MERS-CoV (NCoV / Novel coronavirus) Spike Protein fragment (RBD, aa 367-606, His Tag)


MERS-CoV (NCoV / Novel coronavirus) Spike Protein fragment (RBD, aa 367-606, His Tag): Product Information

> 90 % as determined by SDS-PAGE.
< 1.0 EU per μg protein as determined by the LAL method.
Testing in progress
Protein Construction
A DNA sequence encoding the receptor binding domain (RBD) of spike protein (Human betacoronavirus 2c EMC/2012)(AFS88936.1) (Glu367-Tyr606) was expressed with a polyhistidine tag at the C-terminus.
Expressed Host
Baculovirus-Insect Cells
Predicted N Terminal
Glu 367
Molecule Mass
The recombinant receptor binding domain (RBD) of spike protein (Human betacoronavirus 2c EMC/2012) consists 251 amino acids and predicts a molecular mass of 27.7 kDa.
Lyophilized from sterile 20 mM Tris, 500 mM NaCl, 10 % glycerol, pH 7.4.
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

MERS-CoV (NCoV / Novel coronavirus) Spike Protein fragment (RBD, aa 367-606, His Tag): Images

MERS-CoV (NCoV / Novel coronavirus) Spike Protein fragment (RBD, aa 367-606, His Tag): Alternative Names

S Protein, MERS-CoV

CoV spike Background Information

The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell: they are essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. The SARS-CoV spike (S) protein is composed of two subunits; the S1 subunit contains a receptor-binding domain that engages with the host cell receptor angiotensin-converting enzyme 2 and the S2 subunit mediates fusion between the viral and host cell membranes. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity, during infection with SARS-CoV.
  • Shen S, et al. (2007) Expression, glycosylation, and modification of the spike (S) glycoprotein of SARS CoV. Methods Mol Biol. 379: 127-35.
  • Du L, et al. (2009) The spike protein of SARS-CoV--a target for vaccine and therapeutic development. Nat Rev Microbiol. 7 (3): 226-36.
  • Xiao X, et al. (2004) The SARS-CoV S glycoprotein. Cell Mol Life Sci. 61 (19-20): 2428-30.
  • A Human DPP4-Knockin Mouse's Susceptibility to Infection by Authentic and Pseudotyped MERS-CoV
    Fan, C;Wu, X;Liu, Q;Li, Q;Liu, S;Lu, J;Yang, Y;Cao, Y;Huang, W;Liang, C;Ying, T;Jiang, S;Wang, Y;
  • Immunogenicity of Different Forms of Middle East Respiratory Syndrome S Glycoprotein
    Ozharovskaia, TA;Zubkova, OV;Dolzhikova, IV;Gromova, AS;Grousova, DM;Tukhvatulin, AI;Popova, O;Shcheblyakov, DV;Scherbinin, DN;Dzharullaeva, AS;Erokhova, AS;Shmarov, MM;Loginova, SY;Borisevich, SV;Naroditsky, BS;Logunov, DY;Gintsburg, AL;
    Acta Naturae
    ELISA and cell-based
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