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immunoglobulin G

✓ Approved

Quimbiotec · Polyclonal Antibodies · Polyclonal Antibodies

What is immunoglobulin G?

immunoglobulin G is a polyclonal antibodies developed by Quimbiotec. It is approved for therapeutic indications via injectable (others) or intravenous (iv).

Drug Profile

CompanyQuimbiotec
Drug ClassPolyclonal Antibodies, Antibody
RouteInjectable (Others), Intravenous (IV)
StatusApproved
Sources: ClinicalTrials.gov, Quimbiotec

Therapeutic Indications

immunoglobulin G is developed for 4 unique indications across 4 therapeutic areas.

Therapeutic AreaConditionPhase
Nervous system disordersGuillain-Barre syndrome✓ Approved
Skin and subcutaneous tissue disordersPurpura✓ Approved
Immune system disordersImmunodeficiency✓ Approved
Infections and infestationsBorna virus infection✓ Approved

Related Research Articles

PubMed[Rinsho ketsueki] The Japanese journal of clinical hematology2026-08-30

[Intrathecal immunoglobulin administration for refractory viral central nervous system infection after allogeneic hematopoietic stem cell transplantation].

Matsuo Masaaki M, Kusakabe Shinsuke S, Kurashige Ryumei R, Fukushima Kentaro K et al.

Central nervous system (CNS) viral infections after allogeneic hematopoietic stem cell transplantation are associated with poor prognosis and have limited therapeutic options. We report three cases of refractory CNS viral infection treated by combination therapy with antiviral agents and intrathecal immunoglobulin administration. Case 1 involved cytomegalovirus encephalitis, Case 2 varicella zoster virus meningitis, and Case 3 human herpesvirus 6 encephalitis; all were resistant to antiviral agents. Two patients achieved viral DNA negativity in cerebrospinal fluid, and none experienced adverse events related to intrathecal injection. Although no intrathecal immunoglobulin products have been approved for use in Japan, our findings suggest that this treatment may be a viable option in selected refractory cases. Further studies are warranted to clarify the optimal agent, dosage, and schedule.

PMID 42669504
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PubMedFood chemistry: X2026-08-30

Proteomic insights into goat milk serum proteins at varying altitudes in China.

Li Zhaomin Z, Wang Shanshan S, Cao Hanwen H, Yan Yingying Y et al.

Using Astral DIA quantitative proteomics, this study characterized serum protein profiles and potential functions of goat milk from different altitude regions. A total of 1446 proteins were identified, with 1268, 1256, and 1346 proteins detected in high-altitude, mid-altitude, and low-altitude samples, respectively. The high-altitude sample contained 34 unique proteins and showed higher abundances of α-lactalbumin, serum albumin, and polymeric immunoglobulin receptor, whereas the low-altitude sample contained 87 unique proteins and higher abundances of several immune-related proteins, including osteopontin, lactoferrin, immunoglobulin, lysozyme, xanthine oxidase, lactoperoxidase, and GLYCAM1. Differentially expressed analysis identified 453, 452, and 113 differential proteins in high-altitude vs. low-altitude, mid-altitude vs. low-altitude, and high-altitude vs. mid-altitude comparisons, respectively. KEGG analysis showed that carbohydrate metabolism was enriched in comparisons involving the low-altitude sample, whereas amino acid metabolism was enriched between high-altitude and mid-altitude samples. Notably, HIF-1 signaling pathway was enriched in the high-altitude sample, suggesting hypoxia-associated proteomic adaptation.

PMID 42668543
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PubMedFood & function2026-08-30

Abelmoschus manihot (L.) leaf flavonoids (AMLF) restore cyclophosphamide-induced immunosuppression in mice via gut microbiota and serum metabolomics modulation.

Yang Shengnan S, Jin Jiahui J, Zhao Dou D, Cai Mengquan M et al.

Immune homeostasis serves as the foundation for disease prevention and the cornerstone for ensuring human health. The effects of Abelmoschus manihot (L.) leaf flavonoids (AMLF) on restoring immune function were investigated in a cyclophosphamide (CTX)-induced immunosuppressed mouse model. The underlying repair mechanisms were explored by an integrative analysis of intestinal microbiomics and serum metabolomics. The results demonstrated that AMLF markedly elevated the spleen and thymus indices, promoted the proliferation of splenic lymphocytes in the presence of concanavalin A (ConA) or lipopolysaccharide (LPS) and CD4+ and CD8+ T lymphocyte subsets, and concomitantly enhanced the serum levels of key immunomodulatory cytokines, including interleukin-1β (IL-1β), interleukin-2 (IL-2), and tumor necrosis factor-α (TNF-α), and the antibody immunoglobulin G (IgG). In addition, AMLF treatment effectively mitigated CTX-induced histopathological injuries to immune organs and the colon. AMLF were also found to protect the liver by regulating antioxidant enzyme activities. Furthermore, AMLF markedly improved the intestinal microbial community structure, promoted the enrichment of beneficial bacteria (Lactobacillaceae and Prevotellaceae), inhibited pathogenic bacteria (Muribaculaceae and Desulfovibrionaceae), and increased the content of short-chain fatty acids (SCFAs). Serum metabolomic analysis showed that AMLF upregulated the levels of leukotrienes, S-(PGA1)-glutathione and prostaglandin E2. Correlation analysis identified g_Alistipes, g_norank_f_Muribaculaceae, and g_Kurthia as potential microbiota strongly associated with the restoration of immune and metabolic homeostasis after AMLF treatment. These findings support the dual potential of AMLF in functional foods and as immunomodulatory adjuvants.

