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AB190459

Biotin Anti-MARV GP antibody

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(4 Publications)

Rabbit Polyclonal VGP antibody - conjugated to Biotin. Carrier free. Suitable for WB and reacts with Marburg virus samples. Cited in 4 publications. Immunogen corresponding to Synthetic Peptide within Lake Victoria marburgvirus (strain Angola/2005) GP aa 400 to C-terminus.

View Alternative Names

Envelope glycoprotein, Virion spike glycoprotein, GP

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Conjugation

Biotin

Excitation/Emission
Carrier free

Yes

Reacts with

Marburg virus

Applications

WB

applications

Immunogen

Synthetic Peptide within Lake Victoria marburgvirus (strain Angola/2005) GP aa 400 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q1PD50

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
The purified antibody was conjugated with biotin at a molar ratio of 20:1 (Biotin: antibody), and purified from unconjugated biotin by diafiltration.
Storage buffer
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|Store in the dark

Supplementary information

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

The MARV GP also known as Marburg virus glycoprotein is a critical protein in the structure of the Marburg virus. This glycoprotein plays a central role in viral entry into host cells by mediating attachment and fusion. MARV GP has a mass of approximately 9 kilodaltons and is expressed on the surface of the Marburg virus. The protein's function is essential for the virus to enter human cells facilitating its ability to spread and multiply in the host.
Biological function summary

The Marburg virus glycoprotein aids the virus in evading host immune responses. It is part of a complex that involves other viral proteins enhancing its role in the viral lifecycle. MARV GP helps the virus adhere to host cell membranes subsequently triggering endocytosis—a process where the cell membrane engulfs the virus. This capability allows the virus to replicate inside the host efficiently and complicates the ability of the immune system to detect and eliminate the virus.

Pathways

MARV GP interaction is important within the fusion and endocytosis pathways. It operates alongside cellular proteins that facilitate endocytic uptake such as clathrin and dynamin. MARV GP binding triggers a cascade that utilizes several host cell pathways to ensure fusion of the viral envelope with the host cell membrane enabling the entry of viral RNA into the host cytoplasm. This cooperative action permits seamless integration into the host cell processes.

MARV GP is directly implicated in the pathogenicity of Marburg virus disease a severe and fatal hemorrhagic fever. It shares similarities with proteins in Ebola virus such as Ebola virus glycoprotein which contributes to similar symptoms. Both glycoproteins introduce challenges in developing effective vaccines and therapeutics as they are involved in virus escape from immune detection. Understanding the role of MARV GP in disease mechanisms can drive better-targeted treatments and interventions.

Product protocols

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

Target data

GP1 is responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into the host cell. Binding to CD209 and CLEC4M, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses, facilitate infection of macrophages and endothelial cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by DCs and subsequent transmission to susceptible cells without DCs infection (trans infection) (By similarity).. GP2 acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states : pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide (By similarity).
See full target information GP

Publications (4)

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

eLife 13: PubMed40387093

2025

Human CD29+/CD56+ myogenic progenitors display tenogenic differentiation potential and facilitate tendon regeneration.

Applications

Unspecified application

Species

Unspecified reactive species

Xiexiang Shao,Xingzuan Lin,Hao Zhou,Minghui Wang,Lili Han,Xin Fu,Sheng Li,Siyuan Zhu,Shenao Zhou,Wenjun Yang,Jianhua Wang,Zhanghua Li,Ping Hu

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

Frontiers in microbiology 13:927122 PubMed35756049

2022

A Novel and Secure Pseudovirus Reporter System Based Assay for Neutralizing and Enhancing Antibody Assay Against Marburg Virus.

Applications

Unspecified application

Species

Unspecified reactive species

Jinhao Bi,Haojie Wang,Hongyan Pei,Qiuxue Han,Na Feng,Qi Wang,Xinyue Wang,Zhenshan Wang,Shimeng Wei,Liangpeng Ge,Meng Wu,Hao Liang,Songtao Yang,Feihu Yan,Yongkun Zhao,Xianzhu Xia

Vaccines 8: PubMed32455764

2020

A Multi-Filovirus Vaccine Candidate: Co-Expression of Ebola, Sudan, and Marburg Antigens in a Single Vector.

Applications

Unspecified application

Species

Unspecified reactive species

Sarah Sebastian,Amy Flaxman,Kuan M Cha,Marta Ulaszewska,Ciaran Gilbride,Hannah Sharpe,Edward Wright,Alexandra J Spencer,Stuart Dowall,Roger Hewson,Sarah Gilbert,Teresa Lambe
View all publications

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