Anti-CFC1 (full length) polyclonal antibody

Ail vertebrates display a characteristic asymmetry of internal organs with the cardiac apex, stomach and spleen towards the left, and the liver and gall bladder on the right(1-3). Left-right (L-R) axis abnormalities or laterality defects are common in humans (1 in 8,500 live births). Several genes (such as Nodal, Ebaf and Pitx2) have been implicated in L-R organ positioning in model organisms(2-4), In humans, relatively few genes have been associated with a small percentage of human situs defects. These include ZIC3 (ref. 5), LEFTB (formerly LEFTY2; ref. 6) and ACVR2B (encoding activin receptor IIB; ref, 7). The EGF-CFC genes(8), mouse Cfc1 (encoding the Cryptic protein; ref. 9) and zebrafish one-eyed pinhead (oep; refs 10,11) are essential for the establishment of the L-R axis(12,13). EGF-CFC proteins act as co-factors for Nodal-related signals(11), which have also been implicated in L-R axis development(4). Here we identify loss-of-function mutations in human CFC1 (encoding the CRYPTIC protein) in patients with heterotaxic phenotypes (randomized organ positioning). The mutant proteins have aberrant cellular localization in transfected cells and are functionally defective in a zebrafish oepmutant rescue assay. Our findings indicate that the essential role of EGF-CFC genes and Nodal signalling in left-right axis formation is conserved from fish to humans. Moreover, our results support a role for environmental and/or genetic modifiers in determining the ultimate phenotype in humans.

A bacterial strain CFC1, which produced an extracellular cycloinulooligosaccharide fructanotransferase (CFTase), was isolated from soil. The isolated strain was identified as a strain of Bacillus sp. The synthesis of CFTase by the bacterium was found to be induced by inulin which was added to the culture medium as a carbon source. The highest activity of CFTase was observed at pH 7.5 and 37 degrees C in the medium containing 4% inulin and 0.5% peptone as a carbon source and a nitrogen source, respectively. Under the optimal conditions, the enzyme activity in the culture supernatant reached the highest level of 85 munits/ml after 96 h cultivation.