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AB316063

Recombinant Human Envelop VLP Control protein

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Recombinant Human Envelop VLP Control protein is a HIV-1 M:B_MN Fragment protein, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level.

View Alternative Names

Gag polyprotein, Pr55Gag, gag

Key facts

Purity

>95% HPLC

Endotoxin level

< 1 EU/µg

Expression system

HEK 293 cells

Tags

Tag free

Biologically active

No

Accession

P05888

Animal free

No

Carrier free

Yes

Species

HIV-1 M:B_MN

Storage buffer

Constituents: PBS

storage-buffer

Product details

Recombinant Human Envelop VLP Control is expressed from HEK293. Human Envelop VLP Control is formed by self-assembly of envelop/capsid proteins from viruses, which is pure viral protein particle structure without the displayed proteins. Human Envelop VLP Control can be used as isoytype control for VLPs displaying membrane proteins in various applications.

VLPs are formed by spontaneous interaction between one or more viral structural capsid proteins to form the final structure. VLPs are structurally and visually similar to live viruses but lack either a complete virus genome or lack the entire virus genome. The envelop VLP control is pure viral protein particle structure without the displayed proteins, which can be used as control for the activity assay of the envelope VLP display proteins.

Sequence info

[{"linker":null,"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P05888","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

The Gag polyprotein also known as the Gag protein or HIV Gag is an essential component of the HIV virus. It is expressed predominantly in host cells infected with HIV-1 and HIV-2. The Gag protein organizes into a structural protein that facilitates viral assembly and release. It typically has a mass of around 55 kDa. Gag proteins localize primarily in the cytoplasm and assemble at the plasma membrane where they form virus-like particles (VLPs).
Biological function summary

The Gag polyprotein serves an essential role in the life cycle of HIV. It forms a major structural component of the virus particle and contributes to the virion's architecture. The Gag protein mediates the packaging of the viral RNA genome into new virus particles and is important for forming the matrix capsid and nucleocapsid of the virus. It is not typically considered part of a larger complex but forms its own multimeric assembly during virus budding.

Pathways

The Gag polyprotein is integral to the viral replication pathway and the process of viral budding from host cells. It interacts with host cell membranes and orchestrates the encapsulation of viral components into new virions. Critical pathways like the proteolytic maturation of viral proteins and assembly incorporate Gag proteins involving other viral proteins such as the Pol protein which helps in the processing and maturation of the viral structure.

The Gag protein is directly related to HIV/AIDS. The presence and functionality of the Gag protein enable the virus to replicate within the host contributing to the progression of the disease. The interaction between the Gag protein and other viral components like the Env protein is also essential for the viral entry into new cells which exacerbates the infection process. Efforts to inhibit the Gag polyprotein function are important in controlling HIV proliferation and managing HIV-related disorders.

Specifications

Form

Liquid

General info

Function

Gag polyprotein. Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi).. Matrix protein p17. Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).. Capsid protein p24. Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid.. Nucleocapsid protein p7. Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.. p6-gag. Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1.

Sequence similarities

Belongs to the primate lentivirus group gag polyprotein family.

Post-translational modifications

Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins.. Matrix protein p17. Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association.. Capsid protein p24. Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating.. Nucleocapsid protein p7. Methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription.

Product protocols

Target data

Gag polyprotein. Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi).. Matrix protein p17. Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).. Capsid protein p24. Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid.. Nucleocapsid protein p7. Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly.. p6-gag. Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1.
See full target information gag

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