Human HS(Heparan Sulfate) ELISA Kit (E-EL-H2364)

This ELISA kit uses the Sandwich-ELISA principle. The micro ELISA plate provided in this kit has been pre-coated with an antibody specific to Human HS. Standards or samples are added to the micro ELISA plate wells and combined with the specific antibody. Then a biotinylated detection antibody specific for Human HS and Avidin-Horseradish Peroxidase (HRP) conjugate are added successively to each micro plate well and incubated. Free components are washed away. The substrate solution is added to each well. Only those wells that contain Human HS, biotinylated detection antibody and Avidin-HRP conjugate will appear blue in color. The enzyme-substrate reaction is terminated by the addition of stop solution and the color turns yellow. The optical density (OD) is measured spectrophotometrically at a wavelength of 450 nm ± 2 nm. The OD value is proportional to the concentration of Human HS. You can calculate the concentration of Human HS in the samples by comparing the OD of the samples to the standard curve.

Heparanase (HPA) is an endo-beta-D-glucuronidase encoded by the HPSE gene and the only mammalian enzyme known to cleave internal glycosidic bonds within heparan sulfate chains of proteoglycans. It is synthesized as a latent proenzyme that is processed in lysosomes by cathepsin L and secreted as a heterodimer of 8 and 50 kDa subunits, and it acts at mildly acidic pH to cut heparan sulfate at sites of low sulfation, mediating extracellular matrix degradation and remodeling. By cleaving heparan sulfate, heparanase releases matrix-bound growth factors, cytokines and chemokines, increases their bioavailability and facilitates cell migration, invasion, extravasation and syndecan shedding. Acting together, these effects promote tumor metastasis, angiogenesis, lymphangiogenesis, inflammation, coagulation and wound repair, and heparanase additionally drives exosome secretion, autophagy and gene transcription through non-enzymatic mechanisms. Its expression is up-regulated in many carcinomas and hematological malignancies, correlates with invasion, metastatic dissemination, angiogenesis and poor prognosis, and is low in most normal adult tissues apart from placenta, platelets and activated immune cells. Heparanase is therefore an important target in tumor metastasis, inflammation and proteinuric kidney disease, and heparanase inhibitors derived from heparin and other sulfated polysaccharides have been developed to limit tumor progression. Measurement of heparanase supports research on tumor biology, angiogenesis and extracellular matrix remodeling, and circulating enzyme levels and activity are studied as markers of invasive and metastatic potential.