SARS Spike Protein Antibody - BSA Free

Simple Western lane view shows recombinant SARS-CoV-2 Spike S2 Protein, loaded at 50 ng/mL. A specific band was detected for SARS-CoV-2 Spike S2 Protein at approximately 58 kDa (as indicated) using a serial dilution of Rabbit Anti-SARS-CoV Spike Protein Polyclonal Antibody (Catalog # NB100-56578) followed by incubation with HRP-conjugated Anti-Rabbit IgG Secondary Antibody. This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.

SARS-CoV-2 spike overexpressed 293T cell lysate. Antibody dilution: 1:3000. Two bands for full length spike and cleaved S2 are shown, respectively. Western blot image submitted by a verified customer review.

Western blot shows SARS-CoV-1 Spike (Catalog # 10581-CV), SARS CoV-2 Spike (Catalog # 10586-CV), SArS-CoV-2 Spike S2 Subunit (Catalog # 10584-CV). Membrane was probed with 0.5 ug/mL of SARS Spike Protein Antibody (Catalog # NB100-56578) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for SARS-CoV-2 Spike S2 Subunit at approximately 70 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1. Internally validated Western blot.

Western blot analysis of SARS Spike Protein in (A) transfected and (B) untransfected mouse melanoma cell lysate.

Western blot shows recombinant protein SARS-CoV-2 Spike S2 Subunit. Membrane was probed with 0.5 ug/mL of Rabbit Anti-SARS Spike Protein Polyclonal Antibody (Catalog # NB100-56578) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for SARS-CoV-2 Spike S2 Subunit at approximately 70 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1. Internally validated Western blot.

Simple Western lane view shows SARS-CoV-2 lysate, loaded at 1:20 dilution. SARS-CoV-2 Spike Protein was detected using 6.25 ug/mL of Rabbit Anti-SARS-CoV Spike Protein Polyclonal Antibody (Catalog # NB100-56578) followed by incubation with HRP-conjugated Anti-Rabbit IgG Secondary Antibody. This experiment was conducted under reducing conditions and using the 12-230 kDa separation system. SARS-CoV-2 lysate courtesy of University of Maryland.

• Reactivity: V, V
• Applications: WB, Simple Western, ICC/IF, IHC
• Clonality: Polyclonal
• Host: Rabbit
• Conjugate: Unconjugated
• Format: BSA Free
• Concentration: 1.0 mg/ml

SARS Spike Protein Antibody - BSA Free Summary

• Description: Novus Biologicals Rabbit SARS Spike Protein Antibody - BSA Free (NB100-56578) is a polyclonal antibody validated for use in IHC, WB, ICC/IF and Simple Western. Anti-SARS Spike Protein Antibody: Cited in 33 publications. All Novus Biologicals antibodies are covered by our 100% guarantee.
• Immunogen: The antibody was developed by immunizing rabbits with a synthetic peptide corresponding to amino acids 1124-1140 (C-GNCDVVIGIVNNTVYDP) from the S (Spike glycoprotein)(Spike protein S2') for the Human SARS coronavirus (Genbank accession no. YP_009724390)
• Specificity: Full length Spike protein transfected into UM92 cells was used as a positive control and an approximate 139 kDa band was observed. Dot Blot results using recombinant proteins for cross-reactivity testing revealed high reactivity to SARS-CoV-2 Spike Protein, 1000-1200 a.a. (NBP2-90973) and low/no reactivity towards MERS Spike 2 or H1N1 (NBP1-99041).
• Isotype: IgG
• Clonality: Polyclonal
• Host: Rabbit
• Purity: Immunogen affinity purified

Applications/Dilutions

• Dilutions:
  • Immunocytochemistry/ Immunofluorescence reported in scientific literature (PMID 16081529)
  • Immunohistochemistry reported in scientific literature (PMID 34357881)
  • Simple Western 1:40 - 1:160
  • Western Blot 0.05 - 1.0 ug/mL

Packaging, Storage & Formulations

• Storage: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
• Buffer: PBS
• Preservative: 0.02% Sodium Azide
• Concentration: 1.0 mg/ml
• Purity: Immunogen affinity purified

