Reactive species
Human;Rat;Mouse;
Applications
WB;IHC;IF;ELISA
Antibody type
Polyclonal Antibody
Immunogen
The antiserum was produced against synthesized peptide derived from the Internal region of human HPSE. AA range:241-290
Specificity
HPA1 Polyclonal Antibody detects endogenous levels of HPA1 protein.
Constitute
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Source
Polyclonal, Rabbit,IgG
Dilution rate
WB: 1/500 - 1/2000. IHC-p: 1/100-1/300. ELISA: 1/20000.. IF 1:50-200
Purification process
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Other name
HPSE; HEP; HPA; HPA1; HPR1; HPSE1; HSE1; Heparanase; Endo-glucoronidase; Heparanase-1; Hpa1
Background
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],
Function
enzyme regulation:Inhibited by EDTA, laminarin sulfate and, to a lower extent, by heparin and sulfamin and activated by calcium and magnesium.,function:Endoglycosidase which is a cell surface and extracellular matrix-degrading enzyme. Cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Also implicated in the extravasation of leukocytes and tumor cell lines. Due to its contribution to metastasis and angiogenesis, it is considered to be a potential target for anti-cancer therapies.,PTM:N-glycosylated. Glycosylation of the 50 kDa subunit appears to be essential for its solubility.,PTM:Proteolytically processed. The cleavage of the 65 kDa form leads to the generation of a linker peptide, 8 kDa and 50 kDa product. The active form, the 8/50 kDa heterodimer, is resistant to degradation. Complete removal of the linker peptide appears to be a pre
