P7338
Protease from HIV-1
recombinant, expressed in E. coli, buffered aqueous solution, suitable for cleaving HIV substrate III (Yields 2 peaks which elute before the substrate peak when analyzed by reversed phase HPLC.)
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About This Item
recombinant
expressed in E. coli
form
buffered aqueous solution
suitability
suitable for cleaving HIV substrate III (Yields 2 peaks which elute before the substrate peak when analyzed by reversed phase HPLC.)
shipped in
dry ice
storage temp.
−70°C
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Unit Definition
One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent), unless otherwise indicated.
Physical form
Solution in dilute HCl, pH 1.6.
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J M Louis et al.
Nature structural biology, 6(9), 868-875 (1999-08-31)
In the Gag-Pol polyprotein of HIV-1, the 99-amino acid protease is flanked at its N-terminus by a transframe region (TFR) composed of the transframe octapeptide (TFP) and 48 amino acids of the p6pol, separated by a protease cleavage site. The
A Leuthardt et al.
FEBS letters, 326(1-3), 275-280 (1993-07-12)
The gene coding for the HIV-1 protease was cloned in an Escherichia coli expression vector adding three-histidine codons to the amino and carboxy terminus of the protease sequence. Expression of the protease from this construct led to the accumulation of
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