Alternate Names for SARS Spike Protein Antibody - BSA Free

• COVID-19 Spike
• E2 glycoprotein
• E2
• Human coronavirus spike glycoprotein
• Peplomer protein
• S glycoprotein
• S
• SARS coronavirus S protein
• SARS coronavirus Spike Protein
• SARS CoV S glycoprotein
• SARS CoV Spike protein
• SARS CoV
• SARS-CoV S protein
• SARS-COV Spike
• SARSCoV
• SARS-COV-2 S protein
• SARS-COV-2 Spike glycoprotein
• SARSCOV2 Spike protein
• Severe acute respiratory syndrome spike glycoprotein
• Severe acute respiratory syndrome virus spike glycoprotein
• Spike glycoprotein
• VGL2

Background

It has recently been shown that SARS (severe acute respiratory syndrome) is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness, such as the common cold, in humans. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The glycosilated spike protein (as well as the nucleocapsid protein) can be detected in infected cell culture supernatants with antisera from SARS patients.

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.

Publications for SARS Spike Protein Antibody (NB100-56578)(40)

Publications using NB100-56578

• Baid K, Shrivastava S, Luc J et al. Early innate immune response and evolution of a SARS-CoV-2 furin cleavage site inactive variant in bat cells. Cell reports 2025-07-01 [PMID: 40608518]
• Kugathasan R, Sukhova K, Moshe M et al. Deep mutagenesis scanning using whole trimeric SARS-CoV-2 spike highlights the importance of NTD-RBD interactions in determining spike phenotype PLOS Pathogens 2023-08-03 [PMID: 37535672]
• Peacock TP, Brown JC, Zhou J et al. The SARS-CoV-2 variant, Omicron, shows rapid replication in human primary nasal epithelial cultures and efficiently uses the endosomal route of entry. bioRxiv 2022-01-01 (WB)
• Mitchell J, Mastrodomenico V, Hartnett J et al. A HiBiT-tagged pseudovirus-like particle platform for safe, rapid quantification of virus neutralization and antibody-dependent enhancement. Journal of Virology 2025-10-08 [PMID: 41060029]
• Morgan A, Vu M, Zhou Y et al. The furin cleavage site is required for pathogenesis, but not transmission, of SARS-CoV-2. Journal of Virology 2025-06-10 [PMID: 40492735]
• Hirabayashi A, Muramoto Y, Takenaga T et Al. Coatomer complex I is required for the transport of SARS-CoV-2 progeny virions from the endoplasmic reticulum-Golgi intermediate compartment mBio 2024-11-29 [PMID: 39611845]
• Cone AS, Zhou Y, McNamara RP et Al. CD81 fusion alters SARS-CoV-2 Spike trafficking mBio 2024-09-01 [PMID: 39140770]
• Shengliang Zhang, Wafik S. El-Deiry Transfected SARS-CoV-2 spike DNA for mammalian cell expression inhibits p53 activation of p21(WAF1), TRAIL Death Receptor DR5 and MDM2 proteins in cancer cells and increases cancer cell viability after chemotherapy exposure Oncotarget 2024-01-01 [PMID: 38709242]
• Zhang Y, Anbir S, McTiernan J et Al. Synthesis, insertion, and characterization of SARS-CoV-2 membrane protein within lipid bilayers Sci Adv 2024-03-01 [PMID: 38416838]
• Tomokazu Tamura, Keita Mizuma, Hesham Nasser, Sayaka Deguchi, Miguel Padilla-Blanco, Yoshitaka Oda, Keiya Uriu, Jarel E M Tolentino, Shuhei Tsujino, Rigel Suzuki, Isshu Kojima, Naganori Nao, Ryo Shimizu, Lei Wang, Masumi Tsuda, Michael Jonathan, Yusuke Kosugi, Ziyi Guo, Alfredo A Hinay, Olivia Putri, Yoonjin Kim, Yuri L Tanaka, Hiroyuki Asakura, Mami Nagashima, Kenji Sadamasu, Kazuhisa Yoshimura, Akatsuki Saito, Jumpei Ito, Takashi Irie, Shinya Tanaka, Jiri Zahradnik, Terumasa Ikeda, Kazuo Takayama, Keita Matsuno, Takasuke Fukuhara, Kei Sato Virological characteristics of the SARS-CoV-2 BA.2.86 variant. Cell host & microbe 2024-02-19 [PMID: 38280382]
• Reuter N, Chen X, Kropff B et al. SARS-CoV-2 Spike Protein Is Capable of Inducing Cell-Cell Fusions Independent from Its Receptor ACE2 and This Activity Can Be Impaired by Furin Inhibitors or a Subset of Monoclonal Antibodies Viruses 2023-07-04 [PMID: 37515187] (Western Blot, Immunocytochemistry/ Immunofluorescence)
