Microbiology and Virology

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  1. Recombinant Human SARS-CoV-2 Spike Protein RBD
    • Species: SARS-CoV-2
    • Bioactivity: 1. Immobilized Recombinant Human SARS-CoV-2 Spike Protein RBD (rp155929) at 5.0 μg/mL can bind Recombinant Human ACE-2 Protein (rp176242) with the EC50 of 75.79 ng/mL. 2. Immobilized Recombinant Human SARS-CoV-2 Spike Protein RBD (rp155929) at 1.0 μg/mL can bind Regdanvimab (anti-Spike RBD) (Ab182925) with the EC50 of 12.65 ng/mL. 3. Immobilized Recombinant Human SARS-CoV-2 Spike Protein RBD (rp155929) at 1.0 μg/mL can bind Imdevimab (anti-Spike RBD) (Ab182897) with the EC50 of 7.82 ng/mL. 4. Immobilized Recombinant Human SARS-CoV-2 Spike Protein RBD (rp155929) at 1.0 μg/mL can bind Etesevimab (anti-Spike RBD) (Ab182932) with the EC50 of 23.96 ng/mL. 5. Immobilized Recombinant Human SARS-CoV-2 Spike Protein RBD (rp155929) at 1.0 μg/mL can bind Sotrovimab (anti-Spike RBD) (Ab182938) with the EC50 of 41.33 ng/mL. 6. Immobilized Recombinant Human SARS-CoV-2 Spike Protein RBD (rp155929) at 1.0 μg/mL can bind Casirivimab (anti-Spike RBD) (Ab182896) with the EC50 of 10.50 ng/mL.
    Synonyms: SARS-CoV-2 RBD Protein | SARS-CoV-2 Spike RBD Protein | SARS-CoV-2 S Protein RBD
  2. Recombinant EN-TEV Protease Protein
    • Species: Tobacco etch virus(TEV)
    • Bioactivity: Measured by its ability to cleave a fusion protein containing the recognition sequence Glu-Asn-Leu-Tyr-Phe-Gln-Gly/Ser , with the cleavage point after Gln. One unit of TEV protease cleaves > 85% of 3 μg of control substrate in 1 hour at pH 8.0 at 30°C.It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant Viral TEV Protease, reaction time, or incubation temperature.Complete digestion of 50µg of fusion KGF-MBP tag protein using 1µg TEV enzyme (in 1/50 ratio) in either 1 hours at 30 °C or overnight at 4 °C. The "standard" reaction buffer for TEV protease is 50 mM Tris-HCl (pH 8.0), 0.5 mM EDTA and 1mM DTT.
    Synonyms: NIa | P1 Protease | TEV Protease | Tobacco Etch Virus Protease
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