Rat CD38 (His Tag) recombinant protein
The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Cluster of differentiation 38 (CD38), also known as ADP-ribosyl cyclase, is a glycoprotein found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B and natural killer cells. It shares several characteristics with ADP-ribosyl cyclase 2 CD157. CD38 is a multifunctional ectoenzyme that catalyzes the synthesis and hydrolysis of cyclic ADP-ribose (cADPR) from NAD+ to ADP-ribose. It also functions in cell adhesion, signal transduction and calcium signaling. CD38 has been used as a prognostic marker in leukemia. It can also be used to identify plasma cells.
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
Protein short names
T10; CD38-RS1; CD38; ADPRC1
A DNA sequence encoding the rat CD38 (Q64244) (Trp45-Val303) was expressed, fused with a polyhistidine tag at the C-terminus.
The recombinant rat CD38 comprises 270 amino acids and predicts a molecular mass of 31.2 kDa. The apparent molecular mass of the recombinant protein is approximately 42 kDa in SDS-PAGE under reducing conditions due to glycosylation.
> 95 % as determined by SDS-PAGE
Rat CD38 Protein (His Tag) SDS-PAGE
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