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Monoclonal Anti-Mumps virus HN Antibody, Human IgG1 (7D12) (MALS verified)

抗体来源(Source)

Monoclonal Anti-Mumps virus HN Antibody, Human IgG1 (7D12) is a chimeric monoclonal antibody recombinantly expressed from HEK293, which combines the variable region of a mouse monoclonal antibody with Human constant domain.

克隆号(Clone)

7D12

亚型(Isotype)

Human IgG1 | Human Kappa

偶联(Conjugate)

Unconjugated

抗体类型(Antibody Type)

Recombinant Monoclonal

种属反应性(Reactivity)

Virus

免疫原(Immunogen)

Recombinant Mumps virus (strain Miyahara vaccine) (MuV) HN Protein, His Tag (HNN-M52H3) is expressed from human 293 cells.

特异性(Specificity)

Specifically recognizes Mumps virus (strain Miyahara vaccine) (MuV) HN.

应用(Application)

ApplicationRecommended Usage
ELISA0.1-8 ng/mL 

纯度(Purity)

>90% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

纯化(Purification)

Protein A purified / Protein G purified

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.

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
 

电泳(SDS-PAGE)

Hemagglutinin-neuraminidase/HN (MuV) SDS-PAGE

Monoclonal Anti-Mumps virus HN Antibody, Human IgG1 (7D12) on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90% (With Star Ribbon Pre-stained Protein Marker).

SEC-MALS

Hemagglutinin-neuraminidase/HN (MuV) SEC-MALS

The purity of Monoclonal Anti-Mumps virus HN Antibody, Human IgG1 (7D12) (Cat. No. HNN-M701) is more than 90% and the molecular weight of this protein is around 135-155 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

Hemagglutinin-neuraminidase/HN (MuV) ELISA

Immobilized Mumps virus (strain Miyahara vaccine) (MuV) HN Protein, His Tag (Cat. No. HNN-M52H3) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Mumps virus HN Antibody, Human IgG1 (7D12) (Cat. No. HNN-M701) with a linear range of 0.1-1 ng/mL (QC tested).

Protocol

 

活性(Bioactivity)-SPR

Hemagglutinin-neuraminidase/HN (MuV) SPR

Monoclonal Anti-Mumps virus HN Antibody, Human IgG1 (7D12) (Cat. No. HNN-M701) captured on Protein A Chip can bind Mumps virus (strain Miyahara vaccine) (MuV) HN Protein, His Tag (Cat. No. HNN-M52H3) with an affinity constant of 0.474 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).

Protocol

 
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ACRO质量管理体系
 
 

背景(Background)

The two surface glycoproteins of the mumps virus are the hemagglutinin-neuraminidase (HN) and Fusion proteins. These glycoproteins are essential for viral entry to host cells, and the spread of newly formed virions. The HN protein is a 582-amino acid structural glycoprotein of the mumps virus. HN is a type II membrane protein in which the N terminus is oriented towards the cytoplasm and the C terminus is extracellular.The HN protein exhibits both hemagglutinin and neuraminidase properties and is critical for membrane fusion and viral entry into host cells.

 

