Revision 1

#45394Store at -20C

1 Kit

(8 x 20 microliters)

Cell Signaling Technology

Orders: 877-616-CELL (2355) [email protected]

Support: 877-678-TECH (8324)

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3 Trask LaneDanversMassachusetts01923USA
For Research Use Only. Not for Use in Diagnostic Procedures.
Product Includes Product # Quantity Mol. Wt Isotype/Source
SARS-CoV-2 Spike Protein (S1) (E5S3V) Rabbit mAb 99423 20 µl 110, 220 kDa Rabbit IgG
SARS-CoV-2 Spike Protein (RBD) (E7B3E) Rabbit mAb 63847 20 µl 110, 220 kDa Rabbit IgG
Cleaved SARS-CoV-2 Spike Protein (Ser686) Antibody 84534 20 µl 100 kDa Rabbit 
ACE2 (E5O6J) XP® Rabbit mAb 92485 20 µl 120-135 kDa Rabbit IgG
Neuropilin-1 (D62C6) Rabbit mAb 3725 20 µl 120-140 kDa Rabbit IgG
Basigin/EMMPRIN (E1S1V) Rabbit mAb 13287 20 µl 38-58 kDa Rabbit IgG
Furin Antibody 43996 20 µl 90 kDa Rabbit 
Cathepsin L Antibody 71298 20 µl 25-42 kDa Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl Goat 

Please visit for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.


The SARS-CoV-2 Virus-Host Interaction Antibody Sampler Kit provides an economical means of detecting key viral and host proteins involved in SARS-CoV-2 infection of human host cells. The kit includes enough antibodies to perform two western blot experiments with each primary antibody.


Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibodies.


The cause of the COVID-19 pandemic is a novel and highly pathogenic coronavirus, termed SARS-CoV-2 (severe acute respiratory syndrome coronavirus-2). SARS-CoV-2 is a member of the Coronaviridae family of viruses (1). The SARS-CoV-2 virion is comprised of four key structural proteins: spike (S), envelope (E), membrane (M), and nucleocapsid (N) (2). Coronavirus spike proteins are class I fusion proteins and harbor an ectodomain, a transmembrane domain, and an intracellular tail (3,4). The highly glycosylated ectodomain projects from the viral envelope surface and facilitates attachment and fusion with the host cell membrane. The ectodomain can be further subdivided into the receptor-binding domain (RBD) S1 and membrane-fusion (S2) subunits, which are produced upon proteolysis by host proteases. S1 and S2 subunits are reassociated after cleavage, assembling into crown-like homotrimers (2,4).

The SARS-CoV-2 spike protein contains a novel tetrabasic "furin cleavage site" (FCS) at the S1/S2 junction. Research studies suggest this site is cleaved by proprotein convertases (e.g., furin) or lysosomal proteases (e.g., cathepsin L) (5,6). S1/S2 cleavage elicits a confirmational change in the spike protein that positions elements of the trimeric RBD in an exposed "up" position, priming it for interaction with host receptor proteins. Cleavage can occur at multiple steps of the viral lifecycle, including during viral packaging, or upon contact of the intact virion with the host cell surface. This novel cleavage event has been suggested to contribute to the high infectivity rate of the SARS-CoV-2 virus (7).

The SARS-CoV-2 virus has been shown to utilize the angiotensin-converting enzyme 2 (ACE2) protein as its primary receptor for cellular entry (8). However, research studies have suggested that other cell surface proteins may serve as receptors or co-receptors for SARS-CoV-2. These include neuropilin-1 (NPN1), a single-pass transmembrane receptor that can function as part of a semaphorin receptor complex, and as a vascular endothelial growth factor (VEGF) receptor (9), and Basigin/EMMPRIN (CD147), a type I integral membrane receptor belonging to the immunoglobulin superfamily (10).

  1. Zhou, P. et al. (2020) Nature 579, 270-273.
  2. Tortorici, M.A. and Veesler, D. (2019) Adv Virus Res 105, 93-116.
  3. Li, F. et al. (2006) J Virol 80, 6794-800.
  4. Li, F. (2016) Annu Rev Virol 3, 237-261.
  5. Coutard, B. et al. (2020) Antiviral Res 176, 104742.
  6. Jaimes, J.A. et al. (2020) iScience 23, 101212.
  7. Hasan, A. et al. (2021) J Biomol Struct Dyn 39, 3025-3033.
  8. Shang, J. et al. (2020) Nature 581, 221-224.
  9. Cantuti-Castelvetri, L. et al. (2020) Science 370, 856-860.
  10. Wang, K. et al. (2020) Signal Transduct Target Ther 5, 283.

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