Elafin (human), (recombinant)



ALX-201-240-C100	100 µg	284.00 USD

Belongs to the chelonianin family of protease inhibitors and is involved in the physiological control of neutrophil serine proteinases, where it targets NE and proteinase 3. Shows antiprotease, antibacterial and antiinflammatory activity and primes innate immunity.

Product Specification

Alternative Name:	ESI, Elastase-specific inhibitor, SKALP, Skin-derived antileukoproteinase, Protease inhibitor WAP3

MW:	~5.9kDa

Purity:	≥90% (HPLC, SDS-PAGE, MS)

Appearance:	White to faint yellow powder.

Formulation:	Lyophilized.

Biological Activity:	Inhibits human leukocyte elastase (K_i=0.17nM) and human proteinase 3 (K_i=0.42nM) .

Specific Activity:	Inhibition of human leukocyte elastase: ≥90%

Source/Host:	Produced in yeast.

Reconstitution:	Reconstitute in sterile distilled water. Further dilutions should be made in aqueous buffers, pH 4.0-8.0.

Long Term Storage:	-20°C

Hazard:	HARMFUL.

Handling:	After opening, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles.

Product Literature References

The neutrophil elastase inhibitor elafin triggers rb-mediated growth arrest and caspase-dependent apoptosis in breast cancer: J.A. Caruso, et al.; Cancer Res. 70, 7125 (2010), Abstract;

SLPI and elafin: one glove, many fingers: S.E. Williams, et al.; Clin. Sci. (Lond) 110, 21 (2006), Abstract;

Elafin and Its Precursor Trappin-2 Still Inhibit Neutrophil Serine Proteinases when They Are Covalently Bound to Extracellular Matrix Proteins by Tissue Transglutaminase: N. Guyot, et al.; Biochemistry 44, 15610 (2005), Abstract;

Trappin ovine molecule (TOM), the ovine ortholog of elafin, is an acute phase reactant in the lung: T.I. Brown, et al.; Physiol. Genomics 19, 11 (2004), Abstract; Full Text

Kinetics of the inhibition of proteinase 3 by elafin: Q.L. Ying and S.R. Simon; Am. J. Respir. Cell Mol. Biol. 24, 83 (2001), Abstract;

The role of secretory leukocyte proteinase inhibitor and elafin (elastase-specific inhibitor/skin-derived antileukoprotease) as alarm antiproteinases in inflammatory lung disease: J.M. Sallenave; Respir. Res. 1, 87 (2000), Abstract;

The trappin gene family: proteins defined by an N-terminal transglutaminase substrate domain and a C-terminal four-disulphide core: J. Schalkwijk, et al.; Biochem. J. 340, 569 (1999), Abstract; Full Text

Identification and sequence analysis of two new members of the SKALP/elafin and SPAI-2 gene family. Biochemical properties of the transglutaminase substrate motif and suggestions for a new nomenclature: P.L. Zeeuwen, et al.; J. Biol. Chem. 272, 20471 (1997), Abstract; Full Text

Accelerated evolution in inhibitor domains of porcine elafin family members: I. Tamechika, et al.; J. Biol. Chem. 271, 7012 (1996), Abstract; Full Text

Elastase inhibitor elafin is a new type of proteinase inhibitor which has a transglutaminase-mediated anchoring sequence termed "cementoin": K. Nara, et al.; J. Biochem. (Tokyo) 115, 441 (1994), Abstract;

Characterization and gene sequence of the precursor of elafin, an elastase-specific inhibitor in bronchial secretions: J.M. Sallenave and A. Silva; Am. J. Respir. Cell. Mol. Biol. 8, 439 (1993), Abstract;

Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin: Q.L. Ying and S.R. Simon; Biochemistry 32, 1866 (1993), Abstract;

SKALP/elafin: an elastase inhibitor from cultured human keratinocytes. Purification, cDNA sequence, and evidence for transglutaminase cross-linking: H.O. Molhuizen, et al.; J. Biol. Chem. 268, 12028 (1993), Abstract;

Primary structure of the human elafin precursor preproelafin deduced from the nucleotide sequence of its gene and the presence of unique repetitive sequences in the prosegment: Saheki, et al.; Biochem. Biophys. Res. Commun. 185, 240 (1992), Abstract;

Purification and characterization of elastase-specific inhibitor. Sequence homology with mucus proteinase inhibitor: J.M. Sallenave and A.P. Ryle; Biol. Chem. Hoppe Seyler 372, 13 (1991), Abstract;

Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence: O. Wiedow, et al.; J. Biol. Chem. 265, 14791 (1990), Abstract; Full Text

Skin-derived antileucoproteases (SKALPs): characterization of two new elastase inhibitors from psoriatic epidermis: J. Schalkwijk, et al.; Br. J. Dermatol. 122, 631 (1990), Abstract;