• Tan CCS, Trew J, Peacock TP et al. Genomic screening of 16 UK native bat species through conservationist networks uncovers coronaviruses with zoonotic potential Nature communications 2023-06-27 [PMID: 37369644] (WB)
• Eens S, Van Hecke M, Favere K et al. B-cell lymphoblastic lymphoma following intravenous BNT162b2 mRNA booster in a BALB/c mouse: A case report Frontiers in Oncology 2023-05-01 [PMID: 37197431]
• Vu MN, Morris DR, Alvarado RE et al. Loss-of-function mutation in Omicron variants reduces spike protein expression and attenuates SARS-CoV-2 infection bioRxiv : the preprint server for biology 2023-04-18 [PMID: 37131784] (Western Blot)
• Meng W, Guo S, Cao S et al. Development and characterization of a new monoclonal antibody against SARS-CoV-2 NSP12 (RdRp) Journal of medical virology 2022-10-21 [PMID: 36271490]
• Vu MN, Lokugamage KG, Plante JA et al. QTQTN motif upstream of the furin-cleavage site plays a key role in SARS-CoV-2 infection and pathogenesis Proceedings of the National Academy of Sciences 2022-08-09 [PMID: 35881779]
• E Rosendal, IS Mihai, M Becker, D Das, L Frängsmyr, BD Persson, GD Rankin, R Gröning, J Trygg, M Forsell, J Ankarklev, A Blomberg, J Henriksson, AK Överby, A Lenman Serine Protease Inhibitors Restrict Host Susceptibility to SARS-CoV-2 Infections MBio, 2022-05-09;0(0):e0089222. 2022-05-09 [PMID: 35532162]
• Johnson BA, Xie X, Bailey AL et al. Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis Nature 2021-03-11 [PMID: 33494095]
• Tan C, Trew J, Peacock T et al. Surveillance of 16 UK native bat species through conservationist networks uncovers coronaviruses with zoonotic potential bioRxiv 2023-01-20 (Western Blot)
• Warner BM, Santry LA, Leacy A Et al. Intranasal vaccination with a Newcastle disease virus-vectored vaccine protects hamsters from SARS-CoV-2 infection and disease iScience 2021-11-19 [PMID: 34632328] (WB)
• GarcIa-Dorival I, Cuesta-Geijo MA, Barrado-Gil L Et al. Identification of Niemann-Pick C1 protein as a potential novel SARS-CoV-2 intracellular target Antiviral research 2021-08-24 [PMID: 34450201] (WB, SARS-CoV-2)
• Schaller MA, Sharma Y, Dupee Z Et al. Ex vivo SARS-CoV-2 infection of human lung reveals heterogeneous host defense and therapeutic responses JCI insight 2021-08-06 [PMID: 34357881] (IF/IHC, SARS-CoV-2)
• Meng B, Kemp SA, Papa G et al. Recurrent emergence of SARS-CoV-2 spike deletion H69/V70 and its role in the variant of concern lineage B.1.1.7 Cell 2021-06-29 [PMID: 34166617]
• Peacock TP, Goldhill DH, Zhou J et al. The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets Nature microbiology 2021-04-27 [PMID: 33907312]
• Hornich BF, Grobkopf AK, Schlagowski S et al. SARS-CoV-2 and SARS-CoV Spike-Mediated Cell-Cell Fusion Differ in Their Requirements for Receptor Expression and Proteolytic Activation Journal of Virology 2021-05-12 [PMID: 33608407] (WB)
• Sanchez-Felipe, L, Vercruysse, T Et al. A single-dose live-attenuated YF17D-vectored SARS-CoV-2 vaccine candidate. Nature 2020-12-01 [PMID: 33260195] (Simple Western)
• Plante, J A, Liu, Y Et al. Spike mutation D614G alters SARS-CoV-2 fitness. Nature 2021-04-01 [PMID: 33106671] (IF/IHC)
• Smith T, Patel A, Ramos S et al. Immunogenicity of a DNA Vaccine Candidate for COVID-19 Nat Commun. 2020-05-20 [PMID: 32433465] (WB, ICC/IF, Human)
• Ujike M, Huang C, Shirato K et al. Two palmitylated cysteine residues of the severe acute respiratory syndrome coronavirus spike (S) protein are critical for S incorporation into virus-like particles, but not for M-S co-localization. J Gen Virol. 2012-04-01 [PMID: 22238235]
• Bertram S, Glowacka I, Muller MA et al. Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease. J Virol. 2011-12-01 [PMID: 21994442] (WB)
  
