Anti-MERS-CoV Spike Protein S2 polyclonal antibody (CABT-B1952)

Rabbit Anti-MERS-CoV Spike Protein S2 polyclonal antibody for WB, ELISA, IHC-P, IP

Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Species Reactivity
MERS-CoV
Immunogen
Recombinant MERS-CoV (NCoV / Novel coronavirus) Spike glycoprotein Protein
Conjugate
Unconjugated

Applications


Application Notes
WB: 0.2-1 μg/ml
ELISA: 0.1-0.2 μg/ml
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.

Target


Alternative Names
Middle East respiratory symptom coronavirus Spike Protein S2 subunit

Citations


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Custom Antibody Labeling


We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More

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References


Spike Gene Deletion Quasispecies in Serum of Patient With Acute MERS-CoV Infection

JOURNAL OF MEDICAL VIROLOGY

Authors: Lu, Xiaoyan; Rowe, Lori A.; Frace, Michael; Stevens, James; Abedi, Glen R.; Elnile, Osman; Banassir, Taleb; Al-Masri, Malak; Watson, John T.; Assiri, Abdullah; Erdman, Dean D.

The spike glycoprotein of the Middle East respiratory coronavirus (MERS-CoV) facilitates receptor binding and cell entry. During investigation of a multi-facility outbreak of MERS-CoV in Taif, Saudi Arabia, we identified a mixed population of wild-type and variant sequences with a large 530 nucleotide deletion in the spike gene from the serum of one patient. The out of frame deletion predicted loss of most of the S2 subunit of the spike protein leaving the S1 subunit with an intact receptor binding domain. This finding documents human infection with a novel genetic variant of MERS-CoV present as a quasispecies. (C) 2016 Wiley Periodicals, Inc.

NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Authors: Mahajan, Mukesh; Chatterjee, Deepak; Bhuvaneswari, Kannaian; Pillay, Shubhadra; Bhattacharjya, Surajit

The lethal Coronaviruses (CoVs), Severe Acute Respiratory Syndrome-associated Coronavirus (SARS-CoV) and most recently Middle East Respiratory Syndrome Coronavirus, (MERS-CoV) are serious human health hazard. A successful viral infection requires fusion between virus and host cells carried out by the surface spike glycoprotein or S protein of CoV. Current models propose that the S2 subunit of S protein assembled into a hexameric helical bundle exposing hydrophobic fusogenic peptides or fusion peptides (FPs) for membrane insertion. The N terminus of S2 subunit of SARS-CoV reported to be active in cell fusion whereby FPs have been identified. Atomic-resolution structure of FPs derived either in model membranes or in membrane mimic environment would glean insights toward viral cell fusion mechanism. Here, we have solved 3D structure, dynamics and micelle localization of a 64-residue long fusion peptide or LFP in DPC detergent micelles by NMR methods. Micelle bound structure of LFP is elucidated by the presence of discretely folded helical and intervening loops. The C-terminus region, residues F42-Y62, displays a long hydrophobic helix, whereas the N-terminus is defined by a short amphipathic helix, residues R4-Q12. The intervening residues of LFP assume stretches of loops and helical turns. The N-terminal helix is sustained by close aromatic and aliphatic sidechain packing interactions at the non-polar face. N-15{H-1}NOE studies indicated dynamical motion, at ps-ns timescale, of the helices of LFP in DPC micelles. PRE NMR showed that insertion of several regions of LFP into DPC micelle core. Together, the current study provides insights toward fusion mechanism of SARS-CoV.

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