HPSE WB
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Description
Recombinant Heparanase protein HPA1 is produced in CHO cells.
The protein is purified by several orthogonal chromatography steps.
Product Specs
Heparanase is an enzyme, specifically an endo-β-D-glucuronidase, that breaks down heparan sulfate chains found on heparan sulfate proteoglycans (HSPGs) within the extracellular matrix (ECM). This degradation process is crucial for ECM breakdown, facilitating the movement and penetration of tumor cells and inflammatory leukocytes (1,2,3). The breakdown of HSPGs by heparanase releases growth factors and cytokines, which in turn promote cell growth and directed cell movement (4,5). Structurally, heparanase is a two-part molecule (heterodimer) composed of a 50 kDa subunit containing the active site and an 8 kDa subunit. Initially produced in a latent 65 kDa precursor form, it undergoes proteolytic processing to become active (1,6). Heparanase is highly present in myeloid leukocytes like neutrophils, platelets, and the human placenta. Studies have shown elevated levels of human heparanase in various primary tumor types, often correlating with increased tumor invasion, blood vessel formation, and unfortunately, poorer survival rates (7,8).
Recombinant Heparanase protein HPA1 is generated in Chinese hamster ovary (CHO) cells and undergoes purification using multiple distinct chromatography steps.
Concentration: 1 microgram per milliliter
Content: 100 nanograms
Buffer: LDS-PAGE buffer (140 mM Tris buffer pH 8.5, 10% Glycerol, 2% LDS, 0.015% EDTA, 1.88% (v/v) of 1% Serva Blue G250 and 0.625% (v/v) of 1% Phenol red).
Serves as a positive control in western blot analysis.
Utilize 20 microliters of recombinant human heparanase 1 (HPA1) per lane to serve as a control when using either monoclonal anti-HPA1 clone HP3/17 antibodies (Catalog Number: Ins-AB-04001) or polyclonal rabbit anti-HPA1 antibody (Catalog Number: Ins-AB-04002).
Store at -20 degrees Celsius. Repeated freezing and thawing cycles should be avoided.
Product Science Overview
Heparanase is an endo-β-D-glucuronidase that cleaves heparan sulfate (HS) side chains of HSPGs, resulting in shorter oligosaccharide chains . The enzyme is synthesized as a latent 65 kDa precursor, which is proteolytically processed into its active form, consisting of a 50 kDa subunit harboring the active site and an 8 kDa subunit . This heterodimeric structure is essential for its enzymatic activity.
Heparanase is involved in various physiological and pathological processes, including:
- ECM Degradation: Facilitates the migration and extravasation of tumor cells and inflammatory leukocytes by degrading the ECM .
- Release of Growth Factors: Upon degradation of HSPGs, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis .
- Tumor Progression: Heparanase is highly expressed in various types of primary tumors, correlating with increased tumor invasiveness and vascularity .
Due to its role in ECM degradation and tumor progression, heparanase is considered a potential target for cancer therapy. It has been implicated in promoting arterial and stent thrombosis by cleaving anticoagulant heparan sulfate proteoglycans . Additionally, heparanase interacts with resistin, influencing inflammatory conditions .
Recombinant Human Heparanase-1 WB Control is used as a positive control in western blot analysis. It is prepared by using 20 μl of the recombinant protein per lane, in conjunction with monoclonal or polyclonal antibodies against heparanase . This control ensures the accuracy and reliability of western blot results.