  Details:
  Product cited: SARS-S Spike protein (IMG-557). WB: 293T cells cotransfected with SARS-S and TTSP expression plasmids , Fig 3. Note: The SARS-S (IMG-557) antibody was transfected validated by WB in 293T cells, Fig 3.
• Matsuyama S, Nagata N, Shirato K et al. Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2. J Virol. 2010-12-01 [PMID: 20926566]
• Watanabe R, Matsuyama S, Shirato K et al. Entry from the cell surface of severe acute respiratory syndrome coronavirus with cleaved S protein as revealed by pseudotype virus bearing cleaved S protein. J Virol. 2008-12-01 [PMID: 18786990] (WB)
  
  Details:
  WB (HeLa cells), Fig. 2B.
• Simmons G, Gosalia DN, Rennekamp AJ et al. Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Proc Natl Acad Sci U S A. 2005-08-16 [PMID: 16081529] (ICC/IF)
• Fukushi S, Mizutani T, Saijo M et al. Vesicular stomatitis virus pseudotyped with severe acute respiratory syndrome coronavirus spike protein. J Gen Virol. 2005-08-01 [PMID: 16033974]
• Vu MN Spike Processing and Protease Usage Effects on SARS-CoV-2 Pathogenesis Thesis 2023-01-01 (WB)
• Matsuyama Shutoku, Ujike Makoto, Ishii Koji et al. Enhancement of SARS-CoV infection by proteases. Adv Exp Med Biol. 2006-01-01 [PMID: 17037538]
• Zhang Y, Anbir S, McTiernan J et al. Synthesis, Insertion, and Characterization of SARS-CoV-2 Membrane Protein Within Lipid Bilayers bioRxiv 2023-10-02 (WB)
  
  Details:
  Dilution 1:1000
• Spruth Martin, Kistner Otfried, Savidis-Dacho Helga et al. A double-inactivated whole virus candidate SARS coronavirus vaccine stimulates neutralising and protective antibody responses. Vaccine. 2006-01-30 [PMID: 16214268]
• Matsuyama Shutoku, Ujike Makoto, Morikawa Shigeru et al. Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection. Proc Natl Acad Sci U S A. 2005-08-30 [PMID: 16116101] (WB)

Review for SARS Spike Protein Antibody (NB100-56578) (1)

Average Rating: 5

(Based on 1 review)

We have 1 review tested in 1 species: Human.

reviewed by: Verified Customer WB Human 10/02/2020

Summary

• Application: Western Blot
• Sample Tested: SARS-CoV-2 spike transfected 293T cell lysate
• Species: Human
• Lot: AB092903C-03

FAQs for SARS Spike Protein Antibody (NB100-56578). (Showing 1 - 4 of 4 FAQs).

1. Do you know if Sars Spike Protein Antibody (16F1071) will cross react with SARS-2?
   • NBP2-24746 has no similarity unfortunately. However, NBP2-24808, NBP2-24942, and NB100-56578 have 100% sequence homology with the SARS-CoV-2 Spike Protein.
2. I am looking for a primary antibody to sars spike protein to the new COVID-19.
   • NBP1-28850, NB100-56578, NBP2-24808, NBP2-24942 have 100% homology to the new SARS-CoV-2 virus.
3. Hello can you help me to identify detection antibody for COvid-19 spike protein? NB100-56578 is for spike of the Covid-19 not for the original SARS virus correct?
   • NB100-56578 was originally developed to the original SARS virus, but the homology of the target sequence of this antibody to the spike protein for COVID-19 is identical, so we can guarantee that it will work for COVID-19 detection.
4. The spec sheet says that NB100-56578 species cross reactivity 100% wonder what that means…
   • It means we have blasted homology between our immunogens and COVID19, and this one is 100% homologous. However, we do not have COVID19 samples to validate with, so it is predicted to work on COVID19.