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SARS-CoV-2 Envelope and Membrane Reagents

Upon the entry of SARS-CoV-2 into host cells, from the full-length genomic RNA (29,903 nt) that serves as an mRNA, the first set of viral proteins are translated from the long (>21 kb) open reading frame ORF1ab (1).

The ORF1ab-encoded polyprotein is subsequently processed into 16 individual non-structural proteins (NSP) by two proteases PLpro/nsp3 and 3CLpro/nsp5. The 3’ half of ORF1ab, ORF1b, encodes a variety of enzymes critical for viral transcription and replication (1). In addition to the genomic RNA, nine major sub-genomic RNAs are produced (1). ORF1a and ORF1b are also separately translated and, as in all coronaviruses, translation of ORF1b in SARS-CoV-2 requires a programmed -1 ribosomal frameshift (-1 PRF) (2).

The genome RNA is packaged by the structural proteins to assemble progeny virions. The shorter sub-genomic RNAs encode conserved structural proteins spike protein (S), an envelope protein (E), membrane protein (M) and nucleocapsid protein (N), and several accessory proteins. SARS-CoV-2 is known to have at least 6 accessory proteins (ORFs 3a, 7, 7a, 7b, 8, and 10)

ProSci Incorporated offers antibodies and recombinant proteins representing most of the SARS-CoV-2 proteome. Below is a list of SARS-CoV-2 envelope and membrane reagents to serve as tools for your research needs!

The Envelope and Membrane Proteins (E, M)

The envelope protein is found in small quantities within the virus. It is most likely a transmembrane protein and with ion channel activity. The protein facilitates the assembly and release of the virus and has other functions such as ion channel activity. It is not necessary for viral replication but it is for pathogenesis.

The membrane protein is the most abundant structural protein. It does not contain a signal sequence and exists as a dimer in the virion. It may have two different conformations to enable it to promote membrane curvature as well as bind to nucleocapsid.

SARS-CoV-2 Envelope Reagents

Below are antibodies and recombinant proteins against the SARS-CoV-2 (COVID-19) envelope protein:

Antibodies

PRODUCTCAT. NO.APPLICATIONCLONALITYSPECIES
SARS-CoV-2 (COVID-19) Envelope Antibody (NT)3531ELISAPolyclonalRabbit
SARS-CoV-2 (COVID-19) Envelope Antibody (biotin)3531-biotinELISAPolyclonalRabbit
SARS-CoV-2 (COVID-19) Envelope Antibody (HRP)3531-HRPELISAPolyclonalRabbit
SARS-CoV-2 (COVID-19) Envelope Antibody (CT)9169ELISAPolyclonalRabbit
SARS-CoV-2 (COVID-19) Envelope Antibody10-518ELISAPolyclonalRabbit

Recombinant Proteins

ProductCat. No.SourceFusion TagSequence
SARS-CoV-2 (COVID-19) Envelope Recombinant Protein10-112E. coliHis-Avi TagMet1 - Val75
2019-nCoV Envelope Recombinant Protein97-082E. coliGST TagMet1 - Val75
SARS-CoV-2 (COVID-19) Envelope Recombinant Protein92-730E. coliN-BBP-6His TagMet1 - Val75
SARS-CoV-2 Envelope Protein RP20-205BacteriaN-Term MBP Uncleaved1 - 75
SARS-CoV-2 Envelope Protein RP20-231BacteriaN-Term GST Uncleaved1 - 75

SARS-CoV-2 Membrane Reagents

Below are antibodies and recombinant proteins against the SARS-CoV-2 (COVID-19) membrane protein:

Antibodies

ProductCat. No.ApplicationClonalitySpecies
SARS-CoV-2 (COVID-19) Membrane Antibody (CT)9165ELISA, WBPolyclonalRabbit
SARS-CoV-2 (COVID-19) Membrane Antibody (IN1)9157ELISA, IHC, WBPolyclonalRabbit
SARS-CoV-2 (COVID-19) Membrane Antibody (biotin)9157-biotinELISAPolyclonalRabbit
SARS-CoV-2 (COVID-19) Membrane Antibody (HRP)9157-HRPELISAPolyclonalRabbit
SARS-CoV-2 (COVID-19) Membrane Antibody (IN2)10-516ELISA, WBPolyclonalRabbit

Recombinant Proteins

ProductCat. No.SourceFusion TagSequence
SARS-CoV-2 (COVID-19) Membrane Recombinant Protein10-429E. coliN-His TagArg101 - Gln222
SARS-CoV-2 Membrane Protein Recombinant Protein20-203BacteriaN-Term MBP Uncleaved1 - 222
SARS-CoV-2 Membrane Protein Recombinant Protein20-230BacteriaN-Term GST Uncleaved1 - 222

References

[i] WRAPP D., WANG N., CORBETT K., et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation 13 March 2020 SCIENCE 13 MAR 2020: 1260-1263 DOI: 10.1126/science.abb2507

  • 1. D. Kim et al (2020) Cell 181, 125-130
  • 2. Y. Sun et al (2021) PNAS 118 No. 26, 20223051118 (https://doi.org/10.1073/pnas. 20223051118)

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