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 >  Protein>IgG3 Fc >IG3-M5214

Mouse IgG3 Fc Protein, Tag Free (MALS verified)

分子别名(Synonym)

Ig gamma-3 chain C region,IgG,IgG3

表达区间及表达系统(Source)

Mouse IgG3 Fc Protein, Tag Free (IG3-M5214) is expressed from human 293 cells (HEK293). It contains AA Pro 98 - Pro 327 (Accession # P03987-2).

Request for sequence

蛋白结构(Molecular Characterization)

IgG3 Fc Structure

This protein carries no "tag".

The protein has a calculated MW of 26.1 kDa. The protein migrates as 30-33 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>90% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 100 mM Glycine, 25 mM Arginine, 150 mM NaCl, pH7.5 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)

IgG3 Fc SDS-PAGE

Mouse IgG3 Fc Protein, Tag Free 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

IgG3 Fc SEC-MALS

The purity of Mouse IgG3 Fc Protein, Tag Free (Cat. No. IG3-M5214) is more than 90% and the molecular weight of this protein is around 60-70 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

IgG3 Fc ELISA

Immobilized Mouse IgG3 Fc Protein, Tag Free (Cat. No. IG3-M5214) at 5 μg/mL (100 μL/well) can bind Biotinylated Human CD64, His,Avitag (Cat. No. FCA-H82E8) with a linear range of 0.6-10 ng/mL (QC tested).

Protocol

 
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背景(Background)

Immunoglobulin G3 (IgG3) 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-3 chain C region (IgG3-Fc / IGHG3) contains two constant regions of IgG3 H chain (CH2, CH3).

 

前沿进展

Role of Antibody Glycosylation in Health, Disease, and Therapy
Nimmerjahn
Handb Exp Pharmacol (2025)
Abstract: Immunoglobulin G (IgG) antibodies are an essential component of humoral immunity protecting the host from recurrent infections. Among all antibody isotypes, IgG antibodies have a uniquely long half-life, can basically reach any tissue in the body, and have the ability to kill opsonized target cells, which has made them the molecule of choice for therapeutic interventions in cancer and autoimmunity. Moreover, IgG antibodies in the form of pooled serum IgG preparations from healthy donors are used to treat chronic inflammatory and autoimmune diseases, providing evidence that serum IgG antibodies can have an active immunomodulatory activity. Research over the last two decades has established that the single sugar moiety attached to each IgG heavy chain plays a very important role in modulating the pro- and anti-inflammatory activities of IgG. Moreover, specific sugar moieties such as sialic acid and galactose residues can serve as highly specific biomarkers for ongoing inflammatory processes. This chapter will summarize how different sugar residues in the IgG sugar moiety change upon inflammation and how such changes may translate to altered IgG function and hence maybe useful for optimizing or modulating the function of therapeutic antibodies.© 2025. The Author(s), under exclusive license to Springer Nature Switzerland AG.
Novel, fully human, anti-PfCSP antibodies with potent antimalarial activity using a phage display based strategy
Parveen, Rath, Tabrez et al
Vaccine (2025) 54, 126993
Abstract: Developing an effective vaccine against malaria remains a prime goal of human health. The circumsporozoite protein (CSP) is a major surface protein of the sporozoites, and is the target of two licensed Plasmodium falciparum malaria vaccines, RTS,S/AS01, named Mosquirix and R21/Matrix-M. However, to improve the standards set by these vaccines we require a second-generation or prophylactic vaccine. Recently, monoclonal antibodies have emerged as essential biopharmaceutical prophylactic vaccines. The present study targeted recombinant Plasmodium falciparum CSP (rPfCSP) with a phage display of human single-fold scFv Tomlinson libraries I+J and picked fourteen scFvs that represented two independent clones after sequencing; CL1 and CL3. These phages were analysed for their binding to rPfCSP. The selected scFvs were cloned in a human IgG1 Fc tag vector, to generate scFv-Fc full-length antibody clones. CL1 bound rPfCSP protein with a KD of 3.8x10-6M and CL3 bound rPfCSP protein with a KD of 5.6 x 10-5 M. These antibodies detected native PfCSP on the sporozoite surface. Molecular docking simulation revealed that rPfCSP residues interacting with CL1 and CL3 were downstream of the repeat region. These antibodies inhibited the sporozoite infectivity into HepG2 cells, similar to a gold standard monoclonal antibody, 2A10. Low-dose passive transfer of the CL1 and CL3 antibodies conferred high-level protection when challenged with PfCSP-Pb transgenic parasites in the mouse infection model. The high in vitro and in vivo efficacies of the CL1 and CL3 antibodies have applications in malaria immunoprophylaxis in protecting travellers and military servicemen or as a therapeutic vaccine in malaria elimination programmes.Copyright © 2025 The Authors. Published by Elsevier Ltd.. All rights reserved.
Recovery of Antibody Immunity After a Resurgence of Respiratory Syncytial Virus Infections
Reicherz, Viñeta Paramo, Bone et al
J Infect Dis (2025)
Abstract: Longitudinal measurements of respiratory syncytial virus (RSV) immunity over 4 winter seasons reveal that viral neutralization titers, RSV prefusion F protein (pre-F)-specific immunoglobulin M and immunoglobulin G (IgG) levels, and RSV antibody-dependent cellular phagocytosis function gradually returned to prepandemic levels in female healthcare and school workers of childbearing age after 2 winter seasons, following the resurgence of RSV cases in the Vancouver metropolitan region (British Columbia, Canada). In contrast, pre-F IgG avidity profiles remained unchanged. These findings support the notion that repeated viral infections are necessary to maintain high RSV antibody levels in the population.© The Author(s) 2025. Published by Oxford University Press on behalf of Infectious Diseases Society of America.
An Enhanced Bimetallic Optical Fiber SPR Biosensor Using Graphene Oxide for the Label-Free and Sensitive Detection of Human IgG
Xu, Yin, Cui et al
Sensors (Basel) (2025) 25 (5)
Abstract: A fiber-reinforced SPR sensor based on silver-nucleated gold-shell bimetallic nanoparticles and graphene oxide was developed and applied to human IgG detection. The refractive index (RI) sensitivity of the Ag@Au/GO fiber SPR sensor is as high as 4715.9 nm/RIU in the RI range of 1.333-1.365. Staphylococcus aureus protein A (SPA) can specifically recognize and bind to the fragment crystallizable (Fc) of the antibody; it facilitates the highly targeted immobilization of the antibody. SPA and rabbit anti-human IgG were immobilized on the surface of the Ag@Au/GO fiber SPR sensor for the detection of different concentrations of human IgG with a sensitivity of 0.53 nm/μg/mL and detection limits of 0.037 μg/mL. This biosensor based on the mixed structure of GO and Ag@Au combined the common advantages of the two materials. Therefore, our study provides a simple platform for biological analysis and has a good application prospect.
Showing 1-4 of 10940 papers.
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IgG3 Fc靶点信息
英文全称:Immunoglobulin G
中文全称:免疫球蛋白G
种类:Homo sapiens
上市药物数量:1详情
临床药物数量:5详情
最高研发阶段:批准上市
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