[
International Worm Meeting,
2003]
SCP2 which is also termed non-specific lipid transfer protein has been thought to be involved in the transport of various lipids. In mammalian hepatic peroxisomes this protein is expressed either as a small or a large fusion termed sterol carrier protein x (SCPx) that carries at its C-terminal the complete sequence of SCP2. Proteins similar to SCPx were found in C. elegans; P-44, which is similar to the N-terminal part of SCPx and ORFs coding for the homologues of SCP2/SCPx, namely ZK892.2, M03A8.1 and C17G10.8. This is the first time in a single organism where SCPx homologue (P-44) and SCPx homologue (ZK892.2) are coded independently. Their predicted sequences suggest they are peroxisomal proteins. To be able to study the function of SCP2 independently from any fusion form, ZK892.2 protein was purified and raised mouse antisera against it. This protein was proved to reside in the matrix of peroxisomes.