PMID 42669286
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PubMedProgress in nuclear magnetic resonance spectroscopy2026-08-30

NMR structure study of DNA G-quadruplexes and ligand complexes.

Dickerhoff Jonathan J, Yang Danzhou D

G-quadruplexes (G4s) have emerged as one of the most exciting nucleic acid secondary structures. G-quadruplexes are non-canonical, four-stranded nucleic acid structures formed in sequences with consecutive runs of guanine bases. Unlike duplex DNA, G-quadruplexes are globularly folded structures and can readily form under physiologically relevant solution conditions. G-quadruplex structures have been found in biologically significant nucleic acid regions, including human telomeres, oncogene-promoter regions, replication initiation sites, and untranslated regions (UTRs) of mRNA. They have been shown to be important regulatory motifs in a number of critical cellular processes including gene transcription, translation, DNA replication, and genomic stability. G-quadruplexes have become a new class of molecular targets for drug development. Nuclear magnetic resonance (NMR) spectroscopy is the major method for studying the structures of G-quadruplexes under physiologically relevant solution conditions. NMR spectroscopy is a powerful tool for studying G-quadruplex interactions with small molecule ligands in solution. To date, most G-quadruplex structures have been determined using NMR techniques. This review provides a comprehensive overview of the NMR methods used to determine DNA G-quadruplex structures and their ligand interactions in solution. It covers essential steps such as resonance assignment, which is foundational for all NMR studies, as well as the determination of G-quadruplex folding topology and structure using NMR spectroscopy. Additionally, it discusses NMR structural studies of small molecule interactions with DNA G-quadruplexes. Through examples of NMR-based structure characterization of G-quadruplexes and G-quadruplex-ligand complexes, this review illustrates the rich information that NMR spectroscopy can provide, demonstrating its applicability to a broad range of biologically relevant DNA G-quadruplexes and their ligand interactions.

PMID 42669457
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PubMedJournal of microbiological methods2026-08-30

Development of an A7G variant of recombinant human G-CSF for improved fibroblast-mediated wound healing.

Thota Sujani S, Myneni Praveen P, Venkateswarulu T C TC

Recombinant human granulocyte colony-stimulating factor (rh-G-CSF) is useful in tissue regeneration due to its angiogenic and anti-inflammatory actions. The current study focused on the downstream process of A7G mutant rh-G-CSF (m-rh-G-CSF) and the effects of m-rh-G-CSF on human fibroblasts. The m-rh-G-CSF was purified and had 97.24% purity, a final protein concentration of 0.814 g/L and a molecular weight of 18,784 Da. The addition of m-rh-G-CSF significantly elevated the ATP level in the treated cells in a concentration-dependent manner. The maximal ATP level was achieved at a concentration of 2.5 μg/mL and was 89% higher than in the control cells and 13% higher than in reference rh-G-CSF. In the scratch-wound assay, 92.67% and 98.69% wound closure were observed at 24 and 48 h after the addition of m-rh-G-CSF, respectively, compared with 49.93% in control cells at 48 h. These findings support the potential of m-rh-G-CSF as a therapeutic candidate for fibroblast-mediated wound healing.

PMID 42669396
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PubMedFood chemistry: X2026-08-30

Dual-mode screening system for rapid and accurate aflatoxin B1 detection in edible oils.

Ying Guangyao G, Wang Tingting T, Li Kunlun K, Lu Zheng Z et al.

This study established a dual-mode system integrating a portable flow cytometer with UHPLC-QqQ MS/MS for rapid AFB1 detection in edible oils. A competitive immunofluorescence sensor used streptavidin-magnetic microspheres with biotin-AFB1-BSA, AFB1 antibody, and APC-labeled secondary antibody. The method showed a linear range of 0.025-25 ng/g (R2 = 0.9966), with IC10 of 0.26 ng/g and IC50 of 0.76 ng/g. Recoveries were 90.51-102.73% with precisions ≤9.54%. UHPLC-QqQ MS/MS achieved LODs of 0.20-0.40 ng/g and LOQs of 0.50-1.25 ng/g for AFB1, AFB2, AFG1, and AFG2, with recoveries of 88.99-107.12% and precisions of 1.09-10.58%. Validation with 29 commercial oils and 10 contaminated peanut batches found no AFB1 in market samples and 1.07-9.36 ng/g in contaminated ones, consistent with UHPLC-QqQ MS/MS. The system enables on-site high-throughput screening with a flow cytometric reading speed of approximately 1 min per sample and a batch throughput of ∼32 samples/h (96-well plate format), while maintaining laboratory-grade accuracy. By enabling efficient triage of large sample volumes at the point of sampling, this strategy provides a practical and cost-effective framework for strengthening aflatoxin surveillance in the edible oil supply chain.

PMID 42668490
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