Accéder au contenu
Merck
Toutes les photos(1)

Key Documents

SAB4700771

Sigma-Aldrich

Monoclonal Anti-HIV protease antibody produced in mouse

clone 1696, purified immunoglobulin, buffered aqueous solution

Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme


About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

1696, monoclonal

Forme

buffered aqueous solution

Espèces réactives

human immunodeficiency virus

Concentration

1 mg/mL

Technique(s)

FUNC: suitable
immunoblotting: suitable
indirect ELISA: suitable

Isotype

IgG1

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

Description générale

Human immunodeficiency virus (HIV) protease expressed in the 5′ end of pol gene is part of gag-pol polyprotein. HIV protease has 99 amino acids. The monomers of the protein are inactive; homodimers of the protein are enzymatically active. The antibody 1696 recognizes free N-terminus of mature HIV protease (HIV-1 and HIV-2), an enzyme that hydrolyzes polyproteins of HIV viruses into functional proteins. The antibody 1696 does not react with the precursor.

Immunogène

Bacterially expressed full-length HIV-1 protease

Actions biochimiques/physiologiques

HIV protease is an aspartyl protease which is essential for cleavage of viral progenitor polyprotein. Protease activity is critically essential for the life cycle of the virus. HIV protease cleaves gag protein into three larger fragments p24, p17 and p7, which are the core structural protein and essential for RNA packaging. Protease also cleaves gag-pol fusion protein of the virion. The favourable cleavage site of HIV protease is N-terminal to proline, like phenylalanine-proline, tyrosine-proline, which is uncommon for mammalian proteases. The cleavage happens after the budding of the virion from the infected cell surface, transform into a mature infectious virus. Lack of protease results in immature and non-infectious viral particles. Inhibitors targeted to HIV protease is the recent advancement in the treatment of HIV infection.

Caractéristiques et avantages

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Forme physique

Solution in phosphate buffered saline, pH 7.4, with 15 mM sodium azide.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Vous ne trouvez pas le bon produit ?  

Essayez notre Outil de sélection de produits.

Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme
Kim EE, et al.
Journal of the American Chemical Society, 117(3), 1181-1182 (1995)
HIV protease: a novel chemotherapeutic target for AIDS
Huff JR
Journal of Medicinal Chemistry, 34(8), 2305-2314 (1991)
The mechanism of insulin resistance caused by HIV protease inhibitor therapy
Murata M, et al.
The Journal of Biological Chemistry, 275(27), 20251-20254 (2000)
HIV-protease inhibitors
Flexner C
The New England Journal of Medicine, 338(18), 1281-1293 (1998)

Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..

Contacter notre Service technique