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Updated: Aug 7, 2026

Transcriptomic Analysis of Human Retinal Surgical Specimens Using jouRNAl
Published on: August 14, 2013
Cloning and characterization of a novel, human cellular retinaldehyde-binding protein CRALBP-like (CRALBPL) gene
Ya-Hui Kong1, Guang-Ming Ye, Kai Qu
1State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, People's Republic of China.
Abstract:
Cellular retinaldehyde-binding protein (CRALBP) plays a role in the vertebrate visual process as a substrate-routing protein. It belongs to a widespread lipid-binding SEC14-like protein family. All the members of the family have the lipid-binding domain called CRAL-TRIO. Here we have isolated a new human CRAL-TRIO domain containing a CRALBP-like (CRALBPL) gene from the cDNA library of human adult brain. The CRALBPL gene consisted of 1,694 bp and had an ORF encoding putatively 354 amino acids with a CRAL-TRIO domain from 118 to 279 aa. The expression pattern in 18 human tissues indicated that CRALBPL gene was mainly expressed in brain. The alignment of CRAL-TRIO domain showed that CRALBPL had 45% identity with human CRALBP. Subcellular location revealed that CRALBPL protein was located in the cytoplasm of HeLa cells. Western blotting indicated that the CRALBPL had a molecular weight of about 40 kDa.
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