Name
Elafin, Human, Recombinant
Catalog nr
HC4011 (lot number and expiry date are indicated on the label)
Short description
Elafin is an epithelial proteinase inhibitor also known under various other names such as Skin-derived Anti leukoproteinase (SKALP) and Elastase-Specific Inhibitor (ESI). Elafin belongs to the Trappin gene family and was given the systematic name Trappin-2. The Trappin family is defined by a N-terminal transglutaminase substrate domain and a C-terminal four disulphide core. Trappins have been...
Size
50 µg
Application
Technical datasheet
Description
Elafin is an epithelial proteinase inhibitor also known under various other names such as Skin-derived Anti leukoproteinase (SKALP) and Elastase-Specific Inhibitor (ESI). Elafin belongs to the Trappin gene family and was given the systematic name Trappin-2. The Trappin family is defined by a N-terminal transglutaminase substrate domain and a C-terminal four disulphide core. Trappins have been suggested to play a role in the regulation of inflammation and in protection against tissue damage in stratified epithelia. Elafin is an inhibitor of leukocyte elastase and proteinase-3 and in addition it is a substrate for transglutaminases. The protein is constitutively expressed in various epithelia including those of hair follicles, oesophagus, vagina and oral cavity. Elafin is not present in normal human skin but is strongly induced during inflammation as in psoriasis and wound healing. The full-length protein is translated as a 12.3 kDa protein of 117 amino acids termed pre-elafin or Trappin-2. Cleavage of the signal peptide yields a mature protein with a molecular mass of 9.9 kDa. The 9.9 kDa secreted protein is the major form found in culture medium. In skin extracts a 6 kDa form comprising the 57 most C-terminal amino acids is present, which is the form of elafin originally described by Wiedow et al. In serum both the 9.9 and the 6 kDa form appear to be present.
Formulation
Lyophilized product in PBS, containing 50 µg. Reconstitute the vial by injection of 1 ml distilled or de ionized water (Caution: vial is under vacuum).
Species
Human, E.coli-derived
Use
For dilutions use protein stabilized phosphate buffered saline, pH 7. (Never use serum/plasma).
Storage and stability
Lyophilized product should be stored at 4°C. After reconstitution store stock solutions in aliquots at -20°C. Avoid repeated freezing and thawing. Under recommended storage conditions, product is stable for more than one year.
References
1.Wiedow, O et al; Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence. J Biol Chem 1990, 265: 14791

Erratum in: J Biol Chem 1991, 266: 3356

2. Ying, Q et al; Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin. Biochemistry 1993, 32: 1866

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

4. Ying, Q et al; Kinetics of the inhibition of proteinase 3 by elafin. Am J Respir Cell Mol Biol 2001, 24: 83
Precautions
For research use only. Not for use in or on humans or animals or for diagnostics. It is the responsibility of the user to comply with all local/state and Federal rules in the use of this product. Hycult Biotech is not responsible for any patent infringements that might result with the use of or derivation of this product.
Also available
References
1.Wiedow, O et al; Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence. J Biol Chem 1990, 265: 14791

Erratum in: J Biol Chem 1991, 266: 3356

2. Ying, Q et al; Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin. Biochemistry 1993, 32: 1866

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

4. Ying, Q et al; Kinetics of the inhibition of proteinase 3 by elafin. Am J Respir Cell Mol Biol 2001, 24: 83