Anti-Heparanase 1/Hpse Antibody Picoband® Fluoro647 Conjugated

Heparanase, also known as HPSE, is an enzyme that acts both at the cell-surface and within the extracellular matrix to degrade polymeric heparan sulfate molecules into shorter chain length oligosaccharides. Heparanase is an endo-beta-D-glucuronidase capable of cleaving heparan sulfate and has been implicated in inflammation and tumor angiogenesis and metastasis. The successful penetration of the endothelial cell layer that lines the interior surface of blood vessels is an important process in the formation of blood borne tumour metastases. Heparan sulfate proteoglycans are major constituents of this layer and it has been shown that increased metastatic potential corresponds with increased heparanase activity for a number of cell lines.

E.coli-derived mouse Heparanase 1 recombinant protein (Position: K206-K457) . Mouse Heparanase 1 shares 80.2% and 96.4% amino acid (aa) sequence identity with human and rat Heparanase 1, respectively.

Expressed in skin, mainly in the stratum granulosum and the first layer of the stratum corneum in the upper part of the epidermis. Also detected in hair follicles and in sebaceous glands. .

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. .

1. Hulett MD, Freeman C, Hamdorf BJ, Baker RT, Harris MJ, Parish CR (July 1999), Cloning of mammalian heparanase, an important enzyme in tumor invasion and metastasis, Nature medicine 5 (7) : 803–9. 2. Nakajima M, Irimura T, Nicolson GL. (1988), Heparanases and tumor metastasis, J. Cell. Biochem. 36 (2) : 157–167. 3. Toyoshima, M.; Nakajima, M. : Human heparanase: purification, characterization, cloning, and expression. J. Biol. Chem. 274: 24153-24160, 1999. 4. Vlodavsky I, Friedmann Y, Elkin M, Aingorn H, Atzmon R, Ishai-Michaeli R, Bitan M, Pappo O, Peretz T, Michal I, Spector L, Pecker I (July 1999), Mammalian heparanase: gene cloning, expression and function in tumor progression and metastasis, Nature medicine 5 (7) : 793–802. 5. Vlodavsky I, Goldshmidt O, Zcharia E, et al. (2003), Mammalian heparanase: involvement in cancer metastasis, angiogenesis and normal development., Semin. Cancer Biol. 12 (2) : 121–9.

Lysosome membrane ; Peripheral membrane protein . Secreted . Nucleus . Proheparanase is secreted via vesicles of the Golgi. Interacts with cell membrane heparan sulfate proteoglycans (HSPGs) . Endocytosed and accumulates in endosomes. Transferred to lysosomes where it is proteolytically cleaved to produce the active enzyme. Under certain stimuli, transferred to the cell surface. Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates in perinuclear lysosomal vesicles. Heparin retains proheparanase in the extracellular medium (By similarity) . Associates with lipid rafts. .