SDPR encodes a calcium-independent phospholipid-binding protein whose expression increases in serum-starved cells. This protein has also been shown to be a substrate for protein kinase C (PKC) phosphorylation.
The SDPR cDNA encodes a deduced 425-amino acid peptide with a calculated molecular mass of 47.2 kD. The human and mouse proteins share 84% sequence identity; both contain a leucine zipper-like domain with 7 repeats and 2 putative protein kinase C phosphorylation sites. Northern blot analysis of various human tissues showed nearly ubiquitous expression of a 3.1-kb transcript, which was always coexpressed with a shorter transcript. Highest expression was detected in heart and lung.SDPR is able to bind PS liposomes in a calcium-independent manner.
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