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AB190655

Anti-LASV GP antibody

2

(1 Review)

|

(2 Publications)

Rabbit Polyclonal SHMT1 antibody. Suitable for WB and reacts with Synthetic peptide samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Lassa virus Josiah GPC.

View Alternative Names

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

1 Images
Western blot - Anti-LASV GP antibody (AB190655)
  • WB

Supplier Data

Western blot - Anti-LASV GP antibody (AB190655)

All lanes:

Western blot - Anti-LASV GP antibody (ab190655) at 0.1 µg/mL

Lane 1:

Recombinant Lassa virus glycoprotein at 0.05 µg

Lane 2:

Recombinant Lassa virus glycoprotein at 0.1 µg

Secondary

All lanes:

Anti-rabbit IgG-HRP conjugate and TMB membrane substrate

Predicted band size: 57 kDa

Observed band size: 60 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Applications

WB

applications

Immunogen

Synthetic Peptide within Lassa virus Josiah GPC. The exact immunogen used to generate this antibody is proprietary information.

P08669

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
Preservative: 0.02% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

The Lassa virus glycoprotein (LASV GP) functions as an important element in virus entry. This glycoprotein consists of two subunits GP1 and GP2 which undergo cleavage for activation and have a combined molecular mass of approximately 75 kDa. Of the two GP1 facilitates viral attachment to host cells while GP2 mediates membrane fusion. LASV GP primarily expresses on the surface of Lassa virus particles and infected host cells playing an important role in initiating infection.
Biological function summary

The Lassa virus glycoprotein complex facilitates the entry and replication of the virus inside host cells. It requires interaction between GP1 and host cell receptors like alpha-dystroglycan to initiate virus attachment. GP2's fusogenic activity then enables fusion of viral and host membranes allowing viral RNA entry into the host cell cytoplasm. The glycoprotein complex drives viral infectivity and pathogenicity supporting the cross-species transmission of the virus.

Pathways

LASV GP engages the endocytic pathway to deliver viral genetic material into host cells. This process involves the endocytosis and trafficking of virus-receptor complexes to late endosomes. It also coordinates with cellular proteins like cathepsin L for the cleavage necessary to activate membrane fusion. Such interactions with endocytic components highlight LASV GP's centrality in the viral life cycle and host-pathogen interactions.

LASV GP constitutes a fundamental role in Lassa fever pathogenesis. Lassa fever an acute viral hemorrhagic illness manifests after LASV GP mediates effective viral entry and replication in host tissues. The glycoprotein's interaction with host factors like alpha-dystroglycan marks it as a target in therapeutic strategies and vaccine development. The viral glycoprotein's influence on immune evasion and disease severity highlights its significance in the context of Lassa fever research.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Stable signal peptide. Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C) (PubMed : 35173332). Helps to stabilize the spike complex in its native conformation (PubMed : 35173332). 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 (PubMed : 14555961).. Glycoprotein G1. Forms the virion spikes together with glycoprotein G2 (PubMed : 26849049, PubMed : 35173332). The glycoprotein spike trimers are connected to the underlying matrix (PubMed : 26849049). Interacts with the host receptor. Mediates virus attachment to the host primary receptor alpha-dystroglycan DAG1 (alpha-DG) at the cell surface (PubMed : 11967329, PubMed : 27147735). This attachment induces virion internalization apparently through macropinocytosis (Probable) (PubMed : 27147735). Following endocytosis, there is a pH-dependent switch from binding DAG1 to the host lysosomal receptor LAMP1 (PubMed : 24970085, PubMed : 27605678, PubMed : 28448640). This latter binding triggers the dissociation of GP1, exposing the fusion subunit, GP2, such that fusion can occur (PubMed : 24970085). Down-modulates host DAG1 (PubMed : 17761532).. Glycoprotein G2. Forms the virion spikes together with glycoprotein G1 (PubMed : 26849049, PubMed : 35173332). The glycoprotein spike trimers are connected to the underlying matrix (PubMed : 26849049). 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 (PubMed : 31004664).
See full target information GPC

Publications (2)

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

PLoS pathogens 20:e1012262 PubMed38924060

2024

Potent immunogenicity and protective efficacy of a multi-pathogen vaccination targeting Ebola, Sudan, Marburg and Lassa viruse.

Applications

Unspecified application

Species

Unspecified reactive species

Amy Flaxman,Sarah Sebastian,Sofia Appelberg,Kuan M Cha,Marta Ulaszewska,Jyothi Purushotham,Ciaran Gilbride,Hannah Sharpe,Alexandra J Spencer,Sagida Bibi,Daniel Wright,Isabel Schmidt,Stuart Dowall,Linda Easterbrook,Stephen Findlay-Wilson,Sarah Gilbert,Ali Mirazimi,Teresa Lambe

PloS one 18:e0289745 PubMed37556495

2023

Analytical sameness methodology for the evaluation of structural, physicochemical, and biological characteristics of Armlupeg: A pegfilgrastim biosimilar case study.

Applications

Unspecified application

Species

Unspecified reactive species

Arati Deshmukh,Rishank Goyal,Kalyana Sundaram,Kaustubh Dange,Tejshri Lakhote,Sanjay Niranjan,Jennifer Bharucha,Ashok Mishra,Bhavesh Vats,Sanjay Tiwari
View all publications

Product promise

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