Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. Homo-didecamer, with two decamers assembled face-to-face at their open ends. This didecamer form a stable 25 nM cylinder wall. Hemolymph. The protein is composed of 8 globular functional units (a->h), forming a 'pearl chain'. Each unit is separated from the next by a linker. Since the lengths but not the exact positions are known, lengths are indicated here in free text. Linker lengths in amino acids are: 20 (a->b), 13 (b->c), 19 (c->d), 16 (d->e), 14 (e->f), 17 (f->g), and 17 (g->h). Probably N-glycosylated (Probable). Asn-1280 and Asn-2484 are buried deeply in the protein which make them inaccessible for sugar attachment (Probable). Asn-3278 N-glycan is likely to represent a diantennate carbohydrate tree (Probable). The didecamer is almost evenly tagged by a total of 120 sugar trees (Probable). Potent immunogen used classically as a carrier protein for haptens and more recently in human vaccines and for immunotherapy of bladder cancer. Belongs to the tyrosinase family. Hemocyanin subfamily.