Sulf-2 exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin. Mammalian Sulfs are endoproteolytically processed and secreted into the extracellular space of transfected cells, where they exhibit both arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity against intact heparin. Though the molecular weight of full length human Sulf2 is 100455 Da (870 amino acids), the endogenous Sulf2 is found by western blot to be present at molecular weights of 24.4, 33.7 and 51-60 kDa. Higher molecular weight species may be found depending on tissue and/or cell type.
Analysis of human tumor tissue and tumor cell lines suggests that HSulf-1 is misregulated in cancers. HSulf-1 is found in a variety of normal tissues but is down-regulated in tumor cell lines originating from ovarian, breast, pancreatic, renal, and hepatocellular carcinoma.
Tumors formed by cells expressing Sulf demonstrate enhanced extracellular matrix deposition. The 6-O-sulfation of heparan sulfate of myeloma tumor cells may be a critical factor in determiningand regulating the in vivo growth of this cancer.
Synthetic peptide derived from the human Sulf2 protein.
Antibody tested on human brain lysate
Provided as solution in phosphate buffered saline with 0.08% sodium azide
Product should be stored at -20°C. Aliquot to avoid freeze/thaw cycles
Western blot using Exalpha’s antigen immunoaffinity purified anti-human Sulf2 antibody (0.15 ug/ml) on human brain lysate (20 ug/lane) and developed using goat anti rbbit HRP (1:30,000)Pierce’s Super Signal West Femto.