Human Fibrinogen Like Protein 1 ELISA , FGL1
- Known as:
- Human Fibrinogen Like Protein 1 Enzyme-linked immunosorbent assay test , FGL1
- Catalog number:
- E01F0080
- Product Quantity:
- 96 Tests/kit
- Category:
- -
- Supplier:
- BGene
- Gene target:
- Human Fibrinogen Like Protein 1 ELISA FGL1
Related genes to: Human Fibrinogen Like Protein 1 ELISA , FGL1
- Gene:
- FGL1 NIH gene
- Name:
- fibrinogen like 1
- Previous symbol:
- -
- Synonyms:
- HFREP-1
- Chromosome:
- 8p22
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-25
- Date modifiied:
- 2015-11-09
Related products to: Human Fibrinogen Like Protein 1 ELISA , FGL1
Related articles to: Human Fibrinogen Like Protein 1 ELISA , FGL1
- Ubiquitin-specific protease 7 (USP7) is a multifunctional deubiquitinase that has emerged as an important regulator of cancer progression, with growing evidence linking it to tumor immune evasion, metabolic adaptation, and therapeutic resistance. USP7 promotes immune suppression by stabilizing checkpoint molecules such as PD-L1, modulating FGL1/LAG-3 signaling, reshaping tumor-associated macrophage polarization, and reinforcing T-cell dysfunction. Simultaneously, USP7 regulates metabolic adaptation by maintaining lipid homeostasis, redox balance, ferroptotic resistance, and nutrient stress responses, thereby supporting tumor survival under adverse conditions. These intertwined immune and metabolic functions collectively contribute to resistance against immune checkpoint blockade, targeted therapy, and other anticancer interventions. Pharmacological inhibition of USP7 has shown promise in reprogramming the tumor microenvironment, exposing metabolic vulnerabilities, and sensitizing tumors to combination therapies. This review summarizes current insights into USP7 structure and substrate networks, highlights its multifaceted roles in tumor immunity and metabolism, and discusses the therapeutic potential and translational challenges of targeting USP7 in cancer. - Source: PubMed
Publication date: 2026/05/20
Liu XiaolinZhu Bo ChiLian Li LiLi Yun Feng - Lymphocyte activation gene-3 (LAG-3) is a pivotal immune checkpoint receptor that exerts a negative regulatory effect on T-cell function. Although LAG-3-blocking antibodies have shown promising clinical potential, the inherent limitations of conventional monoclonal antibodies necessitate the development of novel antibody formats with enhanced biological and pharmacological properties. In this study, a panel of single-domain antibodies (sdAbs) targeting human LAG-3 was generated via phage display technology. Among these candidates, 2H-G7 was identified as a high-affinity sdAb that binds to LAG-3 with an equilibrium dissociation constant (K) in the nanomolar range. Notably, 2H-G7 potently blocks the interactions of LAG-3 with both of its key ligands, fibrinogen-like protein 1 (FGL1) and major histocompatibility complex class II (MHC-II). Its capacity to restore impaired T-cell function was validated by quantifying interleukin-2 (IL-2) secretion and CD69 expression in stimulated primary human peripheral blood mononuclear cells (PBMCs). Epitope mapping studies localized the binding site of 2H-G7 to the D1D2 extracellular domains of LAG-3, distinct from relatlimab, a clinically approved LAG-3-blocking antibody serving as the benchmark. In a xenogeneic mouse model of non-small-cell lung cancer (NSCLC), 2H-G7-Fc exhibited superior tumor growth inhibition efficacy compared with relatlimab. These findings demonstrate that 2H-G7 is a promising lead candidate for the development of next-generation LAG-3-targeted tumor immunotherapies. - Source: PubMed
Publication date: 2026/05/04
Dong MengfeiLi WenjieWang TailinLi MingZhang JingyiLiu Xianglei - The role of fibrinogen-like protein 1 (FGL1) in the immune microenvironment in bladder cancer has been extensively studied, but the specific regulatory pathways require further investigation. - Source: PubMed
