Heparinase II, 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 cell membrane and extracellular matrix, where it binds to a variety of protein ligands and regulates a wide range of biological activities, including developmental processes, angiogenesis, blood coagulation and tumor metastasis (1, 2). Heparan sulfate has a domain structure containing sulfated regions interspaced with less or nonsulfated regions (3, 4). Heparin shares the backbone structure with heparan sulfate but contains no nonsulfated regions. Heparinases are a family of lyases that release unsaturated oligosaccharides from heparin and heparan sulfate upon digestion (5). 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 active only on heparan sulfate (6, 7).\n\nSource: \nE. coli-expressed recombinant protein corresponding to Ala26-Arg772 of P. heparinus Heparinase II, with an N-terminal Met and 6-His tag\n\nMolecular Weight: \nPredicted: 86kD\nObserved: 66-75kD (SDS-PAGE, reducing conditions)\n\nSpecific Activity:\nMeasured by its ability to liberate oligosaccharides from heparin. The specific activity is >750 pmoles/min/ug, as measured under the described conditions (see Activity Assay Protocol)\n\nEndotoxin Level:\n<1EU/ug (LAL method)\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

H1892-01A

Size

10ug

Form

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

Purity

(same/more than) 95% (SDS-PAGE, reducing conditions; 5ug protein loaded per lane; visualized by colloidal Coomassie blue staining)

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.