antibody

Rabbit anti-human heparanase polyclonal Antibody

MBS711555

0.05 mL

375 USD

polyclonal

rabbit

nonconjugated

human, mouse

ELISA, immunohistochemistry, enzyme immunoassay

Antibody

Rabbit anti-human heparanase polyclonal Antibody

heparanase

heparanase; HPSE; HPA; HPR1; HPSE1; HSE1

heparanase; Heparanase; heparanase; heparanase-1; endo-glucoronidase; heparanase; Endo-glucoronidase; Heparanase-1; Hpa1

HPSE; HPSE; HPA; HPA1; HPR1; HSE1; HPSE1; HEP; HPA; HPA1; HPR1; HPSE1; HSE1; Hpa1

HPSE_HUMAN

Polyclonal

IgG

Rabbit

Human, Mouse; Other species are not tested. Please decide the specificity by homology.

543

Antigen Affinity Purified

Liquid

ELISA (EIA), Immunohistochemistry (IHC)

Tested applications:. ELISA: Use at an assay dependent dilution. WB: 1:500-1:5000 . IHC: 1:20-1:200 . IF: 1:10-1:100 (Recommender dilutions) . Positive WB detected in: Jurkat cells . Positive IHC detected in: Human liver cancer tissue, human placenta tissue. Positive IF detected in: HeLa cells, HepG2 cells

Immunogen: Human HPSE. Conjugate : Non-conjugated

Storage Buffer: PBS with 0.1% sodium azide and 50% glycerol pH 7.3.

Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparansulfate 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.

5880863

AAD54941.1

Disease Pathway (530764); Glycogen Storage Diseases Pathway (980468); Glycosaminoglycan Degradation Pathway (82981); Glycosaminoglycan Degradation Pathway (355); Glycosaminoglycan Metabolism Pathway (645297); HS-GAG Degradation Pathway (645307); Heparan Sulfate Degradation Pathway (413377); Heparan Sulfate Degradation Pathway (468270); Heparan Sulfate/heparin (HS-GAG) Metabolism Pathway (645304); MPS I - Hurler Syndrome Pathway (685537)

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]

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; Secreted; EC 3.2.1.166; Hydrolase; Secreted, signal peptide; 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: protein dimerization activity; syndecan binding; 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

0.05 mL

375 USD

0.15 mL

715