H1757
Hemocyanin from Limulus polyphemus hemolymph
Type VIII, lyophilized powder, Protein ≥85 % by biuret
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About This Item
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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.[1]
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.[2] Hemocyanin corresponds to a molecular weight of 72 kDa and has phenoloxidase functionality.[3]
Application
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).[9]
Storage Class
13 - Non Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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