Human Calcium Activated Nucleotidase 1/CANT1 Antibody

CANT1 (soluble Calcium-Activated NucleoTidase 1; also SCAN-1, Apyrase homolog and NF kappaB-activating protein 107) is a 45-48 kDa glycoprotein member of the apyrase (ADP/ATP hydrolysing) family of molecules. It is an ER and Golgi-embedded protein that hydrolyzes UDP in a calcium-dependent manner, and appears to be involved in the regulation of protein glycosylation and folding. It is also reported that CANT1 is essential for cell proliferation. CANT1 is not ubiquitous, but is found in multiple cell types, including prostatic epithelium, fibroblasts, lymphocytes and chondrocytes. Human CANT1 is a 401 amino acid (aa) type II transmembrane glycoprotein. It contains a 44 aa N-terminal cytoplasmic region that possesses an ER retention motif (aa 38-42), and a 339 aa luminal domain (aa 63-401). CANT1 is reported to form membrane-bound disulfide-linked homodimers, and potentially form non-covalent homodimers in a soluble (circulating) state. The soluble form is 35‑40 kDa in size, and presumably cleaved near the transmembrane segment. However, multiple splice forms are possible, and may account for the lower MWs. Two splice forms impact the extracellular region, one which contains a four aa substitution for aa 219-401, and a second that possesses a 26 aa substitution for aa 220‑401. Two additional splice forms utilize alternative start sites at Met 31 and Met165. Over aa 80-401, human CANT1 shares 89% aa sequence identity with mouse CANT1.