MERS-CoV Spike/RBD Protein fragment (aa 367-606, His)

Catalog No. TMPY-00402

Synonyms: cov spike Protein, MERS-CoV, coronavirus spike Protein, MERS-CoV, RBD Prote, ncov RBD Protein, MERS-CoV, ncov s1 Protein, MERS-CoV, coronavirus s1 Protein, MERS-CoV, coronavirus s2 Protein, MERS-CoV, ncov s2 Protein, MERS-CoV, ncov spike Protein, MERS-CoV

The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 2019-nCoV) can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.

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MERS-CoV Spike/RBD Protein fragment (aa 367-606, His)

Pack Size	Availability	Price/USD
100 μg	In stock	$ 583.00
200 μg	5 days	$ 994.00
500 μg	5 days	$ 2,010.00

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COA DATASHEET SDS

Biological Description

Technical Params

Product Properties

References and Literature

Biological Information

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Description

Species	MERS-CoV
Expression System	Baculovirus-Insect Cells
Tag	His
Accession Number	K0BRG7
Synonyms	cov spike Protein, MERS-CoV, coronavirus spike Protein, MERS-CoV, RBD Prote, ncov RBD Protein, MERS-CoV, ncov s1 Protein, MERS-CoV, coronavirus s1 Protein, MERS-CoV, coronavirus s2 Protein, MERS-CoV, ncov s2 Protein, MERS-CoV, ncov spike Protein, MERS-CoV
Construction	A DNA sequence encoding the MERS-CoV receptor binding domain (RBD) of spike protein fragment (AFS88936.1) (Glu367-Tyr606) was expressed with a polyhistidine tag at the C-terminus.
Protein Purity	> 90 % as determined by SDS-PAGE.
Molecular Weight	Approxiamtely 27.7 kDa

Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method.
Formulation	Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 8.0. Pleasecon tact usfor any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution	A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
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.
Shipping	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.
Research Background	The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 2019-nCoV) can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.

References and Literature

1. Xiao X,et al. (2004) The SARS-CoV S glycoprotein. Cell Mol Life Sci. 61 (19-20): 2428-30. 2. Shen S,et al. (2007) Expression, glycosylation, and modification of the spike (S) glycoprotein of SARS CoV. Methods Mol Biol. 379: 127-35. 3. 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.

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Keywords

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