MERS-CoV Envelope Protein (E8X6R) Rabbit mAb #89952
- WB
Supporting Data
| REACTIVITY | Vir |
| SENSITIVITY | Transfected Only |
| MW (kDa) | 12 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- Vir-Virus
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
MERS-CoV Envelope Protein (E8X6R) Rabbit mAb recognizes transfected levels of total MERS-CoV envelope protein.
Species Reactivity:
Virus
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro75 of MERS-CoV envelope protein.
Background
Middle East Respiratory Syndrome (MERS) is a contagious viral respiratory infection, whose causative agent was identified as the MERS-related coronavirus (MERS-CoV) (1,2). MERS-CoV is a single-stranded mRNA betacoronavirus. Similar to other infectious coronaviruses (e.g., SARS-CoV-2), the MERS-CoV genome encodes four key structural proteins (spike, envelope, membrane, and nucleocapsid) that make up the virion particle, in addition to at least 10 smaller open reading frames (ORFs) that encode the non-structural (accessory) proteins involved in viral replication (3,4). The MERS envelope protein (E) is the smallest of the structural proteins, and is abundantly expressed in the host cell during viral replication, despite only a fraction of synthesized E protein ultimately being incorporated into new viral particles (5). As in other betacoronaviruses, the MERS E protein likely functions as an ion channel (viroporin), involved in transmembrane molecular transport (6). Within infected host cells, E protein is largely localized to endoplasmic reticulum, Golgi, and related intermediate structures (e.g., ERGIC), consistent with a functionally important role in assembly, budding, and intracellular trafficking of new virion particles (5). This is supported by studies showing that MERS virions were incapable of replication after deletion of the gene encoding the E protein (7).
- Bermingham, A. et al. (2012) Euro Surveill 17, 20290.
- de Groot, R.J. et al. (2013) J Virol 87, 7790-2.
- Javorsky, A. et al. (2021) Commun Biol 4, 724.
- van Boheemen, S. et al. (2012) mBio 3, e00473-12. doi: 10.1128/mBio.00473-12.
- Schoeman, D. and Fielding, B.C. (2019) Virol J 16, 69.
- Barrantes, F.J. (2021) Acta Crystallogr D Struct Biol 77, 391-402.
- Almazán, F. et al. (2013) mBio 4, e00650-13.
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