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Anti-Glycoprotein E (VZV) Antibody, Human IgG1 (1B10) (MALS verified)

抗体来源(Source)

Anti-Glycoprotein E (VZV) Antibody, Human IgG1 (1B10) 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)

1B10

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 Varicella zoster virus (strain Oka vaccine) Envelope Glycoprotein E (gE) derived from human 293 cells.

特异性(Specificity)

This product is a specific antibody specifically reacts with Glycoprotein E/gE (VZV).

应用(Application)

ApplicationRecommended Usage
ELISA0.1-8 ng/mL

纯度(Purity)

>90% as determined by SDS-PAGE.

>95% 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)

Glycoprotein E/gE (VZV) SDS-PAGE

Anti-Glycoprotein E (VZV) Antibody, Human IgG1 (1B10) on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90%.

SEC-MALS

Glycoprotein E/gE (VZV) SEC-MALS

The purity of Anti-Glycoprotein E (VZV) Antibody, Human IgG1 (1B10) (Cat. No. VZV-M544) is more than 95% and the molecular weight of this protein is around 135-155 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

Glycoprotein E/gE (VZV) ELISA

Immobilized Varicella zoster virus (strain Oka vaccine) Envelope Glycoprotein E (gE), His Tag (Cat. No. GLE-V52H3) at 1 μg/mL (100 μL/well) can bind Anti-Glycoprotein E (VZV) Antibody, Human IgG1 (1B10) (Cat. No. VZV-M544) with a linear range of 0.1-1 ng/mL (QC tested).

Protocol

Glycoprotein E/gE (VZV) ELISA

Immobilized Varicella zoster virus (strain Oka vaccine) Envelope Glycoprotein E (gE), His Tag (Cat. No. GLE-V52H3) on Anti-Glycoprotein E (VZV) Antibody, Human IgG1 (1B10) (Cat. No. VZV-M544) precoated (0.2 μg/well) plate can bind Biotinylated Monoclonal Anti-Glycoprotein E (VZV) Antibody, Human IgG1 (4G2) (Cat. No. VZV-BLM545)at 0.25 μg/mL (100 μL/well) with a linear range of 0.2-8 ng/mL (Routinely tested).

Protocol

 

活性(Bioactivity)-SPR

Glycoprotein E/gE (VZV) SPR

Anti-Glycoprotein E (VZV) Antibody, Human IgG1 (1B10) (Cat. No. VZV-M544) captured on Protein A Chip can bind Varicella zoster virus (strain Oka vaccine) Envelope Glycoprotein E (gE), His Tag (Cat. No. GLE-V52H3) with an affinity constant of 5.63 nM as determined in SPR assay (Biacore 8K) (Routinely tested).

Protocol

 
评论(2)
  1. 156XXXXXXX8
  2. 0人赞
  3. 抗体特异性强,捕获目的抗原效能优秀,批次间稳定性良好,能够真实可靠的反映抗原蛋白表达效率,对后期实验参数的优化具有明确的指导意义。
  4. >
  5. 2023-11-22
  1. 132XXXXXXX9
  2. 0人赞
  3. 购买该抗体是用于公司相关产品的检测方法开发,检测及相关质量研究工作,在测试中结果稳定,回收率高,抗体值得信赖
  4. >
  5. 2023-8-15
 
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背景(Background)

Varicella-zoster virus (VZV) is a neurotropic virus belonging to the Herpesviridae family. Primary VZV infection causes chickenpox and is followed by a life-long latent infection established mainly in the cranial and dorsal root ganglia. Reactivation of the virus is often associated with shingles (herpes zoster).
Glycoprotein E (gE) is one of the known glycoproteins (gB, gC, gE, gH, gI, gK, gI) of VZV that is most abundantly expressed on the surface of virus and infected cells, playing an important role in viral replication and cell-to-cell spread. The strongly immunogenic gE can provide strong IgG signal in body fluid, which makes it ideal to be developed as an antigen for analysis of IgG antibodies. gE also demonstrates high potency as a vaccine immunogen and is formulated as the single viral envelope protein that constitutes the GSK VZV recombinant subunit vaccine Shingrix®.

 

