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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Mouse ELANE/Neutrophil elastase Protein, N-His |
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Origin species | Mouse |
Expression system | Prokaryotic expression |
Molecular weight | 25 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 | Phe42-Glu237 |
Aliases /Synonyms | Neutrophil elastase, 3.4.21.37, Elastase-2, Leukocyte elastase, Elane, Ela2 |
Reference | ARO-P10921 |
Note | For research use only. |
Recombinant Mouse ELANE/Neutrophil elastase protein is a highly purified and biologically active protein that is widely used in research and diagnostic applications. This protein is a member of the serine protease family and is primarily expressed in neutrophils, where it plays a crucial role in the innate immune response. In this article, we will discuss the structure, activity, and applications of this important recombinant protein.
The recombinant Mouse ELANE/Neutrophil elastase protein is a 30 kDa protein consisting of 267 amino acids. It is composed of a catalytic domain, a propeptide region, and a C-terminal domain. The catalytic domain is responsible for the proteolytic activity of the protein, while the propeptide region is involved in the regulation of its activity. The C-terminal domain is important for the binding of the protein to its substrates.
The recombinant protein is produced through genetic engineering techniques, where the gene for ELANE is inserted into a suitable expression vector and then expressed in a host cell, such as E. coli. This allows for the production of large quantities of pure and highly active protein.
Recombinant Mouse ELANE/Neutrophil elastase protein is a potent serine protease that is involved in the degradation of extracellular matrix proteins, such as elastin, collagen, and fibronectin. It is also capable of degrading a variety of other proteins, including cytokines, chemokines, and complement proteins. This proteolytic activity is crucial for the proper functioning of the immune system, as it helps in the clearance of pathogens and damaged tissues.
The activity of the recombinant protein can be measured using various assays, such as chromogenic, fluorogenic, and ELISA-based assays. These assays utilize specific substrates that are cleaved by ELANE, resulting in a color or fluorescence signal that can be quantified. This allows for the accurate measurement of the enzyme activity in different samples.
Recombinant Mouse ELANE/Neutrophil elastase protein has a wide range of applications in research and diagnostics. One of its primary uses is in the study of the immune response and inflammation. The recombinant protein can be used to induce inflammation in animal models, allowing for the investigation of the role of ELANE in various disease conditions.
Furthermore, the recombinant protein is also used in the development of diagnostic tests for various diseases. For example, it is used as an antigen in ELISA-based tests for the detection of autoimmune disorders, such as Wegener’s granulomatosis and anti-neutrophil cytoplasmic antibody (ANCA)-associated vasculitis. Its ability to degrade extracellular matrix proteins also makes it a valuable tool in wound healing studies.
In addition, recombinant Mouse ELANE/Neutrophil elastase protein is also used in the production of monoclonal antibodies. The protein can be used as an immunogen to generate specific antibodies that can be used for various research and diagnostic purposes.
Recombinant Mouse ELANE/Neutrophil elastase protein is a highly purified and biologically active protein that plays a crucial role in the innate immune response. Its structure, activity, and applications make it a valuable tool in various research and diagnostic fields. With the advancement of genetic engineering techniques, the production of this important protein has become more efficient and cost-effective, allowing for its widespread use in the scientific community.
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