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Monoclonal Anti-Hendra virus F glycoprotein Antibody, Human IgG1 (3F4) (MALS verified)

抗体来源(Source)

Monoclonal Anti-Hendra virus F glycoprotein Antibody, Human IgG1 (3F4) 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)

3F4

种属(Species)

Mouse

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 Hendra virus Pre-Fusion glycoprotein (A263T) is expressed from human 293 cells.

特异性(Specificity)

Specifically recognizes Hendra virus Pre-Fusion glycoprotein(A263T).

应用(Application)

ApplicationRecommended Usage
Western Blot10-0.02 ug/mL
ELISA4-500 ng/mL

纯度(Purity)

>95% 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)

Fusion glycoprotein SDS-PAGE

Monoclonal Anti-Hendra virus F glycoprotein Antibody, Human IgG1 (3F4) on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

SEC-MALS

Fusion glycoprotein SEC-MALS

The purity of Monoclonal Anti-Hendra virus F glycoprotein Antibody, Human IgG1 (3F4) (Cat. No. FUN-MY2098) is more than 90% and the molecular weight of this protein is around 135-160 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

Fusion glycoprotein ELISA

Immobilized Hendra virus Pre-Fusion glycoprotein (A263T), His Tag (Cat. No. FUN-H52H4) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Hendra virus F glycoprotein Antibody, Human IgG1 (3F4) (Cat. No. FUN-MY2098) with a linear range of 3.9-31 ng/mL (QC tested).

Protocol

 

Western Blot验证

Fusion glycoprotein WESTERN BLOT

Detection of Monoclonal Anti-Hendra virus F glycoprotein Antibody, Human IgG1 (3F4), Human IgG1 | Human Kappa, HEK by Western Blot. Monoclonal Anti-Hendra virus F glycoprotein Antibody, Human IgG1 (3F4), Human IgG1 | Human Kappa, HEK at 0.02ug/ml dilution + Hendra virus Pre-Fusion glycoprotein (A263T), His Tag, His Tag at 400ng.

Secondary Antibody: (HFC)-HRP Goat Anti-Human IgG, Fcγ fragment specific (min X Bov,Hrs,Ms Sr Prot) at 1/2000 dilution.

Predicted band size: 65 kDa 12% Bis-Tris Protein Gel.

 
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背景(Background)

Hendra virus (HeV) and Nipah virus (NiV) are henipaviruses discovered in the mid-to late 1990s that possess a broad host tropism and are known to cause severe and often fatal disease in both humans and animals. HeV and NiV infect host cells through the coordinated efforts of two envelope glycoproteins. The G glycoprotein attaches to cell receptors, triggering the fusion (F) glycoprotein to execute membrane fusion. G is a type II homotetrameric transmembrane protein responsible for binding to ephrinB2 or ephrinB3 (ephrinB2/B3) receptors. F is a homotrimeric type I transmembrane protein that is synthesized as a premature F0 precursor and cleaved by cathepsin L during endocytic recycling to yield the mature, disulfide-linked, F1 and F2 subunits. Upon binding to ephrinB2/B3, NiV G undergoes conformational changes leading to F triggering and insertion of the F hydrophobic fusion peptide into the target membrane. Subsequent refolding into the more stable post-fusion F conformation drives merger of the viral and host membranes to form a pore for genome delivery to the cell cytoplasm.

 

