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H1757

Sigma-Aldrich

Hemocyanin from Limulus polyphemus hemolymph

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

CAS Number:
MDL number:
NACRES:
NA.61

biological source

Limulus polyphemus hemolymph

Quality Level

type

Type VIII

assay

≥85% protein basis (biuret)

form

lyophilized powder

composition

Protein, ≥85% biuret

copper content

0.10-0.20% (ICP-atomic emission)

UniProt accession no.

storage temp.

2-8°C

Gene Information

Limulus polyphemus ... LOC(106468801)

General description

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

Application

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 study 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.

Packaging

100, 500 mg in poly bottle
1 g 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).

Certificate of Analysis

Certificate of Origin

Limulus polyphemus hemocyanin: 10 A cryo-EM structure, sequence analysis, molecular modelling and rigid-body fitting reveal the interfaces between the eight hexamers
Martin AG, et al.
Journal of Molecular Biology, 366(4), 1332-1350 (2007)
Will interventional angiology replace vascular surgery?
R L Dalman et al.
Acta chirurgica Scandinavica. Supplementum, 555, 25-35 (1990-01-01)
S J O'Leary et al.
Hearing research, 298, 27-35 (2013-02-12)
This study reviews the cochlear histology from four hearing preservation cochlear implantation experiments conducted on 73 guinea pigs from our institution, and relates histopathological findings to residual hearing. All guinea pigs had normal hearing prior to surgery and underwent cochlear...
Brian P Enright et al.
Birth defects research. Part B, Developmental and reproductive toxicology, 95(6), 431-443 (2012-12-06)
ABT-874 is an anti-IL-12/23 monoclonal antibody that binds to the p40 subunit of human IL-12 and IL-23. As part of its preclinical safety assessment, studies were conducted to assess its potential effects on pre- and postnatal development in cynomolgus monkeys....
Richard J Ansell et al.
The Analyst, 134(2), 226-229 (2009-01-29)
Native, uncoloured, proteins can be focused in a column containing a fluorescent packing material, using hydrodynamic flow and a counteracting non-linear electric field, and imaged along the length of the channel by fluorescence quenching.

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