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      Molecular cloning of cDNAs encoding human GLEPP1, a membrane protein tyrosine phosphatase: characterization of the GLEPP1 protein distribution in human kidney and assignment of the GLEPP1 gene to human chromosome 12p12-p13.

      Genomics
      Amino Acid Sequence, Animals, Antibodies, Monoclonal, immunology, Base Sequence, Cell Size, Chromosome Mapping, Chromosomes, Human, Pair 12, DNA, Complementary, genetics, Genes, Humans, Kidney Glomerulus, cytology, enzymology, Membrane Proteins, analysis, physiology, Molecular Sequence Data, Molecular Weight, Protein Tyrosine Phosphatases, Rabbits, Receptor-Like Protein Tyrosine Phosphatases, Class 3, Receptors, Cell Surface, Recombinant Fusion Proteins, Sequence Homology, Amino Acid

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          Abstract

          Human glomerular epithelial protein 1 (GLEPP1), a receptor-like membrane protein tyrosine phosphatase (PTPase), was cloned and sequenced from a human renal cortical cDNA library. The human nucleotide and derived amino acid sequences were, respectively, 90 and 97% identical to those of rabbit. Human GLEPP1 is predicted to contain 1188 amino acids. The predicted mature protein is 1159 amino acids long and contains a large extracellular domain, a single transmembrane domain, and a single intracellular PTPase domain. Monoclonal and polyclonal antibodies raised against a human GLEPP1 fusion protein recognized a protein with distribution restricted to the glomerulus in human kidney and with an apparent molecular weight of approximately 200 kDa. The GLEPP1 gene was assigned to human chromosome 12p12-p13 by fluorescence in situ hybridization.

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