Coronavirus/SARS-CoV-2 Basics Materials

We have the most comprehensive collection of coronavirus basic materials including genomic RNA, cDNA, different coronavirus proteins expressed in bacteria, baculouvirus, and 293 expression systems as well as antibodies for general coronavirus protein detection.

RNA and cDNA

abm provides RNA and DNA controls for quality control and validation of diagnostic tests.

RNA ControlsAuthentic coronavirus whole genome RNAs (30kb) isolated from clinical samples by heathcare professionals.
cDNA ControlscDNAs reverse transcribed from coronavirus RNA using a mixture of random coronavirus specific primers.


There are quite a few proteins that are known to be associated with coronavirus biology and we have prepared each of these proteins from different expression systems (bacteria, baculovirus, and 293 cells) in a ready-to-use format.

Spike (S)Mediates binding of SARS-CoV-2 to the ACE2 host cell receptor.
Nucleocapsid (N)Binds and packs viral genome and regulates RNA synthesis during viral replication.
N-S fusion proteinsFusion proteins.
Envelope (E)Integral membrane protein that oligomerizes to form ion channels associated with SARS-CoV-2 pathogenesis.
Membrane (M)Most abundant structural protein of SARS-CoV-2. Involved in organizing viral assembly.
ORF1abEncodes replicase polyproteins required for SARS-CoV-2 viral RNA replication and transcription.
RNA dependent RNA Polymerase (NSP12)RNA replicase that catalyzes replication of RNA from an RNA template.
NSP1Nonstructural leader protein that inhibits translation of host mRNAs.
NSP15Nonstructural endoribonuclease protein important in viral infection and pathogenesis.
NSP7Nonstructural protein that forms a polymerization complex with nsp8 and nsp12.
NSP8Primase protein that forms a polymerization complex with nsp7 and nsp12.
NSP5ANonstructural protein.
NSP9Nonstructural RNA-binding protein that forms the replicase complex.
Papain-like Protease (PLpro)Processes polyproteins into proteins for viral replication and removes ubiquitin and ISG15 from host proteins to inactivate the host immune response.
Guanine-N7 Methyltransferase Recombinant Protein (NSP14)A proofreading exoribonuclease with a (guanine-N7) methyltransferase activity for viral mRNA capping.
Helicase (NSP13)Unwinds double-stranded nucleic acid for viral self-reproduction.


It will be impossible to advance coronavirus research without quality coronavirus antibodies. For this reason, we have developed coronavirus antibodies against different epitope proteins. In addition, we have also successfully isolated a collection of human coronavirus antibodies from convalescent coronavirus patients.

Spike (S)Full lengthView Products
S1 Subunit proteinView Products
S2 SubunitView Products
Receptor Binding Domain (RBD) SubunitView Products
C-terminalView Products
Envelope (E)Full lengthView Products
N-terminalView Products
Nucleocapsid (N)Full lengthView Products
Membrane (M)Full lengthView Products
ORF1abFull lengthView Products
RNA dependent RNA Polymerase (RDRP)Full lengthView Products
ORF7aFull lengthView Products
NSP8Full lengthView Products
NSP3Full lengthView Products
Helicase (NSP13)Full lengthView Products
3CL ProteaseFull lengthView Products

Stable Cell Lines Expressing SARS-CoV-2 Genes

Spike (S)HEK293TT6793
Spike (S), S1 SubunitSF9T6797
Spike (S), S2 SubunitSF9T6798


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Gui, M. et al. “Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding” Cell Res. (2017) 27:119-29. doi: 10.1038/cr.2016.152

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Dong, S. et al. “A guideline for homology modeling of the proteins from newly discovered betacoronavirus, 2019 novel coronavirus (2019‐nCoV)” J. Med. Vir. (2020) doi: 10.1002/jmv.25768

Zhang, L. et al. “Structural and Biochemical Characterization of Endoribonuclease Nsp15 Encoded by Middle East Respiratory Syndrome Coronavirus” J. Virol. (2018) 92:e00893-18. doi: 10.1128/JVI.00893-18

Kirchdoerfer, R.N. et al. “Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors” Nat. Commun. (2019) 10:2342. doi: 10.1038/s41467-019-10280-3

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