different biological processes and to explore its potential as a therapeutic target. With its promising properties, rGPC3 holds great potential for advancing our understanding of cell signaling and for the development of novel treatments for various diseases.
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