CD38 Extracellular Domain (human, recombinant)

CD38, also known as ADP-ribosyl cyclase 1, is a single-chain type II transmembrane glycoprotein with enzymatic activity and cell surface receptor functions that has roles in calcium signaling and immunomodulation. It is composed of a C-terminal catalytic domain, which can be oriented towards the extracellular or intracellular environment, a transmembrane segment, and a short N-terminal cytoplasmic tail, which interacts with the tyrosine kinase Lck. CD38 expression is induced by cytokine, interferon, or endotoxin stimulation in a variety of immune cells, including T cells, B cells, granulocytes, and natural killer (NK) cells, as well as malignant plasma cells, and predominantly localizes to lipid rafts. It is also found in the nucleus and mitochondrial membrane, as well as in the cytoplasm. CD38 regulates calcium signaling by catalyzing the formation of the intracellular calcium mobilizing messengers cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate (NAADP). It is a receptor for CD31, an adhesion molecule expressed by endothelial cells, and associates with a variety of signaling complexes, such as CD3/T cell receptor and CD19/CD21/B cell receptor complexes. CD38 protein expression is increased on plasma cells isolated from patients with multiple myeloma. Cayman's CD38 Extracellular Domain (human, recombinant) protein can be used for enzyme activity and binding assay applications. This protein is a disulfide-linked homodimer. The reduced monomer, composed of CD38 (amino acids 43-300) fused to human IgG1 Fc at its C-terminus, consists of 496 amino acids and has a calculated molecular weight of 56. kDa. As a result of glycosylation, the monomer migrates at approximately 64. kDa by SDS-PAGE under reducing conditions.