Rabbit anti-Human CDS2 Polyclonal Antibody

Uniprot Id

O95674

Target Species

Human

Target Name

CDS2

Target Full Name

Phosphatidate cytidylyltransferase 2

Target Function

Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol. Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid. Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis.

Target Subcellular Location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Target Protein Families

CDS family

Target Tissue Specificity

Widely expressed. Expressed in heart, brain and retina, and to a lesser extent in placenta, lung, liver, skeletal muscle, kidney and pancreas.

Target Synonyms

CDS2; Phosphatidate cytidylyltransferase 2; CDP-DAG synthase 2; CDP-DG synthase 2; CDP-diacylglycerol synthase 2; CDS 2; CDP-diglyceride pyrophosphorylase 2; CDP-diglyceride synthase 2; CTP:phosphatidate cytidylyltransferase 2

Target Background

Breakdown products of phosphoinositides are ubiquitous second messengers that function downstream of many G protein-coupled receptors and tyrosine kinases regulating cell growth, calcium metabolism, and protein kinase C activity. This gene encodes an enzyme which regulates the amount of phosphatidylinositol available for signaling by catalyzing the conversion of phosphatidic acid to CDP-diacylglycerol. This enzyme is an integral membrane protein localized to two subcellular domains, the matrix side of the inner mitochondrial membrane where it is thought to be involved in the synthesis of phosphatidylglycerol and cardiolipin and the cytoplasmic side of the endoplasmic reticulum where it functions in phosphatidylinositol biosynthesis. Two genes encoding this enzyme have been identified in humans, one mapping to human chromosome 4q21 and a second to 20p13.