Keyhole limpet hemocyanin (KLH) is a copper-containing extracellular respiratory protein found in the marine gastropod Megathura crenulata. This protein exists in two isoforms- KLH1 and KLH2. In few pulmonate gastropods this protein is synthesized by connective tissue "pore cells", where KLH resides as cylindrical macromolecules and even forms intracellular crystalline arrays in the endoplasmic reticulum cisternae. It belongs to the hemocyanin protein family which are found in the hemolymph of many molluscs and arthropods.
Synonyms: Megathura crenulata hemocyanin; keyhole limpett hemocyanin
Purity: >=95%
Storage: 2-8C
Biochem Physiol Actions: Keyhole limpet hemocyanin (KLH) is a hemocyanin, and its main function is oxygen uptake, transport and release. Hemocyanins exist as oligomers with one or more subunit types. The protein subunit contains the FU (functional unit), which contains a binuclear copper binding site that is capable of binding oxygen. It has potent immunostimulatory properties in animals and human. This protein finds major clinical use in the treatment of bladder carcinoma. It finds use as a carrier for carcinoma ganglioside and mucin-like epitopes, and has potential for the treatment of various carcinomas, particularly epithelially derived adenocarcinoma.