Heparinase III, Recombinant, P. heparinus

Heparan sulfate is a sulfated glycosaminoglycan with the repeating disaccharide units of -4HexA1,4GlcNAcb1-. It is usually attached to the protein cores of proteoglycans found on the cell membrane and in the extracellular matrix where it binds to a variety of protein ligands and regulates a wide range of biological activities. Heparan sulfate has a domain structure where sulfated regions are interspaced with less or non-sulfated regions. Heparin shares the backbone structure with heparan sulfate but contains no non-sulfated regions. Heparinases are a family of lyases that release unsaturated oligosaccharides from heparin and heparan sulfate upon digestion. Heparinase I recognizes highly sulfated regions and is more specific for heparin. Heparinase II digests both heparin and heparan sulfate. Heparinase III prefers less-sulfated regions and is more active on heparan sulfate.\n\nSource:\nE. coli-expressed recombinant protein corresponding to Gln25-Pro659 of P. heparinus Heparinase III, with an N-terminal Met and 6-His tag\n\nMolecular Weight: \nPredicted: 74kD\nObserved: 66kD (SDS-PAGE, reducing conditions)\n\nActivity: Measured by its ability to liberate oligosaccharides from heparin. \n\nSpecific Activity: >3,000 pmoles/min/ug\n\nStorage and Stability:\nAliquot to avoid repeated freezing and thawing. Store at -70 degrees C. Aliquots are stable for 6 months at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

H1892-01

Size

10ug

Form

Supplied as a sterile-filtered liquid in Tris-buffered saline containing glycerol

Purity

(same/more than) 95% (SDS-PAGE, reducing conditions; 5ug protein loaded per lane; visualized by colloidal Coomassie blue staining). Endotoxin: <1.0 EU/1ug (LAL).

References

1. MacArthur, J. M. et al. (2007) J. Clin. Invest. 117:153. 2. Esko, J. D. and Selleck, S. B. (2002) Annu. Rev. Biochem. 71:435. 3.Maccarana, M. et al. (1996) J. Biol. Chem. 271:17804. 4. Linker, A. and Hovingh, P. (1975) Biochim. Biophys. Acta. 385:324. 5. Linker, A. and Hovingh, P. (1965) J. Biol. Chem. 240:3724. 6. Su, H. et al. (1996) Appl. Environ. Microbiol. 62:2723. 7. Hovingh, P. and Linker, A. (1970) J. Biol. Chem. 245:6170.