前沿进展

Design, Synthesis and Anti-Influenza Virus Activity of 4-Tert-Butyl-N-(3-Oxo-1-Thia-4-Azaspiro[4.5]Dec-4-yl)Benzamide Derivatives That Target Hemagglutinin-Mediated Fusion
Çınar, Alikadıoğlu, Soylu-Eter et al
Drug Dev Res (2025) 86 (2), e70080
Abstract: Hemagglutinin (HA) is a viral glycoprotein that mediates influenza virus entry into the host cell and is considered a relevant viral target. We here report the identification of a class of 4-tert-butylphenyl-substituted spirothiazolidinones as HA-mediated fusion inhibitors with specific activity against influenza A/H3N2 virus. The novel spirocyclic compounds were achieved by using one-pot cyclocondensation method and the chemical structures were characterized by IR, 1H NMR, 13C NMR, and elemental analysis. Compound 2c, bearing methyl substitutions at positions 2- and 8- of the spiro ring displayed an EC50 value against influenza A/H3N2 virus of 1.3 μM and an antiviral selectivity index of 30. The fusion-inhibiting effect of compound 2c was revealed in the polykaryon assay which is based on cell-cell fusion when influenza virus H3 HA-transfected cells are exposed to low pH. Computer-aided docking was performed to predict the possible binding pocket in the H3 HA trimer. Resistance data and in silico studies indicated that compound 2c has an overlapping binding pocket in the stem region of H3 HA with the known fusion inhibitors TBHQ and arbidol.© 2025 The Author(s). Drug Development Research published by Wiley Periodicals LLC.
High soluble expression and characterization of human GalNAc transferase T2 and T11 in Escherichia coli
Wang, Zhang, Shi et al
Protein Expr Purif (2025) 231, 106712
Abstract: The efficient expression of soluble glycosyltransferases from mammalian sources in Escherichia coli (E. coli) remains a significant challenge, often resulting in misfolding and the formation of inclusion bodies. In this study, we investigated strategies to enhance the solubility and catalytic activity of human GalNAc-T2 and GalNAc-T11, two O-glycosyltransferases involved in O-glycosylation of glycoproteins. We found that fusion with maltose-binding protein (MBP) and cellulase catalytic domain (Cel-CD), which led to majority of the fusion proteins being soluble, could increase the solubility of the recombinant proteins. Enzyme activity assays revealed that the fusion glycosyltransferase exhibited significantly higher catalytic efficiency than non-fused enzymes. In addition, the influence of GalNAc-T11 lectin domain on substrate specificity was also determined. The presence of lectin domain had no influence on the recognition of specific substrate and the specific activity of GalNAc-T11. This work offers an efficient approach for the large-scale production of human glycosyltransferases with enhanced bioactivity, highlighting its potential for glycosylation engineering of glycoprotein drugs.Copyright © 2025. Published by Elsevier Inc.
Real-world evidence provides clinical insights into tissue-agnostic therapeutic approvals
Sledge, Yoshino, Xiu et al
Nat Commun (2025) 16 (1), 2646
Abstract: The US Food and Drug Administration approves tissue-agnostic therapies to target tumor biomarkers regardless of tumor type. In light of the growing number of such approvals in recent years, a better understanding of their relative clinical benefit across cancer types is required. To address this need, we analyzed tissue-agnostic indications (TMB-High, MSI-High/MMRd, BRAFV600E mutations, and NTRK and RET fusions) in a database of 295,316 molecularly-profiled tumor samples with associated clinical outcomes data. Here, we show that 21.5% of tumors harbored at least one of the tissue-agnostic indications investigated, including 5.4% lacking a cancer-specific indication. Our analysis reveals poor uptake of targeted therapies for rare NTRK fusions, significant differences in pembrolizumab-associated outcomes across tumor types for TMB-High and MSI-High/MMRd, as well as clinical benefits in tumor types and drugs of the same class not investigated in the pivotal clinical trials. These results demonstrate that treatment effects are not necessarily tissue-agnostic, and suggest possible expansion of therapeutic avenues for a given tissue-agnostic indication.© 2025. The Author(s).
Histopathology of C Cells and Medullary Thyroid Carcinoma
Cameselle-Teijeiro, Sobrinho-Simões
Recent Results Cancer Res (2025) 223, 9-50
Abstract: C cells are the neuroendocrine cell component of the thyroid gland that embryologically arise from the pharyngeal endoderm. Normal C cells are concentrated in the upper two-thirds of both lateral lobes, appear singly or in small groups dispersed in, among or peripherally to the follicles, and are involved in the production of calcitonin. Reactive C-cell hyperplasia should be differentiated from proliferation of atypical C cells (neoplastic C-cell hyperplasia) which is considered an intraepithelial neoplasia of C cells/medullary carcinoma in situ, a precursor lesion associated to familial medullary thyroid carcinoma (MTC). MTC typically exhibits a lobular and/or trabecular growth pattern with amyloid deposits; however, due to its great histological variability, immunohistochemical positivity for calcitonin, carcinoembryonic antigen, calcitonin-gene-related peptide, insulinoma-associated protein 1, and/or other markers is necessary to confirm diagnosis. Investigation of germline RET proto-oncogene mutation is mandatory to identify familial MTC. Somatic RET mutations or fusions as well as RAS mutations in cytological and/or biopsy samples may represent therapeutic targets. Mixed medullary and follicular-derived cell carcinoma is a heterogeneous group of tumors which needs to be distinguished from collision tumors.© 2025. The Author(s), under exclusive license to Springer Nature Switzerland AG.
Showing 1-4 of 35217 papers.
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Fusion glycoprotein靶点信息
英文全称:Respiratory syncytial virus F protein
中文全称:呼吸道合胞病毒F蛋白
种类:Homo sapiens
上市药物数量:3详情
临床药物数量:6详情
最高研发阶段:批准上市
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