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Neutrophil Elastase (ELA2/ELANE)

Cat# : THP-0284

Product Datasheets COA :
Catalog# Product Name Availability Size Price Qty
THP-0284 Neutrophil Elastase (ELA2/ELANE) December 22, 2024 20ug $698.00
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Cat#:  THP-0284
Product Name:  Neutrophil Elastase (ELA2/ELANE)
Description:  Recombinant Human Neutrophil Elastase (ELA2/ELANE) Protein (Ser28-Asn252) is produced by Chinese Hamster Ovary cell line system. This protein is fused with a 10-His tag at the C-terminal. N-terminal Sequence Analysis: Ser28.
Species:  Human
Molecular Weight:  Predicted Molecular Mass: 25 kDa; SDS-PAGE: 29-39 kDa, reducing conditions.
Source:  CHO cells
Introduction:  Neutrophil Elastase (ELA2, ELANE), also known as HNE, is a chymotrypsin family serine protease that plays a key role in pathogen clearance. It is expressed by promyelocytes and stored in the intracellular azurophilic granules of polymorphonuclear leukocytes (PMN). These granules fuse with phagosomes, enabling Neutrophil Elastase to participate in the digestion and killing of endocytosed microbes. The enzyme is released by activated neutrophils at sites of inflammation, and it can remain associated with the cell surface or function as a component of neutrophil extracellular nets (NETs) which trap and kill microbial pathogens. It also can degrade multiple extracellular matrix proteins including Elastin and Fibronectin. In the lung, this activity contributes to pathology in emphysema, cystic fibrosis, and adult respiratory distress syndrome (ARDS). Neutrophil Elastase can be inhibited by Serpin A1/alpha 1-Antitrypsin, SLPI, Serpin B1, and Trappin-2/Elafin. Its activity in the lung is increased by exposure to tobacco smoke which inactivates Serpin A1 through methionine oxidation. Mature human Neutrophil Elastase shares 73% amino acid sequence identity with mouse and rat Neutrophil Elastase. Multiple mutations in the human ELANE gene are causative of severe congenital and cyclic neutropenias.
Purity:  >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Biological Activity:  Measured by its ability to cleave the fluorogenic peptide substrate, MeOSuc-Ala-Ala-Pro-Val-7-amido-4-methylcoumarin (MeOSuc-AAPV-AMC). The specific activity is >1,500 pmol/min/μg, as measured under the described conditions.
Application:  These granules fuse with phagosomes, enabling Neutrophil Elastase to participate in the digestion and killing of endocytosed microbes. It also can degrade multiple extracellular matrix proteins including Elastin and Fibronectin. In the lung, this activity contributes to pathology in emphysema, cystic fibrosis, and adult respiratory distress syndrome (ARDS).
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