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Related Experiment Videos

Human napsin A: expression, immunochemical detection, and tissue localization.

V Schauer-Vukasinovic1, D Bur, D Kling

  • 1F. Hoffmann-La Roche Ltd., Pharma Division, Preclinical Research, Grenzacherstrasse 124, CH-4070, Basel, Switzerland.

FEBS Letters
|December 2, 1999
PubMed
Summary
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Researchers identified a novel aspartic proteinase, napsin A, in humans and mice. An antibody was developed to detect napsin A, confirming its expression as a 38 kDa protein in kidney and lung tissues.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • A novel aspartic proteinase, napsin, has been identified in human and mouse.
  • Napsin shares high structural similarity with cathepsin D, enabling the creation of a structural model for human napsin A.

Purpose of the Study:

  • To develop a specific antibody for human napsin A.
  • To monitor the expression of recombinant human napsin A.
  • To investigate the tissue-specific expression of napsin A.

Main Methods:

  • Structural modeling of human napsin A based on cathepsin D similarity.
  • Identification of a potential epitope (SFYLNRDPEEPDGGE).
  • Antibody generation in rabbits against the identified epitope.
  • Western blot analysis to confirm antibody specificity and protein size.

Related Experiment Videos

  • Immunohistochemical studies for tissue expression analysis.

    • Main Results:

    • A specific antibody against human napsin A was successfully generated.
    • Western blot confirmed human napsin A expression as a single-chain protein (approx. 38 kDa).
    • Immunohistochemistry revealed high napsin A expression in human kidney and lung, with low expression in spleen.

    Conclusions:

    • The developed antibody is a valuable tool for detecting and studying human napsin A.
    • Human napsin A is expressed as a 38 kDa protein.
    • Napsin A shows distinct tissue-specific expression patterns, predominantly in kidney and lung.