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Neutrophil elastase (human), (purified)

Major inflammatory protease released by neutrophils
BML-SE284-0100 100 µg 405.00 USD
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Functions in inflammation. Can cleave a variety of proteins, including fibrous elastin, collagen, clotting factors, TNF-α , and α 1- antichymotrypsin. Because of its potential roles in inflammatory diseases such as emphysema and cystic fibrosis, it is a target for drug discovery.

Product Details

Alternative Name:Leukocyte elastase, LE
Source:Isolated from human neutrophils. Active enzyme.
UniProt ID:P08246
Purity:≥95% (SDS-PAGE). Although this is in highly purified form, and the source material tested negative for HbsAg, anti-HBc, anti-HCV, and anti-HIV-1 and -2, handle this product with all due precautions.
Specific Activity:20-22 U/mg protein. One unit will hydrolyze 1.0 μmole of MeOSuc-Ala-Ala-Pro-Val-pNA (Prod. No. BML-P213) per minute, at 25°C in 100mM Tris-HCl, pH 7.5 with 500 mM NaCl.
Application Notes:Useful for inhibitor screening, kinetic studies, and cleavage of substrates in vitro or in tissue culture.
Reconstitution:Reconstitute with 50mM sodium acetate, pH 5.5, with 150mM sodium chloride to the original volume, followed by gentle mixing to ensure adequate homogenization.
Shipping:Dry Ice
Long Term Storage:-20°C
Use/Stability:This enzyme is stable when stored under the above conditions. Procedures such as dilution of the enzyme followed by refreezing could lead to loss of activity.
Handling:Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -80°C.
Scientific Background:Neutrophil elastase, a serine protease found in polymorphonuclear neutrophils (PMNs), functions in inflammation.
Regulatory Status:RUO - Research Use Only

Product Literature References

Chemical Optimization of Selective Pseudomonas aeruginosa LasB Elastase Inhibitors and Their Impact on LasB-Mediated Activation of IL-1β in Cellular and Animal Infection Models: M.J. Everett, et al.; ACS Infect. Dis. 9, 270 (2022), Abstract;
Multiple modes of action mediate the therapeutic effect of IVIg in experimental epidermolysis bullosa acquisita: E. Pipi, et al.; J. Invest. Dermatol. 142, 1552 (2022), Abstract;
Amblyomma americanum serpin 27 (AAS27) is a tick salivary anti-inflammatory protein secreted into the host during feeding: L. Tirloni, et al.; PLoS Negl. Trop. Dis. 13, e0007660 (2019), Abstract; Full Text
The Coagulation and Immune Systems Are Directly Linked through the Activation of Interleukin-1α by Thrombin: L.C. Burzynski, et al.; Immunity 50, 1033 (2019), Abstract;
Competitive neutrophil elastase inhibitory isoflavones from the roots of Flemingia philippinensis: J. Y. Kim, et al.; Bioorg. Chem. 78, 249 (2018), Abstract;
Calcium-induced Tetramerization and Zinc Chelation Shield Human Calprotectin fromDegradation by Host and Bacterial Extracellular Proteases: J.R. Stephan & E.M. Nolan; Chem. Sci. 2016, 1962 (2016), Application(s): Protease digestion assays, Abstract; Full Text
MrkD1P from Klebsiella pneumoniae strain IA565 allows for coexistence with Pseudomonas aeruginosa and protection from protease-mediated biofilm detachment: B.M. Childers, et al.; Infect. Immun. 81, 4112 (2013), Abstract; Full Text

General Literature References

3-Acylamino-azetidin-2-one as a novel class of cysteine proteases inhibitors: N.E. Zhou, et al.; Bioorg. Med. Chem. Lett. 13, 139 (2003), Abstract;
6-Acylamino-2-1(ethylsulfonyl)oxy]-1H-isoindole-1,3-diones mechanism-based inhibitors of human leukocyte elastase and cathepsin G: effect of chirality in the 6-acylamino substituent on inhibitory potency and selectivity: L.M. Vagnoni, et al.; Bioorg. Med. Chem. 9, 637 (2001), Abstract;
Inhibition of serine proteases by functionalized sulfonamides coupled to the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold: W.C. Groutas, et al.; Bioorg. Med. Chem. 9, 1543 (2001), Abstract;
Human coagulation factor V is activated to the functional cofactor by elastase and cathepsin G expressed at the monocyte surface: D.H. Allen & P.B. Tracy; J. Biol. Chem. 270, 1408 (1995), Abstract;
Inactivation of recombinant human tumor necrosis factor-alpha by proteolytic enzymes released from stimulated human neutrophils: K.P. van Kessel, et al.; J. Immunol. 147, 3862 (1991), Abstract;
Biology of the Extracellular Matrix, vol. 1: Regulation of Matrix Accumulation: J.G. Bieth; New York: Academic Press (R.P. Mecham, ed.) 217-320 (1986), Book,
Human leukocyte granule elastase: rapid isolation and characterization: R.J. Baugh and J. Travis; Biochemistry 15, 836 (1976), Abstract;

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