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 >  Antibody>IgG4 Fc >IG4-MY2180

Monoclonal Anti-Human IgG4 Fc Antibody, Mouse IgG2a (1A10) (MALS verified)

抗体来源(Source)

Monoclonal Anti-Human IgG4 Fc Antibody, Mouse IgG2a (1A10) is a Mouse monoclonal antibody recombinantly expressed from HEK293 cells.

克隆号(Clone)

1A10

种属(Species)

Mouse

亚型(Isotype)

Mouse IgG2a | Mouse Kappa

偶联(Conjugate)

Unconjugated

抗体类型(Antibody Type)

Recombinant Monoclonal

种属反应性(Reactivity)

Human

免疫原(Immunogen)

Recombinant Human IgG4 Fc is expressed from human 293 cells.

特异性(Specificity)

Specifically recognizes IgG4 Fc.

应用(Application)

ApplicationRecommended Usage
ELISA0.5-500 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
 

交叉验证(Cross Verification)

This product No cross-reactivity in ELISA with
UreluMab, Human IgG4.
Monoclonal Anti-Human LAG3 Antibody, Human IgG4 (S108P).
Anti-SARS-CoV-2 Spike RBD Neutralizing Antibody, Human IgG3 (AS35) (Cat. No. SPD-S67).
Monoclonal Anti-IFNγ Antibody, Human IgG1 (8C5F8) (Cat. No. IFN-M412).
Anti-SARS-CoV-2 Spike RBD Broadly Neutralizing Antibody, Human IgG2 (AM359b) (Cat. No. SPD-M400a).
Anti-SARS-CoV-2 Spike RBD Antibody, Chimeric mAb, Human IgA2 (AM130) (Cat. No. SPD-M196b).
Anti-SARS-CoV-2 Spike RBD Antibody, Chimeric mAb, Human IgA1 (AM130) (Cat. No. S1N-M164).
Anti-SARS-CoV-2 Spike RBD Neutralizing Antibody, Chimeric mAb, Cynomolgus IgG1 (AM122) (Cat. No. SPD-M201).
Monoclonal Anti-Eribulin Antibody, Rabbit IgG (1M1G11) (Cat. No. ERN-MY2012b).
Anti-SARS-CoV-2 Spike RBD Neutralizing Antibody, Chimeric mAb, Human IgM (AM122) (Cat. No. SPD-M162).
The antibody does not recognize S108P mutation.
The antibody does not recognize S108P mutation protein.

 

电泳(SDS-PAGE)

IgG4 Fc SDS-PAGE

Monoclonal Anti-Human IgG4 Fc Antibody, Mouse IgG2a (1A10) 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

IgG4 Fc SEC-MALS

The purity of Monoclonal Anti-Human IgG4 Fc Antibody, Mouse IgG2a (1A10) (Cat. No. IG4-MY2180) is more than 90% and the molecular weight of this protein is around 135-165 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

IgG4 Fc ELISA

Immobilized Anti-CD4 Antibody (Ibalizumab-IgG4) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Human IgG4 Fc Antibody, Mouse IgG2a (1A10) (Cat. No. IG4-MY2180) with a linear range of 0.5-31 ng/mL (QC tested).

Protocol

IgG4 Fc ELISA

Immobilized Monoclonal Anti-Human IL-13 Antibody, Human IgG4 at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Human IgG4 Fc Antibody, Mouse IgG2a (1A10) (Cat. No. IG4-MY2180) with a linear range of 2-16 ng/mL (Routinely tested).

Protocol

 
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ACRO质量管理体系
 
 

背景(Background)

Immunoglobulin G4 (IgG4) is a member of many immunoglobulin G developed and secreted by effective B cells. In wake of cutting by pepsin, IgG is divided into two F(ab)s with one antigen binding site and a high conserved Fc segment. The Fc segment bears a highly conserved N-glycosylation site. Ig gamma-4 chain Fc region contains two constant regions of IgG4 H chain (CH2, CH3).

 

