Cloning and expression of a widely expressed receptor tyrosine phosphatase.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Cloning and expression of a widely expressed receptor tyrosine phosphatase. / Sap, J; D'Eustachio, P; Givol, D; Schlessinger, J.

In: Proceedings of the National Academy of Science of the United States of America, Vol. 87, No. 16, 1990, p. 6112-6.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Sap, J, D'Eustachio, P, Givol, D & Schlessinger, J 1990, 'Cloning and expression of a widely expressed receptor tyrosine phosphatase.', Proceedings of the National Academy of Science of the United States of America, vol. 87, no. 16, pp. 6112-6.

APA

Sap, J., D'Eustachio, P., Givol, D., & Schlessinger, J. (1990). Cloning and expression of a widely expressed receptor tyrosine phosphatase. Proceedings of the National Academy of Science of the United States of America, 87(16), 6112-6.

Vancouver

Sap J, D'Eustachio P, Givol D, Schlessinger J. Cloning and expression of a widely expressed receptor tyrosine phosphatase. Proceedings of the National Academy of Science of the United States of America. 1990;87(16):6112-6.

Author

Sap, J ; D'Eustachio, P ; Givol, D ; Schlessinger, J. / Cloning and expression of a widely expressed receptor tyrosine phosphatase. In: Proceedings of the National Academy of Science of the United States of America. 1990 ; Vol. 87, No. 16. pp. 6112-6.

Bibtex

@article{bd0f2f6054ac11dd8d9f000ea68e967b,
title = "Cloning and expression of a widely expressed receptor tyrosine phosphatase.",
abstract = "We describe the identification of a widely expressed receptor-type (transmembrane) protein tyrosine phosphatase (PTPase; EC 3.1.3.48). Screening of a mouse brain cDNA library under low-stringency conditions with a probe encompassing the intracellular (phosphatase) domain of the CD45 lymphocyte antigen yielded cDNA clones coding for a 794-amino acid transmembrane protein [hereafter referred to as receptor protein tyrosine phosphatase alpha (R-PTP-alpha)] with an intracellular domain displaying clear homology to the catalytic domains of CD45 and LAR (45% and 53%, respectively). The 142-amino acid extracellular domain (including signal peptide) of R-PTP-alpha is marked by a high serine/threonine content (32%) as well as eight potential N-glycosylation sites but displays no similarity to known proteins. Genetic mapping assigns the gene for R-PTP-alpha to mouse chromosome 2, closely linked to the Il-1a and Bmp-2a loci. The corresponding mRNA (3.0 kilobases) is expressed in most murine tissues and most abundantly expressed in brain and kidney. Antibodies against a synthetic peptide of R-PTP-alpha identified a 130-kDa protein in cells transfected with the R-PTP-alpha cDNA.",
author = "J Sap and P D'Eustachio and D Givol and J Schlessinger",
note = "Keywords: Amino Acid Sequence; Animals; Base Sequence; Blotting, Northern; Brain; Chromosome Mapping; Cloning, Molecular; DNA; Gene Expression; Gene Library; Genes; Mice; Mice, Inbred BALB C; Mice, Inbred Strains; Molecular Sequence Data; Phosphoprotein Phosphatases; Protein Tyrosine Phosphatases; Receptors, Cell Surface; Restriction Mapping; Species Specificity",
year = "1990",
language = "English",
volume = "87",
pages = "6112--6",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "16",

}

RIS

TY - JOUR

T1 - Cloning and expression of a widely expressed receptor tyrosine phosphatase.

AU - Sap, J

AU - D'Eustachio, P

AU - Givol, D

AU - Schlessinger, J

N1 - Keywords: Amino Acid Sequence; Animals; Base Sequence; Blotting, Northern; Brain; Chromosome Mapping; Cloning, Molecular; DNA; Gene Expression; Gene Library; Genes; Mice; Mice, Inbred BALB C; Mice, Inbred Strains; Molecular Sequence Data; Phosphoprotein Phosphatases; Protein Tyrosine Phosphatases; Receptors, Cell Surface; Restriction Mapping; Species Specificity

PY - 1990

Y1 - 1990

N2 - We describe the identification of a widely expressed receptor-type (transmembrane) protein tyrosine phosphatase (PTPase; EC 3.1.3.48). Screening of a mouse brain cDNA library under low-stringency conditions with a probe encompassing the intracellular (phosphatase) domain of the CD45 lymphocyte antigen yielded cDNA clones coding for a 794-amino acid transmembrane protein [hereafter referred to as receptor protein tyrosine phosphatase alpha (R-PTP-alpha)] with an intracellular domain displaying clear homology to the catalytic domains of CD45 and LAR (45% and 53%, respectively). The 142-amino acid extracellular domain (including signal peptide) of R-PTP-alpha is marked by a high serine/threonine content (32%) as well as eight potential N-glycosylation sites but displays no similarity to known proteins. Genetic mapping assigns the gene for R-PTP-alpha to mouse chromosome 2, closely linked to the Il-1a and Bmp-2a loci. The corresponding mRNA (3.0 kilobases) is expressed in most murine tissues and most abundantly expressed in brain and kidney. Antibodies against a synthetic peptide of R-PTP-alpha identified a 130-kDa protein in cells transfected with the R-PTP-alpha cDNA.

AB - We describe the identification of a widely expressed receptor-type (transmembrane) protein tyrosine phosphatase (PTPase; EC 3.1.3.48). Screening of a mouse brain cDNA library under low-stringency conditions with a probe encompassing the intracellular (phosphatase) domain of the CD45 lymphocyte antigen yielded cDNA clones coding for a 794-amino acid transmembrane protein [hereafter referred to as receptor protein tyrosine phosphatase alpha (R-PTP-alpha)] with an intracellular domain displaying clear homology to the catalytic domains of CD45 and LAR (45% and 53%, respectively). The 142-amino acid extracellular domain (including signal peptide) of R-PTP-alpha is marked by a high serine/threonine content (32%) as well as eight potential N-glycosylation sites but displays no similarity to known proteins. Genetic mapping assigns the gene for R-PTP-alpha to mouse chromosome 2, closely linked to the Il-1a and Bmp-2a loci. The corresponding mRNA (3.0 kilobases) is expressed in most murine tissues and most abundantly expressed in brain and kidney. Antibodies against a synthetic peptide of R-PTP-alpha identified a 130-kDa protein in cells transfected with the R-PTP-alpha cDNA.

M3 - Journal article

C2 - 2166945

VL - 87

SP - 6112

EP - 6116

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 16

ER -

ID: 5070134