• Species Reactivity

  Human

• Specificity

  Detects human ELA2 in direct ELISAs and Western blots.    
   

• Source

  Monoclonal Mouse IgG1 Clone # 950317

• Immunogen

  Chinese hamster ovary cell line CHO-derived recombinant human ELA2    
  Met1-Asn252    
  Accession # P08246

• Formulation

  Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.

• Label

  Alexa Fluor 350

Applications

• 
  

  Recommended    
  Concentration

  Sample

• Intracellular Staining by Flow Cytometry

  0.25-1 µg/10    ⁶ cells

  THP‑1 human acute monocytic leukemia cell line treated with monensin were fixed with Flow Cytometry Fixation Buffer (Catalog # ) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # )

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Preparation and Storage

• Stability & Storage

  Store the unopened product at 2 - 8 °C. Do not use past expiration date.

Background: Neutrophil Elastase/ELA2

Neutrophil Elastase (ELA2, ELANE), also known as HNE, is a chymotrypsin family serine protease that plays a key role in pathogen clearance (1-3). It is expressed by promyelocytes and stored in the intracellular azurophilic granules of polymorphonuclear leukocytes (PMN) (4). 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 (5, 6). It also can degrade multiple extracellular matrix proteins including Elastin and Fibronectin (5). In the lung, this activity contributes to pathology in emphysema, cystic fibrosis, and adult respiratory distress syndrome (ARDS) (1). Neutrophil Elastase can be inhibited by Serpin A1/alpha 1-Antitrypsin, SLPI, Serpin B1, and  
Trappin-2/Elafin (7-11). Its activity in the lung is increased by exposure to tobacco smoke which inactivates Serpin A1 through methionine oxidation (12). Mature human Neutrophil Elastase shares 73% amino acid sequence identity with mouse and rat Neutrophil Elastase (13, 14). Multiple mutations in the human ELANE gene are causative of severe congenital and cyclic neutropenias (15).

• References:

1. Korkmaz, B. et al. (2010) Pharmacol. Rev. 62:726.

2. Stein, R.L. et al. (1987) Biochemistry 26:1301.

3. Bachovchin, W.W. (1986) Biochemistry 25:7751.

4. Garwicz, D. et al. (2005) Haematologica 90:38.

5. Owen, C.A. et al. (1995) J. Cell Biol. 131:775.

6. Stephan, A. and M. Fabri (2015) Exp. Dermatol. 24:161.

7. Carrell, R.W. et al. (1982) Nature 298:329.

8. Rice, W.G. and S.J. Weiss (1990) Science 249:178.

9. Thompson, R.C. et al. (1986) Proc. Natl. Acad. Sci. USA 83:6692.

10. Cooley, J. et al. (2001) Biochemistry 40:15762.

11. Wiedow, O. et al. (1990) J. Biol. Chem. 265:14791.

12. Taggart, C. et al. (2000) J. Biol. Chem. 275:27258.

13. Sinha, S. et al. (1987) Proc. Natl. Acad. Sci. USA 84:2228.

14. Okano, K. et al. (1987) J. Biochem. 102:13.

15. Makaryan, V. et al. (2015) Curr. Opin. Hematol. 22:3.

• Entrez Gene IDs:

  1991 (Human); 50701 (Mouse)

• Alternate Names:

  Bone marrow serine protease; EC 3.4.21; EC 3.4.21.37; ELA2; ELA2granulocyte-derived elastase; ELANE; elastase 2, neutrophil; elastase, neutrophil expressed; Elastase-2; GE; HLEelastase-2; HNE; Human leukocyte elastase; Leukocyte Elastase; Medullasin; NE; Neutrophil Elastase; PMN elastase; PMN-E; polymorphonuclear elastase; SCN1