H8283
Hemocyanin from Megathura crenulata (keyhole limpet)
PBS solution
Synonym(s):
KLH, Keyhole limpet hemocyanin
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About This Item
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biological source
Megathura crenulata
Quality Level
form
PBS solution
concentration
3.0-7.0 mg/mL protein (A280)
copper content
0.10-0.30% (based on protein)
technique(s)
ELISA: suitable
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.
Hemocyanin was used to study if antipeptide antibodies specifically recognize the l1 protein of the human papilloma virus of type 31. It was also used to study the acid-induced unfolding of didecameric keyhole limpet hemocyanin.
Hemocyanin was used to study if antipeptide antibodies specifically recognize the l1 protein of the human papilloma virus of type 31. It was also used to study the acid-induced unfolding of didecameric keyhole limpet hemocyanin.
Physical form
Solution in PBS, pH 7.2, containing 1mM CaCl2 and 0.5 mM MgCl2 with 15 mM sodium azide as preservative
Preparation Note
Chromatographically purified.
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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S M Andreev et al.
Bioorganicheskaia khimiia, 38(6), 667-675 (2013-04-04)
Antibodies that specifically recognize the capsid protein (L1) of human papillomavirus (HPV) are an important tool necessary for designing vaccines against HPV infection. In this work, we have predicted and synthesized peptide fragments mimicking B cell epitopes of L1 HPV
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