H7017
Hemocyanin from Megathura crenulata (keyhole limpet)
Synonym(s):
KLH, Keyhole limpet hemocyanin
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About This Item
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biological source
Megathura crenulata
Quality Level
form
powder
packaging
vial of KLH (KLH is present by weight at approximately 1 part KLH to 5 parts total solid.)
technique(s)
ELISA: suitable
solubility
H2O: soluble
storage temp.
2-8°C
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General description
Gastropod hemocyanins are massive glycoproteins (4 to 8 MDa) designed by an intricate arrangement of 10 subunits that are self-assembled into hollow cylinders 35 nm in diameter.
Hemocyanin is a high molecular weight copper containing glycoprotein. It reversibly binds oxygen and forms the extra-cellular respiratory protein of mollusks. Keyhole limpet hemocyanin (KLH) is filtered from the hemolymph of Megathura crenulata, also called the giant keyhole limpet. It is native to the southern California coast and Mexico.
Application
Keyhole limpet hemocyanin (KLH) is a strong and well known immune-stimulant in both experimental animals and humans. It has been used as a hapten carrier protein to enhance antigen-specific T cell priming and is known to stimulate a CD4+ T-cell response. Hemocyanins stimulate Th1 reactions without known side effects, which make them ideal for long-term continuous treatment of cancer.
Physical form
Lyophilized with stabilizing buffer
Reconstitution
Reconstitute with deionized water to a KLH concentration of 10 mg/mL, to yield an opalescent solution in 31 mM sodium phosphate buffer, pH 7.4, containing 0.46 M NaCl, 2% PVP and 41 mM sucrose.
Reconstituted protein solution may be stored up to 2 months at −20 °C.
Reconstituted protein solution may be stored up to 2 months at −20 °C.
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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J T Brisbin et al.
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The Dictyostelium discoideum homolog of mammalian cyclin dependent kinase 5 (Cdk5) has previously been shown to be required for optimal growth and differentiation in this model organism, however, the subcellular localization of the protein has not previously been studied. In
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