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Recombinant P. heparinus Heparinase II Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 6336-GH

R&D Systems, part of Bio-Techne
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6336-GH-010

Key Product Details

Source

E. coli

Accession #

Conjugate

Unconjugated

Applications

Enzyme Activity

Product Specifications

Source

E. coli-derived p. heparinus Heparinase II protein
Ala26-Arg772, with an N-terminal Met and 6-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

86 kDa

SDS-PAGE

66-75 kDa, reducing conditions

Activity

Measured by its ability to liberate oligosaccharides from heparin.
The specific activity is >750 pmol/min/μg, as measured under the described conditions.

Scientific Data Images for Recombinant P. heparinus Heparinase II Protein, CF

Recombinant P. heparinus Heparinase II Protein Enzyme Activity

Recombinant P. heparinus Heparinase II Protein Enzyme Activity

Heparinase II digestion of Heparin Sulfate (200 μg) is assessed in a 5-minute kinetic assay by monitoring absorbance at 232 nm. R&D SystemsP. heparinusHeparinase I (catalog # 6336-GH) exhibits activity at 2595.6 pm/min/μg.

Formulation, Preparation and Storage

6336-GH
Formulation Supplied as a 0.2 μm filtered solution in PBS.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: Heparinase II

Heparan sulfate is a sulfated glycosaminoglycan with the repeating disaccharide units of ‑4HexA1,4GlcNAc beta1-. 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 non-sulfated regions (3, 4). 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 (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).

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.

UniProt

Additional Heparinase II Products

Product Documents for Recombinant P. heparinus Heparinase II Protein, CF

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant P. heparinus Heparinase II Protein, CF

For research use only

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