General description
Recombinant human heparanase-1 is expressed in human HEK 293 cells as an active heterodimer glycoprotein containing a 50 kDa subunit and a 8 kDa subunit. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports higher specific activity of the protein. The protein is produced with no artificial tags.
Biochem/physiol Actions
Heparanase-1 (heparanase) is the only heparan sulfate degrading endoglycosidase. It is involved in the regulation of multiple biological processes that increase tumor growth, metastasis, angiogenesis and inflammation. Heparanase is involved in ECM remodeling and heparan sulfate-linked biological molecules release, including cytokines and growth factors. Heparanase cleaves the heparan sulfate side chains of heparan sulfate proteoglycans into fragments of 10–20 sugar units.
Heparanase is initially translated as a preproenzyme containing a signal peptide. Cleavage of the signal sequence yields a latent 65 kDa pro-heparanase, which must undergo further processing for activity. Mature active heparanase is a heterodimer consisting an N-terminal 8 kDa subunit and a C-terminal 50 kDa subunit.
Other Notes
One heparanase activity unit is the amount of heparanase required to cleave 1 pmol of pentasaccharide to disaccharide and trisaccharide in one minute, at 37 °C, pH 5.0.
| recombinant | expressed in HEK 293 cells |
| assay | ≥95.0% (SDS-PAGE) |
| form | lyophilized powder |
| impurities | ≤1.00 EU/μg (LAL) |
| UniProt accession no. | Q9Y251 |
| shipped in | ambient |
| storage temp. | −20°C |
