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H1757 Sigma-Aldrich

Hemocyanin from Limulus polyphemus hemolymph

Type VIII, lyophilized powder, Protein ≥85 % by biuret



Related Categories Application Index, Biochemicals and Reagents, Enzymes, Inhibitors, and Substrates, Serum Proteins, Serum Proteins and Related Enzymes More...
type   Type VIII
form   lyophilized powder
composition   Protein, ≥85% biuret
copper content   0.10-0.20% (ICP-atomic emission)
storage temp.   2-8°C


General description

Hemocyanin in the hemolymph of Limulus polyphemus L (horseshoe crab) is a high-molecular-weight copper protein which binds oxygen passively.

The structure of hemocyanin from Limulus polyphemus comprises of a domain I at N-terminal with α-helical regions, domain II with active site copper residue and four α helical bundle and domain III at C-terminus with an anti-parallel β-barrel structure. Hemocyanin corresponds to a molecular weight of 72 kDa and has phenoloxidase functionality.


Hemocyanin from Limulus polyphemus hemolymph has been used:
• in electrophoretic field gradient focusing as a reference standard for optimizing fluorescence quenching for noncolored proteins
• as standard protein for pH based crystallization screening experiments
• in peptide conjugation studies

Hemocyanins were used in a stud to test LIM kinase 1 accumulation in presynaptic terminals during synapse maturation. It was also used in the topographic analysis of human follicle-stimulating hormone-β using anti-peptide antisera.


1 g in poly bottle

100, 500 mg in poly bottle

Biochem/physiol Actions

The largest hemocyanin molecules consisting of 48 (8 × 6) subunits are present in horseshoe crabs (Limulus polyphemus) have up to eight distinct subunits type (6 × subunit type I, 8 × II, 2 × IIA, 8 × IIIA, 8 × IIIB, 8 × IV, 4 × V, 4 × VI).

Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 


Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Protocols & Articles
Peer-Reviewed Papers


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