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CHO/Human MRGPRX2 Stable Cell Line Development Service

For research use only.

  1. Genetically modified cell lines best reflect MOA (Mechanism of Action)
  2. Higher activity and larger assay window for robust and reproducible cell-based bioassay
  3. Comprehensive application data to support assay development and validation
  4. Full tracible record, stringent quality control and validated cell passage stability
  5. Parental cell line legally obtained from internationally recognized cell resource bank and commercially licensed
  6. Global commercial license assistance whenever regulatory filing is required

描述(Description)

The CHO/Human MRGPRX2 Stable Cell Line was engineered to express the receptor full length human MRGPRX2 (Uniprot: Q96LB1). Surface expression of human MRGPRX2 was confirmed by flow cytometry.

应用说明(Application)

• Useful for cell-based MRGPRX2 binding assay

生长特性(Growth Properties)

Adherent

筛选标记(Selection Marker)

Puromycin (2 μg/mL)

培养基(Complete Growth Medium)

F-12K + 10% FBS

冻存液(Freeze Medium)

Serum-free cell cryopreservation medium

装量(Quantity)

1 vial contains at least 5×10^6 cells in 1 mL serum-free cryopreservation medium

存储(Storage)

Frozen in liquid nitrogen.

支原体检测(Mycoplasma Testing)

Negative

无菌检测(Sterility Testing)

Negative

使用说明(Instructions for Use)

See data sheet for detailed culturing and assay protocol.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

Receptor Assay

MRGPRX2 FACS

Expression analysis of human MRGPRX2 on CHO/Human MRGPRX2 Stable Cell Line by FACS.
Cell surface staining was performed on CHO/Human MRGPRX2 Stable Cell Line or negative control cell using PE-labeled anti-human MRGPRX2 antibody.

Protocol

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背景(Background)

MRGPRX2, a member of the Mas-related gene family, was found to be expressed in sensory neurons, mast cells and, most recently, in keratinocytes. MRGPRX2 mRNA is present in adipose tissue, esophagus, urinary bladder, lungs with the highest levels found in skin. Activation of MRGPRX2 leads to mast cell degranulation with subsequent pseudo-allergic reactions.

Limited Use&License Disclosure

BY USE OF THIS PRODUCT, RESEARCHER AGREES TO BE BOUND BY THE FOLLOWING TERMS OF LIMITED USE OF THIS CELL LINE PRODUCT.

  1. If the researcher is not willing to accept the terms of limited use of this cell line product, and the product is unused, ACRO will accept return of the unused product.
  2. Researchers may use this product for research use only, no commercial use is allowed. "Commercial use" means any and all uses of this product and derivatives by a party for profit or other consideration and may include but is not limited to use in: (1) product manufacture; and (2) to provide a service, information or data; and/or resale of the product or its derivatives, whether or not such product or derivatives are resold for use in research.
  3. This cell line is neither intended for any animal or human therapeutic purposes nor for any direct human in vivo use . You have no right to share, modify, transfer, distribute, sell, sublicense, or otherwise make the cell line available for use to other researchers, laboratories, research institutions, hospitals, universities, or service organizations.
  4. ACROBIOSYSTEMS MAKES NO WARRANTIES OR REPRESENTATIONS OF ANY KIND, EITHER EXPRESSED OR IMPLIED, WITH RESPECT TO THE SUITABILITY OF THE CELL LINE FOR ANY PARTICULAR USE.
  5. ACROBIOSYSTEMS ACCEPTS NO LIABILITY IN CONNECTION WITH THE HANDLING OR USE OF THE CELL LINE.
  6. Modifications of the cell line, transfer to a third party, or commercial use of the cell line may require a separate license and additional fees. Please contact order.cn@acrobiosystems.com for further details.

 

