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Human Monoclonal NAPSA Primary Antibody for IHC (p), IHC - ABIN259020
Hirano, Auer, Maeda, Hagiwara, Okada, Ohira, Okuzawa, Fujioka, Franzén, Hibi, Seito, Ebihara, Kato: Human tissue distribution of TA02, which is homologous with a new type of aspartic proteinase, napsin A. in Japanese journal of cancer research : Gann 2000
Show all 2 Pubmed References
Fruit Fly (Drosophila melanogaster) Polyclonal NAPSA Primary Antibody for WB - ABIN2668697
Kimura: The Nap family proteins, CG5017/Hanabi and Nap1, are essential for Drosophila spermiogenesis. in FEBS letters 2013
Dog (Canine) Polyclonal NAPSA Primary Antibody for ICC, IF - ABIN4337855
Mangan, Sietsema, Li, Moore, Citi, Prekeris: Cingulin and actin mediate midbody-dependent apical lumen formation during polarization of epithelial cells. in Nature communications 2016
Human Monoclonal NAPSA Primary Antibody for IHC, ELISA - ABIN1724854
Aikawa, Kawahara, Hattori, Yamaguchi, Abe, Taira, Azuma, Kage: Comparison of the expression levels of napsin A, thyroid transcription factor-1, and p63 in nonsmall cell lung cancer using cytocentrifuged bronchial brushings. in Cancer cytopathology 2011
Napsin A is of value in resolving diagnostic confusion between gastric-type adenocarcinoma (GAS) and clear cell carcinoma (CCC), whereas HNF1beta lacks specificity and its use in this setting is discouraged.
Raspberry bodies and hyaline globules with positive napsin A immunoexpression are useful features in diagnosing clear cell carcinoma.
These data indicated that napsin A expression may inhibit TGFbetalinduced EMT and was negatively associated with EMTmediated erlotinib resistance, suggesting that napsin A expression may improve the sensitivity of lung cancer cells to EGFRTKI through the inhibition of EMT.
Although napsin A is infrequently expressed in endometrial carcinomas, positive results of napsin A immunostaining in endometrial neoplasms might support the diagnosis of clear cell carcinoma when the pathologic differential diagnosis includes other histologic subtypes
Immunohistochemical detection of thyroid transcription factor 1, Napsin A, and P40 fragment of TP63 can be used in the subclassification of non-small cell lung carcinomas.
it may be useful to combine NAPA and TTF-1 for increased sensitivity in lung cancer diagnostics. There is no substantial difference between monoclonal and polyclonal p40 and between different NAPA clones, whereas there is a difference between the TTF-1 clones 8G7G3/1 and SPT24
To the best of our knowledge, expression of monoclonal Napsin A in lymphomas has never been reported. ALK-DLBCL should be considered in the differential diagnosis when evaluating a Napsin A-positive tumor of poorly differentiated morphology and of unknown primary
It is important for pathologists to be aware that breast carcinomas with apocrine features can express napsin A.
High Napsin A expression is associated with adenocarcinoma in non-small cell lung carcinoma.
Napsin-A, and Desmocollin-3 were sensitive and specific markers for the diagnosis of AC and SCC, respectively. Both markers allowed classification of 54/60 cases into either AC or SCC.
napsin A is aberrantly expressed in a subset of lymphomas
CK7, TTF-1 and napsin A are predominantly expressed in primary lung adenocarcinoma patients, with CDX-2 being inconsistently expressed.
The immunocytochemical expressions of napsin A and p40 in imprint cytology seem to be of great utility for the accurate histological differentiation of lung cancers.
Combining HNF-1beta and napsin A may distinguish clear cell carcinoma from high-grade serous carcinoma, endometrioid adenocarcinoma and metastatic Krukenberg tumors.
napsin A is another sensitive and specific marker for distinguishing ovarian clear cell tumors (especially adenocarcinomas) from other ovarian tumors
Napsin A is expressed in a broad spectrum of renal neoplasms.
Low expression levels of NAPSA is associated with lung adenocarcinoma.
In diagnosis of ovarian clear cell carcinoma, Napsin A is specific but of intermediate sensitivity.
Napsin A is frequently expressed in ovarian and endometrial clear cell carcinomas.
Data indicate that polyclonal but not monoclonal napsin A antibody has a virtually universal nonspecific labeling in mucinous adenocarcinomas of various sites.
The activation peptides of aspartic proteinases plays role as inhibitors of the active site. These peptide segments, or pro-parts, are deemed important for correct folding, targeting, and control of the activation of aspartic proteinase zymogens. The pronapsin A gene is expressed predominantly in lung and kidney. Its translation product is predicted to be a fully functional, glycosylated aspartic proteinase precursor containing an RGD motif and an additional 18 residues at its C-terminus.
, asp 4
, aspartyl protease 4
, kidney-derived aspartic protease-like protein
, pronapsin A
, napsin 1
, napsin A aspartic peptidase L homeolog