ELANE Primary Antibody
Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode structurally similar proteins. The encoded preproprotein is proteolytically processed to generate the active protease. Following activation, this protease hydrolyzes proteins within specialized neutrophil lysosomes, called azurophil granules, as well as proteins of the extracellular matrix. The enzyme may play a role in degenerative and inflammatory diseases through proteolysis of collagen-IV and elastin. This protein also degrades the outer membrane protein A (OmpA) of E. coli as well as the virulence factors of such bacteria as Shigella, Salmonella and Yersinia. Mutations in this gene are associated with cyclic neutropenia and severe congenital neutropenia (SCN). This gene is present in a gene cluster on chromosome 19.
Purified recombinant fragment of human ELANE (AA: 140-267) expressed in E. Coli.
Purified antibody in PBS with 0.05% sodium azide
4°C; -20°C for long term storage
Figure 1: Black line: Control Antigen (100 ng);Purple line: Antigen (10ng); Blue line: Antigen (50 ng); Red line:Antigen (100 ng)
Figure 2:Western blot analysis using ELANE mAb against human ELANE (AA: 140-267) recombinant protein. (Expected MW is 39 kDa)
Figure 3:Western blot analysis using ELANE mAb against HEK293 (1) and ELANE (AA: 140-267)-hIgGFc transfected HEK293 (2) cell lysate.
Figure 4:Western blot analysis using ELANE mouse mAb against HL-60 (1), THP-1 (2), MOLT4 (3), C6 (4), and K562 (5) cell lysate.
Figure 5:Flow cytometric analysis of K562 cells using ELANE mouse mAb (green) and negative control (red).
For Research Use Only. Not for use in diagnostic procedures.