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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
Summary
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.
- 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.