前沿进展

Targeting the Neonatal Fc Receptor in Autoimmune Diseases: Pipeline and Progress
Gjølberg, Mester, Calamera et al
BioDrugs (2025)
Abstract: Autoimmune diseases are highly prevalent and affect people at all ages, women more often than men. The most prominent immunological manifestation is the production of antibodies directed against self-antigens. In many cases, these antibodies (Abs) drive the pathogenesis by attacking the body's own healthy cells, causing serious health problems that may be life threatening. Most autoantibodies are of the immunoglobulin G (IgG) isotype, which has a long plasma half-life and potent effector functions. Thus, there is a need for specific treatment options that rapidly eliminate these pathogenic IgG auto-Abs. In this review, we discuss how the neonatal Fc receptor (FcRn) acts as a regulator of the high levels of not only IgG Abs, but also albumin, by rescuing both these soluble proteins from cellular catabolism, and how a molecular and cellular understanding of this complex biology has spurred an intense interest in the development of FcRn-targeting strategies for the treatment of IgG-driven autoimmune diseases. We find that this emerging therapeutic class demonstrates efficacy within several autoimmune diseases with distinct pathophysiology. This offers hope for both new therapeutic avenues for highly prevalent diseases currently treated by other means, and rare diseases with no approved therapies to date. In addition, we elaborate on studies that have led to approval of the first FcRn antagonists, the clinical progress and structural design of molecules in the pipeline, their position in the overall therapeutic landscape of autoimmunity, the design of next-generation antagonists as well as the use of this receptor-targeting principle for other therapeutic applications.© 2025. The Author(s).
IgG Biomarkers in Multiple Sclerosis: Deciphering Their Puzzling Protein A Connection
Apeltsin, Yu
Biomolecules (2025) 15 (3)
Abstract: Identifying reliable biomarkers in peripheral blood is critical for advancing the diagnosis and management of multiple sclerosis (MS), particularly given the invasive nature of cerebrospinal fluid (CSF) sampling. This review explores the role of B cells and immunoglobulins (Igs), particularly IgG and IgM, as biomarkers for MS. B cell oligoclonal bands (OCBs) in the CSF are well-established diagnostic tools, yet peripheral biomarkers remain underdeveloped. Emerging evidence highlights structural and functional variations in immunoglobulin that may correlate with disease activity and progression. A recent novel discovery of blood IgG aggregates in MS patients that fail to bind Protein A reveals promising diagnostic potential and confirms previous findings of the unique features of immunoglobulin G in MS and the potential link between the superantigen Protein A and MS. These aggregates, enriched in IgG1 and IgG3 subclasses, exhibit unique structural properties, including mutations in the framework region 3 (FR3) of IGHV3 genes, and are associated with complement-dependent neuronal apoptosis. Data based on ELISA have demonstrated that IgG aggregates in plasma can distinguish MS patients from healthy controls and other central nervous system (CNS) disorders with high accuracy and differentiate between disease subtypes. This suggests a role for IgG aggregates as non-invasive biomarkers for MS diagnosis and monitoring.
Influence of Distinct Maternal Cytomegalovirus-Specific Neutralizing and Fc Receptor-Binding Responses on Congenital Cytomegalovirus Transmission in HIV-Exposed Neonates
Miller, Mahant, Jenks et al
Viruses (2025) 17 (3)
Abstract: Congenital cytomegalovirus (cCMV) is the most common infectious cause of birth defects worldwide, affecting approximately 1 in every 200 live-born infants globally. Recent work has identified potential immune correlates of protection against cCMV transmission including maternal and placentally transferred antibody levels and their function, which may inform the development of maternal active (vaccine) and passive (mono/polyclonal antibody) immunizations. However, these correlates need to also be assessed in diverse cohorts, including women living with HIV who have increased risk of cCMV transmission. Using a case-control design, we investigated whether the magnitude, specificity, function and placental transfer of maternal IgG responses are associated with protection against and/or risk of cCMV transmission in HIV/HCMV co-infection. Within 3 historical cohorts of pregnant women with HIV/HCMV co-infection, we identified 16 cCMV transmitting cases that were matched to 29 cCMV non-transmitting controls. Using a systems serology approach, we found that normalized HCMV-specific IgG binding to FcγR1α was higher in non-transmitting dyads, whereas HCMV-neutralizing antibody responses were higher in transmitting dyads. These findings suggest that engagement of FcγR1α by HCMV-specific IgG may help confer protection against cCMV transmission. Building upon previous research, our study reinforces the critical role of validating maternal humoral immune correlates of cCMV transmission risk across diverse seropositive cohorts, providing essential insights to inform and accelerate the development of effective HCMV vaccines.
Plant-derived recombinant macromolecular PAP-IgG Fc as a novel prostate cancer vaccine candidate eliciting robust immune responses
Kang, Kim, Hwang et al
Transgenic Res (2025) 34 (1), 16
Abstract: Prostatic acid phosphatase (PAP) is a specific protein that is highly expressed in prostate cancer. In this study, we constructed two recombinant PAP fusion genes: PAP fused to the immunoglobulin G (IgG) Fc fragment (designated PAP-Fc) and PAP-Fc fused to the endoplasmic reticulum retention sequence KDEL (designated PAP-FcK). Transgenic Nicotiana tabacum plants expressing these recombinant macromolecular proteins (MPs) were generated using Agrobacterium-mediated transformation, and the presence of both genes was confirmed through genomic PCR. Western blot analysis validated the expression of PAP-Fc and PAP-FcK MPs, which were successfully purified via protein A affinity chromatography. Size-exclusion high-performance liquid chromatography revealed dimeric peaks for PAP-Fc (PAP-FcP) and PAP-FcK (PAP-FcKP). Bio-transmission electron microscopy demonstrated 'Y'-shaped protein particles resembling antibody structures. Moreover, PAP-FcP and PAP-FcKP exhibited a high association rate with human FcγR and FcRn. Vaccination of mice with both PAP-FcP and PAP-FcKP resulted in increased total IgG against PAP and enhanced activation of CD4+ T cells, comparable to mice immunized with PAP, which served as a positive control. These findings indicate that both plant-derived MPs can effectively induce adaptive immunity, positioning them as promising candidates for prostate cancer vaccines. Overall, plants expressing PAP-Fc and PAP-FcK represent a viable production system for antigenic macromolecule-based prostate cancer vaccines.© 2025. The Author(s), under exclusive licence to Springer Nature Switzerland AG.
Showing 1-4 of 10939 papers.
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