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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Mouse MMP7 Protein, N-His |
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Origin species | Mouse |
Expression system | Prokaryotic expression |
Molecular weight | 29.36 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 | Asp26-Leu264 |
Aliases /Synonyms | Matrix metalloproteinase-7, MMP-7, Uterine metalloproteinase, Matrilysin, Pump-1 protease, Matrin, Mmp7 |
Reference | ARO-P11017 |
Note | For research use only. |
Recombinant Mouse MMP7 Protein, also known as Matrix Metalloproteinase 7, is a type of enzyme that plays a crucial role in various biological processes such as tissue remodeling, wound healing, and cell migration. This protein is a member of the matrix metalloproteinase family, which consists of zinc-dependent enzymes that are involved in the breakdown of extracellular matrix components.
The recombinant form of MMP7 protein is produced through genetic engineering techniques, where the gene encoding for the protein is inserted into a host organism, typically bacteria or yeast, for production. The resulting protein is a homodimer, meaning it is composed of two identical subunits, each with a molecular weight of approximately 28 kDa.
The structure of recombinant MMP7 protein consists of a catalytic domain, a propeptide domain, and a hemopexin-like domain. The catalytic domain is responsible for the enzymatic activity of the protein, while the propeptide domain is involved in the regulation of its activation. The hemopexin-like domain is responsible for substrate recognition and binding.
The main function of recombinant MMP7 protein is to cleave and degrade various components of the extracellular matrix, such as collagen, elastin, and fibronectin. This activity is crucial for tissue remodeling, wound healing, and cell migration processes. MMP7 also has the ability to activate other matrix metalloproteinases, further amplifying its role in extracellular matrix degradation.
In addition to its role in tissue remodeling, MMP7 has been shown to have other biological activities, such as promoting cell proliferation, inhibiting cell apoptosis, and regulating immune responses. These activities are mediated through interactions with various signaling pathways and other proteins in the extracellular environment.
Recombinant MMP7 protein has a wide range of applications in both research and clinical settings. In research, it is commonly used as a tool to study the role of MMP7 in various biological processes. This includes studying its effects on cell migration, wound healing, and tissue remodeling. Recombinant MMP7 protein is also used in drug discovery and development, as it can be used to screen potential inhibitors or activators of the enzyme.
In the clinical setting, recombinant MMP7 protein has potential as a biomarker for various diseases, including cancer. Elevated levels of MMP7 have been observed in several types of cancer, and it has been suggested that it could be used as a diagnostic or prognostic marker. Additionally, MMP7 inhibitors have been investigated as potential therapeutic agents for cancer and other diseases involving excessive extracellular matrix degradation.
Recombinant Mouse MMP7 Protein is a crucial enzyme involved in various biological processes, with its main function being the degradation of extracellular matrix components. Its structure consists of a catalytic domain, propeptide domain, and hemopexin-like domain. The protein has a wide range of activities, including tissue remodeling, wound healing, and cell migration. It has applications in both research and clinical settings, and its potential as a biomarker and therapeutic target is currently being investigated.
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