Recombinant Mouse ELANE/Neutrophil elastase Protein, N-His

Description of Recombinant Mouse ELANE/Neutrophil elastase Protein, N-His

Introduction

Recombinant Mouse ELANE/Neutrophil elastase Protein is a highly versatile and important protein in the field of immunology and biomedical research. It is a member of the serine protease family and is primarily expressed in neutrophils, a type of white blood cell responsible for fighting against infections. This protein plays a crucial role in the immune response by degrading and eliminating foreign pathogens, making it an essential component of the innate immune system. In this article, we will explore the structure, activity, and application of Recombinant Mouse ELANE/Neutrophil elastase Protein.

Structure of Recombinant Mouse ELANE/Neutrophil elastase Protein

Recombinant Mouse ELANE/Neutrophil elastase Protein is a 30-kDa protein composed of 267 amino acids. It is a homodimer, meaning it is made up of two identical subunits, each containing a catalytic domain and a non-catalytic domain. The catalytic domain is responsible for the proteolytic activity of the protein, while the non-catalytic domain is involved in substrate recognition and binding.

The crystal structure of Recombinant Mouse ELANE/Neutrophil elastase Protein has been extensively studied and has revealed the presence of a highly conserved active site, consisting of a serine, histidine, and aspartic acid residue. This active site is crucial for the proteolytic activity of the protein and is responsible for the cleavage of peptide bonds in its target substrates.

Activity of Recombinant Mouse ELANE/Neutrophil elastase Protein

Recombinant Mouse ELANE/Neutrophil elastase Protein is a potent serine protease with broad substrate specificity. It is capable of cleaving a variety of proteins, including extracellular matrix proteins, cytokines, and chemokines. This proteolytic activity is essential for the recruitment and activation of immune cells, as well as the degradation of harmful pathogens.

One of the key functions of Recombinant Mouse ELANE/Neutrophil elastase Protein is its role in the destruction of bacterial and fungal cell walls. It does this by cleaving the peptide bonds in the peptidoglycan layer, which is essential for the structural integrity of these microorganisms. This activity is crucial for the elimination of bacterial and fungal infections, making Recombinant Mouse ELANE/Neutrophil elastase Protein a valuable component of the innate immune system.

Furthermore, Recombinant Mouse ELANE/Neutrophil elastase Protein is also involved in the activation of other immune cells, such as macrophages and dendritic cells. It does this by cleaving and activating pro-inflammatory cytokines and chemokines, which play a crucial role in the recruitment and activation of these cells. This activity is essential for the initiation and maintenance of the immune response.

Application of Recombinant Mouse ELANE/Neutrophil elastase Protein

Recombinant Mouse ELANE/Neutrophil elastase Protein has a wide range of applications in both research and clinical settings. In research, it is commonly used as a model protein to study the structure and function of serine proteases. Its broad substrate specificity and well-characterized crystal structure make it an excellent candidate for these studies.

In clinical settings, Recombinant Mouse ELANE/Neutrophil elastase Protein has been used in the diagnosis and treatment of various diseases. Its high activity against bacterial and fungal pathogens makes it a potential therapeutic agent for the treatment of infectious diseases. It has also been studied for its potential role in autoimmune diseases, such as rheumatoid arthritis and lupus, where its proteolytic activity may contribute to tissue damage and inflammation.

Additionally, Recombinant Mouse ELANE/Neutrophil elastase Protein has been used as an antigen in the development of diagnostic tests for various conditions. Its presence in the blood can be an indicator of certain diseases, making it a valuable biomarker for early detection and monitoring of these