catalog number :
MBS142402
products type :
Recombinant Protein
products full name :
Recombinant Human Heparanase-1 WB Control
products short name :
Heparanase-1 WB Control
products name syn :
HPSE WB; Recombinant Human Heparanase-1 WB Control; HPSE WB
other names :
heparanase isoform 1 preproprotein; Heparanase; heparanase; endo-glucoronidase; heparanase-1; heparanase; Endo-glucoronidase; Heparanase-1; Hpa1
products gene name :
HPSE
other gene names :
HPSE; HPSE; HPA; HPA1; HPR1; HSE1; HPSE1; HEP; HPA; HPA1; HPR1; HPSE1; HSE1; Hpa1
uniprot entry name :
HPSE_HUMAN
products categories :
ENZYMES; Enzymes
ncbi acc num :
NP_001092010.1
ncbi gb acc num :
NM_001098540.2
ncbi mol weight :
42,791 Da
ncbi pathways :
Defective B3GAT3 Causes JDSSDHD Pathway (1127588); Defective B4GALT1 Causes B4GALT1-CDG (CDG-2d) Pathway (1127592); Defective B4GALT7 Causes EDS, Progeroid Type Pathway (1127587); Defective CHST14 Causes EDS, Musculocontractural Type Pathway (1127591); Defective CHST3 Causes SEDCJD Pathway (1127590); Defective CHST6 Causes MCDC1 Pathway (1127593); Defective CHSY1 Causes TPBS Pathway (1127589); Defective EXT1 Causes Exostoses 1, TRPS2 And CHDS Pathway (1127594); Defective EXT2 Causes Exostoses 2 Pathway (1127595); Defective PAPSS2 Causes SEMD-PA Pathway (1127586)
ncbi summary :
Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. The protein encoded by this gene is an enzyme that cleaves heparan sulfate proteoglycans to permit cell movement through remodeling of the extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2011]
uniprot summary :
HPSE: 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 procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extacellular 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. Belongs to the glycosyl hydrolase 79 family. Protein type: Glycan Metabolism - glycosaminoglycan degradation; Hydrolase; Secreted, signal peptide; EC 3.2.1.166; Secreted; Extracellular matrix. Chromosomal Location of Human Ortholog: 4q21.3. Cellular Component: nucleoplasm; lysosomal lumen; intracellular membrane-bound organelle; lysosome; lysosomal membrane; extracellular region; nucleus; lipid raft. Molecular Function: syndecan binding; protein dimerization activity; protein binding; beta-glucuronidase activity; heparanase activity. Biological Process: positive regulation of hair follicle development; positive regulation of protein kinase B signaling cascade; proteoglycan metabolic process; glycosaminoglycan catabolic process; positive regulation of blood coagulation; heparan sulfate proteoglycan catabolic process; glycosaminoglycan metabolic process; cell-matrix adhesion; positive regulation of osteoblast proliferation; carbohydrate metabolic process; pathogenesis; regulation of hair follicle development