SARS-CoV-2 Envelope Antibody [DyLight 650] Summary
| Immunogen |
This antibody was raised against a peptide corresponding to 14 amino acids near the carboxyl terminus of SARS-CoV-2 (COVID-19) Envelope protein. The immunogen is located within the last 50 amino acids of SARS-CoV-2 (COVID-19) Envelope protein. |
| Predicted Species |
SARS-CoV (93%). Backed by our 100% Guarantee. |
| Isotype |
IgG |
| Clonality |
Polyclonal |
| Host |
Rabbit |
| Gene |
E |
| Purity |
Peptide affinity purified |
| Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
| Dilutions |
- ELISA
- Immunohistochemistry
- Western Blot
|
| Application Notes |
Optimal dilution of this antibody should be experimentally determined. |
Reactivity Notes
Packaging, Storage & Formulations
| Storage |
Store at 4C in the dark. |
| Buffer |
50mM Sodium Borate |
| Preservative |
0.05% Sodium Azide |
| Purity |
Peptide affinity purified |
Notes
DyLight (R) is a trademark of Thermo Fisher Scientific Inc. and its subsidiaries.
Alternate Names for SARS-CoV-2 Envelope Antibody [DyLight 650]
Background
The SARS-CoV-2 Envelope protein is one of the four major structural proteins of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative agent of COVID-19 (1). The envelope protein is the smallest of the four structural proteins, which also includes the membrane protein, spike protein, and nucleocapsid protein (1,2). The envelope protein is synthesized as a 75 amino acid protein with a theoretical molecular weight of approximately 8.4 kDa (2,3). Furthermore, the envelope protein of SARS-CoV-2 has 94.7% sequence identity and 97.4% sequence similarity to the envelope protein of SARS-CoV (2). Structurally, the envelope protein is a membrane protein with a N-terminal domain, an alpha-helical transmembrane domain, and a hydrophilic C-terminal domain (1,4). The envelope protein has multiple functions in viral replication including viral assembly, release, and pathogenesis (2,4). Additionally, the SARS-CoV-2 envelope protein has ion channel activity and functions as a viroporin with a role in virion trafficking (2,4). Coronaviruses lacking the envelope protein are shown to have reduced viral titer and slowed or defective maturation, indicative of a role in virus production and growth (4).
References
1. Malik Y. A. (2020). Properties of Coronavirus and SARS-CoV-2. The Malaysian Journal of Pathology.
2. Yoshimoto F. K. (2020). The Proteins of Severe Acute Respiratory Syndrome Coronavirus-2 (SARS CoV-2 or n-COV19), the Cause of COVID-19. The Protein Journal. https://doi.org/10.1007/s10930-020-09901-4
3. Uniprot (P0DTC4)
4. J Alsaadi, E. A., & Jones, I. M. (2019). Membrane binding proteins of coronaviruses. Future Virology. https://doi.org/10.2217/fvl-2018-0144
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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Product General Protocols
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Video Protocols
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Secondary Antibodies
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Isotype Controls
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Blogs on SARS-CoV-2 Envelope
![Western Blot: Goat anti-Rabbit IgG (H+L) Secondary Antibody [HRP] [NB7160] - Western blot showing vemurafenib treatment in BRAFV600E CRC cells inhibits fission mediator DRP1 with no significant effect on fusion proteins (Mfn1 & 2) using MFN-1 antibody (NBP1-51841) and corresponding secondary antibody, goat anti-rabbit IgG-HRP (NB7160). Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/33738242).](https://images.novusbio.com/images/Goat-anti-Rabbit-IgG-H+L-Secondary-Antibody-HRP-Western-Blot-NB7160-img0001.jpg "Western Blot: Goat anti-Rabbit IgG (H+L) Secondary Antibody [HRP] [NB7160] - Western blot showing vemurafenib treatment in BRAFV600E CRC cells inhibits fission mediator DRP1 with no significant effect on fusion proteins (Mfn1 & 2) using MFN-1 antibody (NBP1-51841) and corresponding secondary antibody, goat anti-rabbit IgG-HRP (NB7160). Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/33738242).")
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