H1757
Hemocyanin from Limulus polyphemus hemolymph
Type VIII, lyophilized powder, Protein ≥85 % by biuret
biological source
Limulus polyphemus hemolymph
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
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.
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.
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).
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
动植物来源生物产品
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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)
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
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R L Dalman et al.
Acta chirurgica Scandinavica. Supplementum, 555, 25-35 (1990-01-01)
Bernard R Lauwerys et al.
Arthritis and rheumatism, 65(2), 447-456 (2012-12-04)
We developed interferon-α-kinoid (IFN-K), a drug composed of inactivated IFNα coupled to a carrier protein, keyhole limpet hemocyanin. In human IFNα-transgenic mice, IFN-K induces polyclonal antibodies that neutralize all 13 subtypes of human IFNα. We also previously demonstrated that IFN-K
Victoria A Valdenegro-Vega et al.
Veterinary immunology and immunopathology, 151(1-2), 113-123 (2012-12-05)
This study aimed to assess systemic and mucosal immune responses of Atlantic salmon (Salmo salar) exposed to two protein-hapten antigens - dinitrophenol (DNP) and fluorescein isothiocyanate (FITC) each conjugated with keyhole limpet haemocyanin (KLH) - administered using different delivery strategies.
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