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Receptor-type protein-tyrosine phosphatase β (RPTPβ or PTPζ) is the first mammalian tyrosine phosphatase to be characterized whose expression is limited to the nervous system. RPTP? consists of a large extracellular domain, a single transmembrane domain, and a cytoplasmic portion with two tandem catalytic domains. Three forms of RPTPβ exist which appear to be derived from alternative splicing. The 9.5kb and 6.4kb transcripts encode two transmembrane forms. The 8.5kb transcript encodes a secreted form of the extracellular domain of RPTPβ. A region of 266 amino acids in the extracellular domain shows a high degree of homology with carbonic anhydrase. This region is very similar to rat brain chondroitin sulfate proteoglycan (3F8 PG) which appears to be the rat homologue of the entire extracellular domain of human RPTPβ. The apparent molecular weight of human RPTPβ is 250kDa and approaches 300kDa when the protein is glycosylated. This antibody was generated against a region known to have a high degree of homology to other proteoglycans, such as RPTP? (75% homology).Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
