SARS MERS RBD

SARS MERS Spike Receptor Binding Domain Recombinant
Cat. No.
BT5250
Source

Sf9, Baculovirus cells.

Synonyms

Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein

Appearance
Sterile filtered colorless solution.
Purity

Greater than 90.0% as determined by SDS-PAGE.

Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

SARS MERS RBD Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 258 amino acids (358-606 aa) and having a molecular mass of 28.2kDa.
SARS MERS RBD is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

The Middle East Respiratory Syndrome Coronavirus (MERS-CoV) has been a concern since April 2012, with cases reported globally. Coronaviruses, responsible for illnesses ranging from the common cold to severe conditions like SARS (severe acute respiratory syndrome), are a family of viruses known for high mortality rates. MERS-CoV, a novel strain within this family, triggers severe pneumonia and acute respiratory distress, leading to significant mortality. As of January 27th, 2015, the World Health Organization (WHO) has documented 956 human cases, with 351 fatalities. The anticipation is for a continued rise in cases involving this new coronavirus strain. A key structural protein in this virus, and other coronaviruses, is the large surface spike glycoprotein. This protein protrudes from the virion surface and plays a crucial role in binding to and entering target cells. The spike protein consists of two domains: S1 and S2. The S1 domain determines cellular tropism and facilitates interaction with the target cell, while the S2 domain is responsible for membrane fusion. Located at the C-terminal of the S1 domain is a receptor-binding domain. This domain is critical for vaccine development and serves as a potential antigen for diagnostic purposes.

Description

SARS MERS RBD Recombinant, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It consists of 258 amino acids (spanning positions 358 to 606) and has a molecular weight of 28.2kDa. A 6 amino acid His-tag is fused to the C-terminus of the SARS MERS RBD. Purification is achieved using proprietary chromatographic techniques.

Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation

The SARS MERS RBD solution is provided at a concentration of 0.5mg/ml. It is formulated in a solution containing 10% glycerol and Phosphate-Buffered Saline (PBS) at a pH of 7.4.

Stability

For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure long-term stability during storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. It is crucial to avoid repeated cycles of freezing and thawing.

Purity

The purity of the product is determined to be greater than 90.0% using SDS-PAGE analysis.

Synonyms

Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein

Source

Sf9, Baculovirus cells.

Amino Acid Sequence

ADPSGVYSVS SFEAKPSGSV VEQAEGVECD FSPLLSGTPP QVYNFKRLVF TNCNYNLTKL LSLFSVNDFT CSQISPAAIA SNCYSSLILD YFSYPLSMKS DLSVSSAGPI SQFNYKQSFS NPTCLILATV PHNLTTITKP LKYSYINKCS RLLSDDRTEV PQLVNANQYS PCVSIVPSTV WEDGDYYRKQ LSPLEGGGWL VASGSTVAMT EQLQMGFGIT VQYGTDTNSV CPKLEFANDT KIASQLGNCV EYHHHHHH

Product Science Overview

Introduction

The Severe Acute Respiratory Syndrome (SARS) and Middle East Respiratory Syndrome (MERS) are both caused by coronaviruses, specifically SARS-CoV and MERS-CoV. These viruses have spike (S) proteins on their surfaces, which play a crucial role in the virus’s ability to infect host cells. The spike protein contains a region known as the Receptor Binding Domain (RBD), which is responsible for binding to the host cell receptors, facilitating viral entry.

Structure and Function of Spike Protein

The spike protein is a trimeric class I fusion protein that mediates the entry of the virus into host cells. It consists of two subunits:

  • S1 subunit: Contains the RBD, which directly interacts with the host cell receptor.
  • S2 subunit: Facilitates the fusion of the viral and host cell membranes.

For SARS-CoV, the RBD binds to the Angiotensin-Converting Enzyme 2 (ACE2) receptor on human cells. In contrast, MERS-CoV’s RBD binds to the Dipeptidyl Peptidase 4 (DPP4) receptor .

Recombinant RBD Proteins

Recombinant RBD proteins are engineered versions of the RBD that can be used for various applications, including vaccine development and therapeutic interventions. These recombinant proteins are produced using genetic engineering techniques, where the gene encoding the RBD is inserted into an expression system, such as bacteria, yeast, or mammalian cells, to produce the protein in large quantities.

Applications in Vaccine Development

Recombinant RBD proteins have shown promise as vaccine candidates due to their ability to induce strong neutralizing antibody responses. For instance, a study demonstrated that a truncated RBD of MERS-CoV spike protein fused with a human IgG Fc fragment (S377-588-Fc) could potently inhibit MERS-CoV infection and induce strong neutralizing antibody responses in vaccinated mice . This suggests that recombinant RBD proteins can be further developed as effective and safe vaccines for preventing MERS-CoV infection.

Therapeutic Potential

In addition to vaccine development, recombinant RBD proteins can also be used as therapeutic agents. By blocking the interaction between the viral RBD and the host cell receptor, these proteins can prevent the virus from entering and infecting host cells. This approach has been explored for both SARS-CoV and MERS-CoV, showing potential in inhibiting viral infection and reducing disease severity .

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