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Publication : Molecular cloning and characterization of mouse ficolin-A.

First Author  Fujimori Y Year  1998
Journal  Biochem Biophys Res Commun Volume  244
Issue  3 Pages  796-800
PubMed ID  9535745 Mgi Jnum  J:46796
Mgi Id  MGI:1202090 Doi  10.1006/bbrc.1998.8344
Citation  Fujimori Y, et al. (1998) Molecular cloning and characterization of mouse ficolin-A. Biochem Biophys Res Commun 244(3):796-800
abstractText  A novel ficolin-related gene was isolated from the mouse liver lambda ZAPII cDNA library. The protein encoded by this gene consists of both collagen- and fibrinogen-like domains, which are common features of the ficolin family, and was named mouse ficolin-A. The amino acid sequence of mouse ficolin-A is 60.2, 59.8, 59.8, and 59.6% identical to those of porcine ficolin-alpha, -beta, human ficolin-1, and EBP-37/P35, respectively. Northern blot analysis showed that mRNA of mouse ficolin- A is highly expressed in liver and spleen. Immunoblot analysis using an anti-mouse ficolin-A antiserum showed that mouse ficolin-A is a plasma protein with binding activity to elastin and GlcNAc.
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