登录 | 注册    关注公众号  
微信公众号
搜索
 >  Protein>IgG1 Fc >IG1-H52C9

Human IgG1 Fc (C103S) Protein, Flag Tag (MALS verified)

分子别名(Synonym)

IgG1

表达区间及表达系统(Source)

Human IgG1 Fc (C103S), Flag Tag (IG1-H52C9) is expressed from human 293 cells (HEK293). It contains AA Pro 100 - Lys 330 (Accession # P01857-1(C103S)).

Predicted N-terminus: Pro 100

Request for sequence

蛋白结构(Molecular Characterization)

Online(Pro 100 - Lys 330) P01857-1 (C103S)

This protein carries a flag tag at the C-terminus.

The protein has a calculated MW of 27.1 kDa. The protein migrates as 28-33 kDa 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)

>95% as determined by SDS-PAGE.

>95% as determined by SEC-MALS.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in Tris with Glycine, Arginine and NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.

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)

Human IgG1 Fc (C103S), Flag Tag (Cat. No. IG1-H52C9) SDS-PAGE gel

Human IgG1 Fc (C103S), Flag Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

SEC-MALS

Human IgG1 Fc (C103S), Flag Tag (Cat. No. IG1-H52C9) MALS images

The purity of Human IgG1 Fc (C103S), Flag Tag (Cat. No. IG1-H52C9) is more than 95% and the molecular weight of this protein is around 51-63 kDa verified by SEC-MALS.

Report

 
评论(0)
 
ACRO质量管理体系
 
 

背景(Background)

Crystallizable fragments composed of the carboxy-terminal halves of both IMMUNOGLOBULIN HEAVY CHAINS linked to each other by disulfide bonds. Fc fragments contain the carboxy-terminal parts of the heavy chain constant regions that are responsible for the effector functions of an immunoglobulin (COMPLEMENT fixation, binding to the cell membrane via FC RECEPTORS, and placental transport). IgG1 Fc was reported has a novel role as a potential anti-inflammatory drug for treatment of human autoimmune diseases.

 

 

前沿进展

Enhancing activity of FcαRI-bispecific antibodies using glycoengineering
Sewnath, Damelang, Bentlage et al
J Immunol (2025)
Abstract: Macrophages and natural killer (NK) cells can effectively kill tumor cells in the presence of anti-cancer IgG monoclonal antibodies (mAbs), but neutrophils are less effective. We previously showed that IgG1 bispecific antibodies (BsAb), which target the IgA Fc receptor (FcαRI, CD89) and a tumor associated antigen induce effective neutrophil recruitment and tumor cell killing in vivo. Here we investigated if the efficacy of an anti-EGFR (CetuximAb)/FcαRI-bispecific antibody could be further improved by implementing glycoengineering of the IgG-Fc, aimed at increasing FcγRIIIa/b binding and/or complement activity. Fc afucosylation was introduced to enhance antibody-dependent cellular cytotoxicity (ADCC) by FcγRIIIa on NK/macrophages, which can also reduce neutrophil-mediated ADCC through their GPI-linked FcγRIIIb. Fc galactylation was found to enhance antibody hexamerization and thereby complement dependent cytotoxicity (CDC). Low fucosylated BsAbs moderately increased NK cell-mediated tumor cell killing, but did not affect neutrophil-mediated tumor cell killing nor phagocytosis by macrophages. Glycoengineering of these EGFR-specific BsAb, which normally are devoid of CDC-activity, did not enable their complement activities. In conclusion, glycoengineered FcαRI BsAbs increased ADCC by NK cells but had little effect on neutrophil or macrophage mediated tumor killing.© The Author(s) 2025. Published by Oxford University Press on behalf of The American Association of Immunologists.
An engineered antibody-lectin conjugate targeting the HIV glycan shield protects humanized mice against HIV challenge
Kumariya, Sun, Lusvarghi et al
Mol Ther (2025)
Abstract: Enveloped viruses responsible for global health pandemics often display a glycan shield on their surface envelope glycoproteins. In HIV, the glycan shield is formed by clusters of high-mannose glycans and plays essential roles in viral fitness and immune evasion. A few mannose-binding lectins potently inactivate HIV but have not been fully exploited due to poor pharmacokinetics and short serum half-lives. To address this, we engineered an antibody-lectin conjugate comprising the anti-HIV lectin griffithsin (GRFT) to the Fc region of human IgG1, with the aim of extending its serum half-life and augmenting anti-HIV activity by inducing immune effector responses. Engineered mGRFT-Fc produced in bacteria exhibited picomolar anti-HIV activity and an extended serum half-life, and mGRFT-Fc produced in mammalian cells (mGRFT-Fcglyc) elicited immune effector responses. In HIV-infected CD34+-humanized mice, both GRFT and mGRFT-Fcglyc effectively suppressed viral loads for up to 8 weeks after a single dose. Significantly, mGRFT-Fcglyc prevented HIV infection by neutralizing HIV and provided sustained protection from break through infections via Fc-mediated immune effector responses, exhibiting a dual mode of protection. This study demonstrates the successful engineering of a lectin-based biologic and provides early evidence that a glycan-targeting agent alone can confer protection from viral infection in vivo.Published by Elsevier Inc.
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.
Rapid In Vivo Screening of Monoclonal Antibody Cocktails Using Hydrodynamic Delivery of DNA-Encoded Modified Antibodies
Fausther-Bovendo, Babuadze, Ivanciuc et al
Biomedicines (2025) 13 (3)
Abstract: Background: Monoclonal antibodies (mAbs) are potent treatment options for infectious diseases. The rapid isolation and in vivo validation of therapeutic mAb candidates, including mAb cocktails, are essential to combat novel or rapidly mutating pathogens. The rapid selection and production of mAb candidates in sufficient amount and quality for preclinical studies are a major limiting step in the mAb development pipeline. Methods: Here, we developed a method to facilitate the screening of therapeutic mAbs in mouse models. Four conventional mAbs were transformed into single-chain variable fragments fused to the fragment crystallizable (Fc) region of a human IgG1 (scFv-IgG). These scFv-IgG were expressed individually or as a cocktail in vitro and in mice following transfection or hydrodynamic delivery of the corresponding plasmids. Results: This method induced high expression of all scFv-IgG and provided protection in two murine infection models. Conclusions: This study highlights the benefits of this approach for the rapid, low-cost screening of therapeutic mAb candidates.
Showing 1-4 of 12155 papers.
Powered by BizGenius
 
 
货号/价格
文档
联系电话:
+86 400-682-2521(全国)
010-53681107(北京)
021-50850665(上海)
运输方式
订单邮箱:
order.cn@acrobiosystems.com
技术支持邮箱:
tech.cn@acrobiosystems.com
前沿进展
点击查看详细

消息提示

请输入您的联系方式,再点击提交!

确定