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AB109969

Recombinant HIV1 Gag protein

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(1 Publication)

Recombinant HIV1 Gag protein is a Full Length protein, in the 1 to 508 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, WB.

View Alternative Names

Capsid, Gag polyprotein, Matrix, Nucleocapsid, Pr55(Gag), Pr55Gag, p6

1 Images
SDS-PAGE - Recombinant HIV1 Gag protein (AB109969)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant HIV1 Gag protein (AB109969)

ab109969 is >90% pure estimated by SDS-PAGE.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

WB, SDS-PAGE

applications

Biologically active

No

Animal free

No

Carrier free

No

Reconstitution

Reconstitute in PBS

Storage buffer

Constituents: 1% Glycerol (glycerin, glycerine)

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"56.5 kDa","actualMolecularWeight":null,"aminoAcidEnd":508,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":null,"tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The HIV-1 Gag protein often simply referred to as Gag plays a central role in the life cycle of the HIV virus. Also known as the Group-specific antigen this protein has a molecular mass of approximately 55 kDa. The Gag protein is expressed in the cytoplasm of HIV-infected cells where it is essential for virus particle assembly and release. It facilitates the formation of virus-like particles by self-assembling into a spherical capsid. Moreover various Gag proteins are produced through proteolytic processing and these are vital in the maturation of the viral particle.
Biological function summary

The function of Gag protein involves the orchestration of viral particle assembly at the plasma membrane of the host cell. The Gag proteins are essential because they interact with viral RNA and other viral proteins to form immature viral particles. It is a multi-domain protein that includes the matrix (MA) capsid (CA) nucleocapsid (NC) and p6 domains. These domains participate collectively in the encapsidation of genomic RNA and recruitment of host cell factors necessary for virion morphogenesis. Therefore Gag is indispensable in the viral replication process though it does not function as part of a larger multiprotein complex outside the viral context.

Pathways

Gag protein is an important player in the retroviral replication pathway. It facilitates the budding of new viral particles from the host cell an essential step in the viral life cycle. It interacts with host proteins including TSG101 and ALIX of the host cell's ESCRT pathway which is critical for the proper scission of budding particles from the host cell membrane. Additionally Gag's interaction with the cyclophilin A protein suggests a corresponding regulatory mechanism within the host’s cellular environment to ensure efficient virion formation.

Gag protein is intimately associated with HIV/AIDS a devastating condition resulting from HIV infection. Gag protein plays a primary role in the assembly and maturation of the virus rendering it a target for therapeutic intervention. Inhibition of Gag functions can potentially block virus production. During disease progression the protein interacts with envelope proteins such as gp120 and gp41 which are important for viral entry into host cells. This facilitates the spread of infection and progression to AIDS making Gag an important target in the search for new therapeutic strategies against HIV.

Specifications

Form

Lyophilized

General info

Product protocols

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Cell reports 31:107520 PubMed32320662

2020

Pan-retroviral Nucleocapsid-Mediated Phase Separation Regulates Genomic RNA Positioning and Trafficking.

Applications

Unspecified application

Species

Unspecified reactive species

Anne Monette,Meijuan Niu,Lois Chen,Shringar Rao,Robert James Gorelick,Andrew John Mouland
View all publications

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