Publication date: 2026/04/09
Hu KeyaoLuo LeiLi PengWang XiaofeiSun Lijiang - The immune checkpoint lymphocyte activation gene-3 (LAG-3) interacts with major histocompatibility complex class II and fibrinogen-like protein 1 (FGL-1) to suppress T cell activity, contributing to resistance against immunotherapies such as programmed death-ligand 1 (PD-L1) blockade. This study aimed to identify LAG-3-binding peptides capable of disrupting these immunosuppressive interactions. Using a phage-displayed peptide library, we identified 2 candidate peptides, LAG3pep-1 and LAG3pep-2, that preferentially bound to LAG-3-expressing cells and recombinant LAG-3 protein. A LAG-3 D1 domain-blocking antibody competitively inhibited the peptide binding to LAG-3-expressing cells, confirming target specificity. Among the 2 peptides, LAG3pep-2 demonstrated higher binding affinity and greater stability toward LAG-3. These findings were further supported by structural modeling and all-atom simulation of the LAG-3 and peptide complexes and in silico mutational analysis. Functionally, LAG3pep-2 restored interleukin-2 secretion in T cells suppressed by tumor-derived FGL-1 more effectively than LAG3pep-1. Furthermore, LAG3pep-2 synergized with a PD-L1-blocking antibody to rescue T cell cytotoxicity and cytokine production in tumor cell co-culture assays. In vivo, systemic administration of LAG3pep-2 in combination with PD-L1 blockade significantly suppressed syngeneic tumor growth, enhanced anti-tumor immunity, and exhibited no observable systemic toxicity, outperforming either monotherapy. Collectively, these findings identify LAG3pep-2 as a peptide inhibitor of LAG-3 interaction with FGL-1 and a promising combinatorial agent to potentiate PD-L1-targeted cancer immunotherapies. - Source: PubMed
Publication date: 2026/05/14
Lee Seok-MinGurung SmritiPark Min-SungVadevoo Sri Murugan PoongkavithaiGunassekaran Gowri RangaswamyKim Min-JongKim Sang-HyunKim Ha-JeongPark Eun JungLee SangminIm WonpilKim SoyounLee Byungheon - Amphibians face threats from emerging bacterial, viral, and fungal pathogens, and their innate immune response plays a key role in early defense. The liver is a central immune organ that produces acute-phase proteins (APPs) and complement system proteins, which are essential for early pathogen neutralization and a positive disease outcome. Here, we investigated the temporal dynamics of hepatic gene expression for APPs [C-reactive protein (CRP), serum amyloid A (SAA), fibrinogen-like protein 1 (FGL1)] and complement components (C1s, C3, C4, C5, C9) in Rhinella diptycha toads injected with lipopolysaccharide (LPS) or saline. Using RT-qPCR at four time points post-injection (1h, 3h, 6h, and 18h), we detected a significant effect of LPS on C1s expression and a treatment × time interaction for C4, C5, and C9, indicating time-dependent activation of different complement proteins. In contrast, we found no evidence for LPS-induced changes in APPs expression. However, several APPs were positively correlated with complement components, suggesting coordinated regulation even in the absence of differential expression. Our findings provide a temporal analysis of hepatic acute-phase responses to LPS in Rhinella diptycha toads, unraveling a complex network of complement system activation. By showing that complement components, rather than APPs, dominate the early hepatic response to a bacterial antigen in a widespread Neotropical toad species, our study provides a temporal and mechanistic baseline for future investigations of amphibian innate immunity and underscores the need for future work to determine how these early pathways respond to different pathogens and contribute to variation in disease outcomes among amphibians. - Source: PubMed
Publication date: 2026/05/07
Zenga-Carrenho MarinaTiton BrazTiton Stefanny Christie Monteirode Assis Vania ReginaGomes Fernando RibeiroFloreste Felipe Rangel