SARS Spike (14-667)

SARS Spike (14-667 a.a.), Recombinant
Cat. No.
BT6380
Source

HEK293

Synonyms
Appearance
Sterile Filtered clear solution.
Purity

Protein is >90% pure as determined SDS-PAGE.

Usage
THE BioTek'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

The HEK293 derived recombinant protein contains the SARS Coronavirus Spike S1 Gycoprotein, amino acids 14-667 fused to His tag at C-terminal.

Product Specs

Introduction
The SARS Coronavirus is an enveloped virus that has three outer structural proteins: membrane (M), envelope (E), and spike (S) proteins. The virus's spike (S)-glycoprotein interacts with a cellular receptor and mediates membrane fusion, which allows the virus to enter susceptible target cells. Therefore, S-protein plays a crucial role in the virus infection cycle and is the primary target of neutralizing antibodies.
Description
This recombinant protein derived from HEK293 contains the SARS Coronavirus Spike S1 Glycoprotein, amino acids 14-667. It is fused to a His tag at the C-terminal.
Physical Appearance
Sterile Filtered clear solution.
Formulation
SARS Spike S1 glycoprotein is lyophilized from 1x PBS pH-7.4 + 10% Glycerol.
Stability
Protein is shipped on ice packs. Upon arrival, Store at -20°C.
Biological Activity
Biological activity is measured by the protein's binding ability in a functional ELISA with Human ACE-2 (CAT# enz-1125)
Purity
Protein purity is >90% as determined by SDS-PAGE.
Source

HEK293

Purification Method

Purified by immobilized metal affinity chromatographic technique.

Product Science Overview

Introduction

The SARS Spike (14-667 a.a.), Recombinant, refers to a specific segment of the spike (S) glycoprotein from the Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV). This recombinant protein is expressed in human 293 cells (HEK293) and contains amino acids from Serine 14 to Arginine 667 . The spike protein is crucial for the virus’s ability to infect host cells and is a major target for vaccine development and therapeutic interventions.

Structure and Function

The spike (S) glycoprotein of coronaviruses, including SARS-CoV, is essential for the virus’s ability to bind to host cells and initiate infection. The spike protein is composed of two subunits:

  • S1 Subunit: Contains the receptor-binding domain (RBD) that engages with the host cell receptor, angiotensin-converting enzyme 2 (ACE2).
  • S2 Subunit: Mediates the fusion between the viral and host cell membranes, facilitating viral entry into the host cell .

The recombinant SARS Spike (14-667 a.a.) includes the S1 subunit and part of the S2 subunit, making it a valuable tool for studying the virus’s entry mechanism and for developing neutralizing antibodies.

Expression and Purification

The recombinant SARS Spike (14-667 a.a.) is typically expressed in HEK293 cells, which are human embryonic kidney cells commonly used for protein production. The protein is purified and often tagged with a His-tag to facilitate purification and detection . The molecular weight of this recombinant protein is approximately 67.2 kDa .

Applications

The recombinant SARS Spike (14-667 a.a.) has several important applications:

  • Vaccine Development: As a major immunogen, the spike protein is a key target for vaccine development. It induces neutralizing antibodies and T-cell responses, providing protective immunity against SARS-CoV .
  • Therapeutic Research: The spike protein is a target for entry inhibitors, which can block the virus from entering host cells and prevent infection .
  • Diagnostic Tools: The recombinant protein can be used in immunoassays to detect antibodies against SARS-CoV in patient samples, aiding in the diagnosis of SARS-CoV infections .
Storage and Handling

For long-term storage, the recombinant SARS Spike (14-667 a.a.) should be kept in a lyophilized state at -20°C or lower. It is important to avoid repeated freeze-thaw cycles to maintain the protein’s stability and functionality .

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