前沿进展

Optimal injection sites for therapeutic angiogenesis: HGF-mediated regulation of HIF-1α via MAPK/PI3K pathways in hypoxic endothelial cells
Wang, Rong, Li et al
Tissue Cell (2025) 95, 102871
Abstract: Therapeutic angiogenesis offers a promising strategy for patients with critical limb-threatening ischemia (CLTI) who are unsuitable candidates for revascularization. However, the optimal administration sites for gene therapy agents, such as pCK-HGF-X7, remains undefined. Clinical trials commonly employ multiple intramuscular injections at sites of arterial occlusion; yet the necessity and efficacy of such extensive and repetitive protocols remains unclear. Targeted injections into ischemic tissues or their margins may improve therapeutic outcomes. Moreover, the molecular mechanisms by which hepatocyte growth factor (HGF)/c-Met signaling regulates hypoxia-inducible factor-1α (HIF-1α) expression under hypoxic conditions are not fully understood. This study aims to elucidate these molecular mechanisms in endothelial cells under hypoxic conditions and to identify the most effective injection sites for therapeutic angiogenesis agents. The effects of various HGF isoforms/complexes on human aortic endothelial cells (HAECs) were evaluated under normoxic and hypoxic conditions, focusing on proliferation, migration, and tube formation. Pathway inhibitors were used to explore the underlying mechanisms in hypoxic HAECs, and the findings were validated in a rat hindlimb ischemia model. Results demonstrated that HGF723 and HGF728 activated the mitogen-activated protein kinase (MAPK) and phosphatidylinositol 3-kinase (PI3K) pathways, regulating HIF expression and significantly enhanced endothelial cell proliferation, migration, and tube formation, particularly under hypoxia. Despite these cellular effects, HGF treatment did not significantly improve tissue perfusion or neovascularization in normal rat hindlimbs. However, in ischemic rat hindlimbs, it markedly promoted angiogenesis and improved tissue perfusion in the gastrocnemius muscle. These findings indicate that therapeutic angiogenesis agents should primarily target hypoxic tissues, extending to the interface between normoxic and hypoxic regions, to optimize treatment efficacy.Copyright © 2025 Elsevier Ltd. All rights reserved.
Effects of Chlorella protothecoides-derived polydeoxyribonucleotides on skin regeneration and wound healing
Park, Nam, Lee et al
Arch Dermatol Res (2025) 317 (1), 483
Abstract: The skin acts as a crucial barrier and, upon injury, initiates complex wound-healing processes involving various cell types. Polydeoxyribonucleotides (PDRNs) are well-known for their efficacy in enhancing skin regeneration and wound healing. This study sought to investigate the effectiveness of PDRNs derived from Chlorella protothecoides, a sustainable and scalable microalgal source, in promoting skin regeneration and wound healing. Keratinocytes and fibroblasts were used for assessing the impact of PDRNs on cell proliferation, migration, collagen synthesis, and angiogenesis. Gene expression and associated signaling pathways were also examined using RT-qPCR and Western blot analyses. Our findings demonstrated that PDRNs significantly enhanced the proliferation and migration of skin cells, upregulated growth arrest specific 6 (GAS6) and hepatocyte growth factor (HGF) expression, and increased collagen synthesis by modulating collagen type I alpha 1 (COLIA1) expression. Additionally, PDRNs enhanced angiogenesis by promoting vascular endothelial growth factor (VEGF) expression and activation of ERK, AKT, β-catenin and STAT3 pathways via an adenosine A2A receptor (A2AR)-dependent mechanism. These findings suggest that microalgal-derived PDRNs have significant potential as sustainable and effective agents for clinical and cosmetic applications aimed at improving skin health and wound healing.© 2025. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
Genetic insights into avian influenza resistance in Jeju Island chickens: the roles of Mx1 and oligoadenylate synthetase-like single nucleotide polymorphisms
Kim, Jeong, Yang et al
J Anim Sci Technol (2025) 67 (1), 69-85
Abstract: Influenza A virus (FLUAV) causes serious diseases in both poultry and humans. Various host proteins, including Mx1, are considered candidates for avian influenza (AI) resistance. After infecting Jeju Native chicken embryo fibroblasts (CEFs) with three types of AI viruses, we performed gene expression profiling, identified single nucleotide polymorphisms (SNPs) through RNA-sequencing, and confirmed phenotypes showing antiviral activity in vitro. Highly pathogenic AI viruses upregulated FGF2, LYN, and FLT4 and downregulated HGF, ANGPT1, and ROR2, while a low pathogenicity AI upregulated PARK7, RACK1, and DTX3L and downregulated SIRT1, LRRK2, and WAC. However, no virus affected Mx1 expression. Although SNPs in Mx1 could not discriminate antiviral activity alone, the only CEF resistant to H5N6, strain AN4, contained the Mx1 631 R/R genotype and strongly expressed an oligoadenylate synthetase-like (OASL) variant with a unique SNP: c.G880A (p.E294K). Using transfected cell lines, H5N6-infected cells expressing OASL with the c.G880A SNP showed minimal cytopathic effects and the lowest M gene expression. This study confirms that Jeju Native chickens with specific SNP combinations in both Mx1 and OASL showed H5N6 resistance and demonstrates the interplay of genetic factors in host-pathogen dynamics, suggesting a need for integrated analyses of multiple resistance genes to inform AI prevention strategies.© Copyright 2025 Korean Society of Animal Science and Technology.
Super-Resolution Fluorescence Imaging Reveals the Mechanism of NRP1 Clustering on Non-Small-Cell Lung Cancer Membranes
Li, Gao, Qi et al
Anal Chem (2025) 97 (4), 2326-2334
Abstract: Neuropilin 1 (NRP1) is upregulated in various types of malignant tumors, especially non-small-cell lung cancer (NSCLC). However, the precise mechanisms for membrane localization and regulation are not fully understood. Observations from super-resolution microscopy have revealed that NRP1 tends to form nanoscale clusters on the cell membrane, with these clusters varying significantly in size and density across different regions. Further research has shown that stimulation by hepatocyte growth factor (HGF) can reorganize the distribution of NRP1, reducing the number of small clusters while promoting the formation of larger ones. This suggests a propensity for internalization after activation. Additionally, dual-color dSTORM imaging has demonstrated a certain degree of colocalization between NRP1 and c-MET, indicating that c-MET plays an important role in stabilizing NRP1 clusters. This study provides new insights into the mechanism behind NRP1's clustered distribution on cell membranes and paves the way for developing more effective therapeutic strategies targeting NRP1 within tumors.
Showing 1-4 of 810 papers.
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