3.4.23.B1: napsin
This is an abbreviated version!
For detailed information about napsin, go to the full flat file.
Word Map on EC 3.4.23.B1
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3.4.23.B1
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adenocarcinoma
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thyroid
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pulmonary
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resect
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cytokeratins
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non-small
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factor-1
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papillary
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immunophenotype
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alk
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endometrioid
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synaptophysin
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chromogranin
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adenosquamous
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medicine
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calretinin
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analysis
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lepidic
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a-positive
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diagnostics
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immunomarkers
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nonpulmonary
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sarcomatoid
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immunoprofile
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amacr
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micropapillary
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cytopathol
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mammaglobin
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mucicarmine
- 3.4.23.B1
- adenocarcinoma
- thyroid
- pulmonary
-
resect
-
cytokeratins
-
non-small
- factor-1
-
papillary
-
immunophenotype
- alk
-
endometrioid
-
synaptophysin
-
chromogranin
-
adenosquamous
- medicine
-
calretinin
- analysis
-
lepidic
-
a-positive
- diagnostics
-
immunomarkers
-
nonpulmonary
-
sarcomatoid
-
immunoprofile
- amacr
-
micropapillary
-
cytopathol
-
mammaglobin
-
mucicarmine
Reaction
belongs to the aspartic proteinases =
Synonyms
napsin, napsin A, napsin-A, TA02 protein, TAO2
ECTree
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Specific Activity
Specific Activity on EC 3.4.23.B1 - napsin
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additional information
amounts and activities of napsin A studied by immunoblotting and specific substrate cleavage, general defect in napsin A expression or activity not observed as cause for abnormal surfactant accumulation in juvenile pulmonary alveolar proteinosis
additional information
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amounts and activities of napsin A studied by immunoblotting and specific substrate cleavage, general defect in napsin A expression or activity not observed as cause for abnormal surfactant accumulation in juvenile pulmonary alveolar proteinosis
additional information
expression of napsin A determined by mRNA in situ hybridization in renal cells, tumor-suppression activity determined, mutation of one of the aspartic acid residues in the napsin A catalytic site shown to affect enzyme activity but not processing, glycosylation or intracellular localization, napsin A shown to inhibit tumor growth of transformed cells by a mechanism independent of its catalytic activity
additional information
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expression of napsin A determined by mRNA in situ hybridization in renal cells, tumor-suppression activity determined, mutation of one of the aspartic acid residues in the napsin A catalytic site shown to affect enzyme activity but not processing, glycosylation or intracellular localization, napsin A shown to inhibit tumor growth of transformed cells by a mechanism independent of its catalytic activity
additional information
napsin A as a diagnostic marker for lung adenocarcinoma tested, comparative study between napsin A and thyroid transcription factor TTF-1 by immunohistochemical analysis, napsin A reactivity in more than 75% of the tumor cells in 9/10 positive cases obtained, napsin A shown to be useful as an alternative marker to thyroid transcription factor TTF-1 in cytological diagnosis of effusions with low amounts of tumor cells
additional information
napsin A-expressing cells shown to form tumors in SCID mice with lower efficiency and slower onset compared to vector-transfected control cells