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Manufactured by BioVendor

HIV-1 Protease E.coli

  • Regulatory status:RUO
  • Type:Active protein
  • Source:E. coli
  • Species:Human Immunodeficiency Virus 1
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Cat. No. Size Price


RH1P0001 0.1 mg
PubMed Product Details
Technical Data

Type

Active protein

Description

Total 99 AA. MW: 10.8 kDa (monomer), protein active as dimer

Amino Acid Sequence

PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMNLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNF

Source

E. coli

Purity

Purity as determined by densitometric image analysis: >95%

SDS-PAGE Gel

14% SDS-PAGE separation of Human HIV-1 Protease
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and heated sample, 2.5 μg/lane

Formulation

20 mM Tris, 20 mM MES, 200 mM NaCl, 1mM EDTA, 10% (v/v) glycerol, 0,05% 2-mercaptoethanol, pH 6.5 – filtered (0.4 μm), frozen

Reconstitution

Defrost at ambient temperature.

Applications

Kinetic studies, Inhibitor screening, Crystallography

Shipping

On ice. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store protein at –80°C. Protein remains stable until the expiry date when stored at –80°C. Avoid repeated freezing/thawing cycles.

Quality Control Test

SDS PAGE to determine purity of the protein.
Active site titration by tightly binding inhibitor.

Note

Km = 15.1 μM Kcat = 30 s-1 Kcat /Km = 1981 mM-1 s-1 with peptide substrate KARVF(NO2 )VRKA (F(NO2 ) … p-nitrophenylalanine)

Summary

Research topic

Others

Summary

Retroviral protease from HIV-1 virus is an enzyme important in the life cycle of the virus. It is expressed in the infected cells as a part of Gag-Pol polyprotein from which it is autocatalytycaly released after formation of immature viral particle. The enzyme subsequently cleaves the other parts of viral polyproteins causing the maturation of the virus. In HIV-infected patients the enzyme is a subject of intensive mutagenesis and mutants resistant to applied medcines are produced as a consequence of the seletion pressure. HIV-1 protease is active as a homodimer.

Product References (5)

References

  • Ingr M, Uhlíková T, Strísovský K, Majerová E, Konvalinka J. Kinetics of thedimerization of retroviral proteases: the "fireman's grip" and dimerization.Protein Sci. 2003 Oct;12(10):2173-82. PubMed PMID: 14500875; PubMed CentralPMCID: PMC2366921. See more on PubMed
  • Lindsten K, Uhlíková T, Konvalinka J, Masucci MG, Dantuma NP. Cell-basedfluorescence assay for human immunodeficiency virus type 1 protease activity.Antimicrob Agents Chemother. 2001 Sep;45(9):2616-22. PubMed PMID: 11502538;PubMed Central PMCID: PMC90701. See more on PubMed
  • Parra A, Martin-Fonseca S, Rivas F, Reyes-Zurita FJ, Medina-O'Donnell M,Martinez A, Garcia-Granados A, Lupiañez JA, Albericio F. Semi-synthesis ofacylated triterpenes from olive-oil industry wastes for the development ofanticancer and anti-HIV agents. Eur J Med Chem. 2014 Mar 3;74:278-301. doi:10.1016/j.ejmech.2013.12.049. Epub 2014 Jan 8. PubMed PMID: 24480359. See more on PubMed
  • Sasková KG, Kozísek M, Rezácová P, Brynda J, Yashina T, Kagan RM, KonvalinkaJ. Molecular characterization of clinical isolates of human immunodeficiencyvirus resistant to the protease inhibitor darunavir. J Virol. 2009Sep;83(17):8810-8. doi: 10.1128/JVI.00451-09. Epub 2009 Jun 17. PubMed PMID:19535439; PubMed Central PMCID: PMC2738195. See more on PubMed
  • Zhang Y, Chen X, Roozbahani GM, Guan X. Graphene oxide-based biosensingplatform for rapid and sensitive detection of HIV-1 protease. Anal Bioanal Chem. 2018 Sep;410(24):6177-6185. doi: 10.1007/s00216-018-1224-2. Epub 2018 Jul 2.PubMed PMID: 29968105; PubMed Central PMCID: PMC6159923. See more on PubMed
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