Recombinant Human Heparanase 1 protein (denatured) (His tag N-Terminus)
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Recombinant Human Heparanase 1 protein (denatured) (His tag N-Terminus) is a Human Full Length protein, in the 36 to 543 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
View Alternative Names
HEP, HPA, HPA1, HPR1, HPSE1, HSE1, HPSE, Heparanase, Endo-glucoronidase, Heparanase-1, Hpa1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Heparanase 1 protein (denatured) (His tag N-Terminus) (AB181927)
15% SDS-PAGE analysis of ab181927 (3μg)
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
When heparan sulfate is cleaved by Heparanase 1 it causes the release of HS-bound growth factors and cytokines making them available to cells. This enzymatic activity facilitates cell proliferation and angiogenesis affecting processes important for tissue repair and cancer progression. Heparanase 1 does not require a complex for its function but operates as a monomeric enzyme. Its activity is investigated using assays like heparanase activity assays or ELISA for measuring the enzyme's activity in different biological contexts including mouse models.
Pathways
The activity of Heparanase 1 intersects significantly with the regulation of angiogenesis and cell signaling pathways such as the VEGF and FGF pathways. These pathways are important for new blood vessel formation making them significant in both normal development and cancer. Heparanase 1 interacts with proteins such as VEGF which is important for blood vessel growth and integrins which are involved in cell-matrix interactions and signaling.
Specifications
Form
Liquid
General info
Function
Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as a procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis.
Sequence similarities
Belongs to the glycosyl hydrolase 79 family.
Post-translational modifications
Proteolytically processed. The cleavage of the 65 kDa form leads to the generation of a linker peptide, and 8 kDa and 50 kDa products. The active form, the 8/50 kDa heterodimer, is resistant to degradation. Complete removal of the linker peptide appears to be a prerequisite to the complete activation of the enzyme.. N-glycosylated. Glycosylation of the 50 kDa subunit appears to be essential for its solubility.
Subcellular localisation
Lysosome membrane
Target data
Product promise
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