前沿进展

Structure-based design of glycoprotein subunit vaccines for mumps
Loomis, Lai, Sowers et al
Proc Natl Acad Sci U S A (2024) 121 (47), e2404053121
Abstract: Mumps virus (MuV) is a highly contagious paramyxovirus that is endemic in most regions of the world and continues to cause outbreaks even in highly immunized populations. Outbreaks of mumps in countries with high measles, mumps, and rubella vaccination coverage have been attributed to waning immunity and antigenic differences between the Jeryl Lynn vaccine strain (genotype A) and circulating wild-type viruses. To obtain a subunit vaccine, we used structure-based design to engineer the mumps fusion (F) glycoprotein stabilized in its prefusion conformation (Pre-F) as well as a chimeric immunogen comprising Pre-F linked to mumps hemagglutinin neuraminidase (HN); in mice, both Pre-F antigen and the chimeric antigen elicited potent cross-reactive plaque reducing neutralizing titers to genotypes A, G, and H mumps. A crystal structure of mumps Pre-F at 2.16 Å resolution validated the stabilization strategy, while a post-fusion form of F was engineered as a comparator. Monoclonal antibodies to mumps Pre-F and HN were isolated from immunized mice; 7 of 14 Pre-F-specific antibodies and 9 of 15 HN-specific antibodies were capable of neutralizing genotype G MuV with a range of potencies. Additionally, 7 of 14 Pre-F-specific antibodies neutralized genotype A mumps. Structural and binding analyses of Pre-F-specific antibodies revealed binding to four discrete neutralizing antigenic sites and binding analyses of HN-specific antibodies revealed binding to five discrete neutralizing antigenic sites. Overall, the PreF and the chimeric Pre-F/HN immunogens are promising candidates to boost MMR-elicited immunity to mumps or as a next-generation vaccine.
Novel sialidase inhibitors suppress mumps virus replication and infection
Takahashi, Kurebayashi, Otsubo et al
Glycobiology (2024) 34 (11)
Abstract: The prevalent human pathogen, mumps virus (MuV; orthorubulavirus parotitidis) causes various complications and serious sequelae, such as meningitis, encephalitis, deafness, and impaired fertility. Direct-acting antivirals (DAAs) targeting MuV which can prevent mumps and mumps-associated complications and sequelae are yet to be developed. Paramyxoviridae family members, such as MuV, possess viral surface hemagglutinin-neuraminidase (HN) protein with sialidase activity which facilitates efficient viral replication. Therefore, to develop DAAs targeting MuV we synthesized MuV sialidase inhibitors. It is proposed that the viral HN has a single functional site for N-acetylneuraminic acid (Neu5Ac) binding and sialidase activity. Further, the known MuV sialidase inhibitor is an analog of Neu5Ac-2,3-didehydro-2-deoxy-N-acetylneuraminic acid (DANA)-which lacks potency. DANA derivatives with higher MuV sialidase inhibitory potency are lacking. The MuV-HN-Neu5Ac binding site has a hydrophobic cavity adjacent to the C4 position of Neu5Ac. Exploiting this, here, we synthesized DANA derivatives with increasing hydrophobicity at its C4 position and created 3 novel sialidase inhibitors (Compounds 1, 2, and 3) with higher specificity for MuV-HN than DANA; they inhibited MuV replication step to greater extent than DANA. Furthermore, they also inhibited hemagglutination and the MuV infection step. The insight-that these 3 novel DANA derivatives possess linear hydrocarbon groups at the C4-hydroxyl group of DANA-could help develop highly potent sialidase inhibitors with high specificity for MuV sialidase, which may function as direct-acting MuV-specific antivirals.© The Author(s) 2024. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.
Characterization of Natural and Synthetic Sialoglycans Targeting the Hemagglutinin-Neuraminidase of Mumps Virus
Forgione, Di Carluccio, Milanesi et al
Front Chem (2021) 9, 711346
Abstract: The inhibition of surface viral glycoproteins offers great potential to hamper the attachment of viruses to the host cells surface and the spreading of viral infection. Mumps virus (MuV) is the etiological agent of the mumps infectious disease and causes a wide spectrum of mild to severe symptoms due to the inflammation of the salivary glands. Here we focus our attention on the hemagglutinin-neuraminidase (HN) isolated from MuV SBL-1 strain. We describe the molecular features of host sialoglycans recognition by HN protein by means of NMR, fluorescence assays and computational studies. Furthermore, we also describe the synthesis of a N-acetylneuraminic acid-derived thiotrisaccharide targeting the viral protein, and the corresponding 3D-complex. Our results provide the basis to improve the design and synthesis of potent viral hemagglutinin-neuraminidase inhibitors.Copyright © 2021 Forgione, Di Carluccio, Milanesi, Kubota, Fabregat Nieto, Molinaro, Hashiguchi, Francesconi, Marchetti and Silipo.
Evolutionary analysis of mumps viruses of genotype F collected in mainland China in 2001-2015
Cui, Rivailler, Zhu et al
Sci Rep (2017) 7 (1), 17144
Abstract: Mumps incidence in mainland China remains at a high level. Genotype F has been the predominant genotype of mumps virus (MuV) in the last 20 years in mainland China. To better understand the genetic characteristics of MuV in China, the sequences of the Small Hydrophobic (SH), Hemagglutinin-Neuraminidase (HN) and Fusion (F) genes of MuVs of genotype F collected during 2001-2015 were determined. The evolutionary rates of the HN and F genes were similar (0.5 × 10-3 substitutions/site/year) whereas the SH gene evolutionary rate was three times faster. The most recent common ancestor of genotype F was traced back to 1980. Four lineages were identified within HN and F MuV sequences. A phylogeographic analysis indicated that the genotype F viruses originally spread from the Liaoning and Shandong provinces followed by a spread to the South and East of China. This study provides important genetic baseline data for the development of prevention and control measures of mumps.
Showing 1-4 of 13 papers.
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