Cayman Chemical Item Number 10340
Recombinant N-terminal His-tagged GRFT, purified from E. coli
Griffithsin (GRFT), is a lectin isolated from Griffithsia sp. with anti-HIV activity at subnanomolar concentrations.1 GRFT activity is glycosylation-dependent and acts by binding to glycoproteins gp41, gp120, and gp160 on the viral envelope, blocking the virus from binding to CD4 receptor-expressing cells in the host. It also prevents cell fusion between infected and uninfected cells, further inhibiting the spread of HIV in the body. GRFT functions as a homodimer, with each monomer containing three carbohydrate binding sites.1,2 GRFT unique anti-viral activity is of interest for use in microbicide production to stop transmission of HIV through sexual contact. It has also been shown to have inhibitory effects with SARS-related coronavirus; where GRFT binding to the SARS-CoV S protein can prevent viral entry and reduce viral load in succeeding rounds of infection.3
Mori, T., O'Keefe, B.R., Sowder, R.C., et al. Isolation and characterization of griffithsin, a novel HIV-inactivating protein, from the red alga Griffithsia sp.. J Biol Chem 280(10) (2005).
Ziólkowska, N.E., O'Keefe, B.R., Mori, T., et al. Domain-swapped structure of the potent antiviral protein griffithsin and its mode of carbohydrate binding. Structure 14 (2006).
O'Keefe, B.R., Giomarelli, B., Barnard, D.L., et al. Broad spectrum in vitro activity and in vivo efficacy of the antiviral protein griffithsin against emerging viruses of the family Coronaviridae. J Virol (2009).
||50 mM sodium phosphate pH 7.2, containing100 mM sodium chloride, 2.5 mM DTT, and 20% glycerol
in continental US; may vary elsewhere
InCHI Key generation software
Pricing updated 2015-03-02.
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