前沿进展

Construction and evaluation of recombinant rabies virus encoding three copies codon-optimized G genes as inactivated rabies vaccine in dogs and cats
Wu, Li, Wang et al
Vet Microbiol (2025) 304, 110481
Abstract: Rabies is a fatal zoonotic disease affecting various warm-blooded animals. The number of dogs and cats in China has surpassed 120 million, yet no domestic universal rabies vaccine for them. The glycoprotein (G) of the rabies virus (RABV) serves as the principal antigen for inducing virus-neutralizing antibodies (VNA). In this study, we constructed a recombinant RABV strain (designated SAD-tOG) carrying three copies of the codon-optimized G gene using reverse genetics. The SAD-tOG strain exhibited comparable growth kinetics to the parent strain in cell culture while demonstrating enhanced G protein expression. Mouse challenge experiments revealed significantly reduced pathogenicity and elevated immunogenicity in the recombinant strain. Subsequently, a safe and efficient water-based adjuvant was selected to prepare an inactivated rabies vaccine. In another experiment, the VNA titers of dogs and cats after vaccination were both greater than the WHO-recommended protective antibody titer of 0.5 IU/ml for 360 days. Comparative analysis showed these titers were higher than those induced by commercial vaccines currently used in China. These findings collectively indicate that the SAD-tOG strain represents a safer and more effective vaccine candidate for dog and cat rabies prevention.Copyright © 2025 Elsevier B.V. All rights reserved.
Evaluation of the immune status of dogs vaccinated against rabies by an enzyme-linked immunosorbent assay using crude preparations of insect cells infected with a recombinant baculovirus encoding the rabies virus glycoprotein gene
Santosh, Kumar, Kaur et al
PLoS One (2024) 19 (12), e0314516
Abstract: Evaluation of the effectiveness of vaccination of animals against rabies is not routinely implemented. In cases where it is carried out, the rapid fluorescent focus inhibition test (RFFIT) or the fluorescent antibody virus neutralization (FAVN) test are the recommended tests. However, both of these tests require handling of live rabies virus (RABV), and are cumbersome to perform. In view of this, the enzyme-linked immunosorbent assay (ELISA) has been proposed as a surrogate test; however, availability of appropriate antigen is a major impediment for the development of ELISAs to detect anti-rabies antibodies. The most widely used antigen is the RABV glycoprotein (G) purified from cell culture-propagated virus, which requires a biosafety level 3 containment. The alternative is to use recombinantly expressed G, which needs to be to be properly glycosylated and folded to serve as the best antigen. The most suitable system for its production is the baculovirus expression system (BVES). However, purification of RABV G is challenging. We therefore tested partially purified preparations in the form of extracts of insect cells infected with baculovirus expressing RABV G, against sera from vaccinated dogs in an indirect ELISA. The results showed good concordance against RFFIT, with sensitivity and specificity of 90.48% and 80.00%, respectively. The system may be used for quick screening to determine the presence and an approximate level of antibodies, and can be modified to enable monitoring of mass dog vaccination programs, as well as to facilitate certification of dogs intended for international travel and transportation.Copyright: © 2024 Santosh et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Structural insight into rabies virus neutralization revealed by an engineered antibody scaffold
Kedari, Iheozor-Ejiofor, Salminen et al
Structure (2024) 32 (12), 2220-2230.e4
Abstract: Host-cell entry of the highly pathogenic rabies virus (RABV) is mediated by glycoprotein (G) spikes, which also comprise the primary target for the humoral immune response. RABV glycoprotein (RABV-G) displays several antigenic sites that are targeted by neutralizing monoclonal antibodies (mAbs). In this study, we determined the epitope of a potently neutralizing human mAb, CR57, which we engineered into a diabody format to facilitate crystallization. We report the crystal structure of the CR57 diabody alone at 2.38 Å resolution, and in complex with RABV-G domain III at 2.70 Å resolution. The CR57-RABV-G structure reveals critical interactions at the antigen interface, which target the conserved "KLCGVL" peptide and residues proximal to it on RABV-G. Structural analysis combined with a cell-cell fusion assay demonstrates that CR57 effectively inhibits RABV-G-mediated fusion by obstructing the fusogenic transitions of the spike protein. Altogether, this investigation provides a structural perspective on RABV inhibition by a potently neutralizing human antibody.Copyright © 2024 The Author(s). Published by Elsevier Inc. All rights reserved.
Analysis of the antigenic and immunogenic properties of the native rabies virus glycoprotein purified by Lens culinaris lectin affinity chromatography
da Silva, Queiroz, Nogi et al
J Virol Methods (2025) 331, 115044
Abstract: Rabies virus glycoprotein (RABV-G) is responsible for the recognition of specific cell surface receptors and induces the production of neutralizing antibodies (VNA). Since RABV-G is a glycoprotein, this work aimed to evaluate Lens culinaris (LCA) chromatography as a simple and effective purification method. The purity and identification of the protein obtained were analyzed by SDS-PAGE, ELISA and lectin-binding assay. The antigenic properties of the purified RABV-G were evaluated by direct ELISA using human serum samples from individuals who had received rabies pre-exposure vaccination. For the immunogenicity study, Swiss Webster mice were immunized with purified RABV-G and the specific antibodies were measured by direct ELISA and RFFIT. As results, it was observed that the purified protein reveled a molecular mass of 55 kDa and the presence of carbohydrate; additionally, it was recognized by anti-rabies virus glycoprotein monoclonal antibody. Purified RABV-G induced high VNA titers (>50.0 IU/ml) in vivo, as detected by RFFIT, as well as RABV-G specific IgG1 (0.8 mean OD±SD) and IgG2a (0.3 mean OD±SD) antibodies, with a predominance of IgG1 (p< 0.001). In addition, it was observed that RABV-G was efficient in selectively detecting anti- RABV-G IgG in the sera of vaccinated individuals compared to the negative control. Therefore, LCA chromatography was efficient in preserving the native properties of RABV-G that are essential in inducing an adequate humoral immune response. In addition, the purified RABV-G presented analytical potential as an ELISA reagent.Copyright © 2024 Elsevier B.V. All rights reserved.
Showing 1-4 of 110 papers.
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