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Literature summary for 3.2.1.166 extracted from
- Bacterial expression and functional reconstitution of human heparanase (2014), Carbohydr. Res., 389, 72-77.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged smaller 8 kDa subunit in Escherichia coli strain BL21 (DE3)plysS | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular matrix | - |
Homo sapiens | 31012 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 8000 | - |
1 * 50000 + 1 * 8000, SDS-PAGE | Homo sapiens |
| 50000 | - |
1 * 50000 + 1 * 8000, SDS-PAGE | Homo sapiens |
| 65000 | - |
1 * 65000, precursor polypeptide, SDS-PAGE | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the 65 kDa precursor polypeptide that is enzymatically inactive. Proteolytic excision by cathepsin L of a 48 amino acid peptide yields an active heterodimer comprising 8 and 50 kDa subunits | Homo sapiens |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purifiecation of the His-tagged smaller subunit fragment of the human heparanase to homogeneity by immobilized metal affinity chromatography and dialysis from Escherichia coli strain BL21 (DE3)plysS | Homo sapiens |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | 1 * 50000 + 1 * 8000, SDS-PAGE | Homo sapiens |
| monomer | 1 * 65000, precursor polypeptide, SDS-PAGE | Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4.2 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | human heparanase is a heparan sulfate degrading enzyme located in the extracellular matrix playing a decisive role in angiogenesis and tumor metastasis | Homo sapiens |
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Release 2023.1 (January 2023)
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