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AB256440

Recombinant Lassa Fever Virus GP2 glycoprotein (Fc Chimera)

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Recombinant Lassa Fever Virus GP2 glycoprotein (Fc Chimera) is a Lassa virus GA391 Fragment protein, in the 259 to 426 aa range, expressed in HEK 293 cells, with >95%, suitable for SDS-PAGE.

View Alternative Names

GP-C, GPC, Pre-glycoprotein polyprotein GP complex, Pre-GP-C

1 Images
SDS-PAGE - Recombinant Lassa Fever Virus GP2 glycoprotein (Fc Chimera) (AB256440)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Lassa Fever Virus GP2 glycoprotein (Fc Chimera) (AB256440)

SDS-PAGE analysis of ab256440 (10 μg) under reducing conditions.

Key facts

Purity

>95% SDS-PAGE

Expression system

HEK 293 cells

Tags

Fc tag C-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P17332

Animal free

No

Carrier free

No

Species

Lassa virus GA391

Storage buffer

pH: 7 - 8 Constituents: PBS

storage-buffer

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Reactivity data

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

[{"sequence":"GTFTWTLSDSEGNETPGGYCLTRWMLIEAELKCFGNTAVAKCNEKHDEEFCDMLRLFDFNKQAIRRLKTEAQMSIQLINKAVNALINDQLIMKNHLRDIMGIPYCNYSRYWYLNHTSTGKTSLPRCWLISNGSYLNETKFSDDIEQQADNMITEMLQKEYIDRQGKTP","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":426,"aminoAcidStart":259,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P17332","tags":[{"tag":"Fc","terminus":"C-Terminus"}]}]
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Properties and storage information

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

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

The Pre-glycoprotein polyprotein GP complex often referred to simply as GP or GP1 is a viral protein essential for the life cycle of certain viruses particularly the Ebola virus. This protein plays an important role in virus attachment entry and fusion with host cells. It is synthesized as a large precursor that undergoes post-translational cleavage to form smaller functional units. The GP complex is expressed on the surface of the viral envelope and is important for mediating the interaction between the virus and host cellular receptors. The molecular mass of the GP complex depends on the specific viral strain but is generally around 150-200 kDa.
Biological function summary

The GP complex is involved in the encapsulation of the viral RNA aiding the virus to evade the host immune response. It functions as part of a larger assembly known as the viral envelope complex. By promoting fusion between the viral membrane and the host's cellular membrane GP enables the viral genome to enter the host cell. This fusion facilitates the infection process and contributes to the viral pathogenicity. Its role in immune evasion involves forming a protective shield by cloaking the receptor-binding sites challenging the host's immune surveillance mechanisms.

Pathways

The GP complex influences the viral entry pathway which is an important step in the infection process for viral replication. It also interacts closely with the NPC1 receptor pathway in humans an important receptor for Ebola virus entry. The interaction with NPC1 a protein that traffics cholesterol in cells is essential for the virus's entry into the host cell endosome where the viral and endosomal membranes fuse. Another protein related through this pathway is the cathepsin family which processes the GP complex to enable effective fusion.

The GP complex is significantly associated with Ebola virus disease a severe and often fatal illness. The protein's ability to mediate host cell entry and immune evasion complicates the course of the disease contributing to high virulence. Another disorder linked to the GP complex is hemorrhagic fever seen in Ebola-infected patients. This association occurs through interactions with host cytokines and integrins which the virus manipulates to compromise the host's immune response. Understanding these connections helps researchers target GP in developing therapeutic strategies and vaccines.
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Specifications

Form

Liquid

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General info

Function

Stable signal peptide. Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.. Glycoprotein G1. Forms the virion spikes together with glycoprotein G2. The glycoprotein spike trimers are connected to the underlying matrix. Interacts with the host receptor. Mediates virus attachment to the host primary receptor alpha-dystroglycan DAG1 (alpha-DG) at the cell surface. This attachment induces virion internalization apparently through macropinocytosis. Following endocytosis, there is a pH-dependent switch from binding DAG1 to the host lysosomal receptor LAMP1. This latter binding triggers the dissociation of GP1, exposing the fusion subunit, GP2, such that fusion can occur. Down-modulates host DAG1.. Glycoprotein G2. Forms the virion spikes together with glycoprotein G1. The glycoprotein spike trimers are connected to the underlying matrix. Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced by acidification.

Sequence similarities

Belongs to the arenaviridae GPC protein family.

Post-translational modifications

Pre-glycoprotein polyprotein GP complex. Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleavage by signal peptidase.

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Product protocols

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Target data

Stable signal peptide. Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.. Glycoprotein G1. Forms the virion spikes together with glycoprotein G2. The glycoprotein spike trimers are connected to the underlying matrix. Interacts with the host receptor. Mediates virus attachment to the host primary receptor alpha-dystroglycan DAG1 (alpha-DG) at the cell surface. This attachment induces virion internalization apparently through macropinocytosis. Following endocytosis, there is a pH-dependent switch from binding DAG1 to the host lysosomal receptor LAMP1. This latter binding triggers the dissociation of GP1, exposing the fusion subunit, GP2, such that fusion can occur. Down-modulates host DAG1.. Glycoprotein G2. Forms the virion spikes together with glycoprotein G1. The glycoprotein spike trimers are connected to the underlying matrix. Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced by acidification.
See full target information GPC
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Product promise

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