Human immunodeficiency virus protease monoclonal antibody, clone 1696
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More Files
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Dot Blot
Dot Blot analysis of recombinant HIV protease. The total amount of recombinant HIV-protease spotted on the nitrocellulose membrane are indicated in HIV protease monoclonal antibody, clone 1696 (Cat # MAB3853).
Lane 1 : 0.2 ug/mL.
Lane 2 : 1.0 ug/mL.
Lane 3 : 2.0 ug/mL.
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Specification
Product Description
Mouse monoclonal antibody raised against full length recombinant human immunodeficiency virus protease.
Immunogen
Recombinant protein corresponding to full length human immunodeficiency virus protease.
Host
Mouse
Reactivity
Viruses
Specificity
This antibody recognizes free N-terminus of mature HIV protease (HIV-1 and HIV-2),an enzyme that hydrolyzes polyproteins of HIV viruses into functional proteins.This antibody does not react with the precursor.
Form
Liquid
Isotype
IgG1
Recommend Usage
Dot Blot
ELISA
Western Blot (0.5 ug/mL)
The optimal working dilution should be determined by the end user.Storage Buffer
In PBS, pH 7.4 (0.09% sodium azide)
Storage Instruction
Store at 4°C. Do not freeze.
Aliquot to avoid repeated freezing and thawing.Note
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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Applications
Western Blot
Enzyme-linked Immunoabsorbent Assay
Dot Blot
Dot Blot analysis of recombinant HIV protease. The total amount of recombinant HIV-protease spotted on the nitrocellulose membrane are indicated in HIV protease monoclonal antibody, clone 1696 (Cat # MAB3853).
Lane 1 : 0.2 ug/mL.
Lane 2 : 1.0 ug/mL.
Lane 3 : 2.0 ug/mL. -
Publication Reference
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Proteochemometric modeling of HIV protease susceptibility.
Lapins M, Eklund M, Spjuth O, Prusis P, Wikberg JE.
BMC Bioinformatics 2008 Apr; 9:181.
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Inhibition of HIV-2 protease by HIV-1 protease inhibitors in clinical use.
Brower ET, Bacha UM, Kawasaki Y, Freire E.
Chemical Biology & Drug Design 2008 Feb; 71(4):298.
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Potent inhibition of drug-resistant HIV protease variants by monoclonal antibodies.
Bartonova V, Kral V, Sieglova I, Brynda J, Fabry M, Horejsi M, Kozisek M, Saskova KG, Konvalinka J, Sedlacek J, Rezacova P.
Antiviral Research 2008 Feb; 78(3):275.
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Proteochemometric modeling of HIV protease susceptibility.
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