InVivoMAb human IgG1 isotype control
Product Description
Specifications
| Isotype | Human IgG1 |
|---|---|
| Recommended Dilution Buffer | InVivoPure pH 7.0 Dilution Buffer |
| Conjugation | This product is unconjugated. Conjugation is available via our Antibody Conjugation Services. |
| Formulation |
PBS, pH 7.0 Contains no stabilizers or preservatives |
| Endotoxin |
≤1EU/mg (≤0.001EU/μg) Determined by LAL assay |
| Purity |
≥95% Determined by SDS-PAGE |
| Sterility | 0.2 µm filtration |
| Production | Purified from human myeloma serum |
| Purification | Protein A |
| RRID | AB_2687817 |
| Molecular Weight | 150 kDa |
| Human Pathogen Test Results |
Hepatitis B Surface Antigen: Negative Human Immunodeficiency Virus 1 antibodies: Negative Human Immunodeficiency Virus 2 antibodies: Negative Hepatitis C Virus antibodies: Negative * These tests cannot guarantee the absence of infective agents |
| Storage | The antibody solution should be stored at the stock concentration at 4°C. Do not freeze. |
| Need a Custom Formulation? | See All Antibody Customization Options |
Application References
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Li, M., et al (2019). "Genomic ERBB2/ERBB3 mutations promote PD-L1-mediated immune escape in gallbladder cancer: a whole-exome sequencing analysis" Gut 68(6): 1024-1033.
PubMed
OBJECTIVES: Patients with gallbladder carcinoma (GBC) lack effective treatment methods largely due to the inadequacy of both molecular characterisation and potential therapeutic targets. We previously uncovered a spectrum of genomic alterations and identified recurrent mutations in the ErbB pathway in GBC. Here, we aimed to study recurrent mutations of genes and pathways in a larger cohort of patients with GBC and investigate the potential mechanisms and clinical significance of these mutations. DESIGN: We performed whole-exome sequencing (WES) in 157 patients with GBC. Functional experiments were applied in GBC cell lines to explore the oncogenic roles of ERBB2/ERBB3 hotspot mutations, their correlation with PD-L1 expression and the underlying mechanisms. ERBB inhibitors and a PD-L1 blocker were used to evaluate the anticancer activities in co-culture systems in vitro and in vivo. RESULTS: WES identified ERBB2 and ERBB3 mutations at a frequency of 7%-8% in the expanded cohort, and patients with ERBB2/ERBB3 mutations exhibited poorer prognoses. A set of in vitro and in vivo experiments revealed increased proliferation/migration on ERBB2/ERBB3 mutation. Ectopic expression of ERBB2/ERBB3 mutants upregulated PD-L1 expression in GBC cells, effectively suppressed normal T-cell-mediated cytotoxicity in vitro through activation of the PI3K/Akt signalling pathway and contributed to the growth and progression of GBC in vivo. Treatment with an ERBB2/ERBB3 inhibitor or a PD-L1 monoclonal antibody reversed these immunosuppressive effects, and combined therapy revealed promising therapeutic activities. CONCLUSIONS: ERBB2/ERBB3 mutations may serve as useful biomarkers in identifying patients who are sensitive to ERBB2/ERBB3 inhibitors and PD-L1 monoclonal antibody treatment. TRIAL REGISTRATION NUMBER: NCT02442414;Pre-results.
Product Citations
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DF6215, an α-optimized IL-2-Fc fusion, expands immune effectors and drives robust preclinical anti-tumor activity.
In Cell Rep Med on 20 January 2026 by Stockmann, A. P., Vincent, S., et al.
PubMed
DF6215 is a rationally engineered interleukin-2 (IL-2) Fc-fusion protein developed to overcome efficacy and safety limitations of traditional IL-2 cancer immunotherapy. Unlike non-alpha (non-α) IL-2 variants that eliminate CD25 binding and underperform clinically, DF6215 retains moderate IL-2 receptor α (IL-2Rα) affinity while enhancing IL-2Rβγ signaling and extending the half-life via an engineered immunoglobulin (Ig)G1 Fc domain. This design preferentially expands cytotoxic CD8+ T cells and natural killer cells over regulatory T cells, resulting in favorable effector-to-regulatory cell ratios, enhanced immune activation, and robust tumor regression in mouse models. In poorly immunogenic tumors, DF6215 synergized with PD-1 blockade to achieve durable responses without added toxicity. Cynomolgus monkey studies confirm DF6215's pharmacodynamics and favorable safety profile, with no signs of vascular leak syndrome or cytokine release syndrome. These findings position DF6215 as a differentiated IL-2 capable of modulating the tumor microenvironment and achieving potent anti-tumor immunity with improved tolerability, supporting its advancement into clinical trials for solid tumors.
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Dinutuximab beta effectively treats Ewing sarcoma when combined with chemotherapy.
In iScience on 16 January 2026 by Frapolli, R., Meroni, M., et al.
PubMed
Ewing sarcoma is a rare and aggressive cancer of the bone and soft tissues primarily affecting children and young adults. Prognosis for patients with metastatic or recurrent disease remains poor despite intensive multimodal therapy, highlighting the need of novel therapeutic approaches. The disialoganglioside GD2 is highly expressed on Ewing sarcoma cells, making this tumor eligible for anti-GD2 immunotherapy with dinutuximab beta. Through in vitro and in vivo approaches, this study demonstrated that dinutuximab beta effectively suppressed tumor growth by 60% (p = 0.0135) and improved survival rate by 68% (p = 0.0006) in a mouse model xenograft. The combination therapy with doxorubicin demonstrated superior efficacy compared to monotherapy, with enhanced tumor suppression (86%; p = 0.0009) and an extension of survival rate (146%; p = 0.000025). This study showed that dinutuximab beta, particularly in combination with standard chemotherapy, offers a promising approach to improve outcomes for high-risk Ewing sarcoma patients, providing a more effective alternative to current treatments.
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Activation of the pituitary adenylate cyclase-activating polypeptide type I receptor promotes neuroblastoma proliferation and migration through distinct G protein pathways.
In Cell Commun Signal on 16 January 2026 by Jang, S., Jeong, J. Y., et al.
PubMed
The pituitary adenylate cyclase-activating polypeptide type I receptor (PAC1R) is a class B G protein-coupled receptor implicated in a variety of physiological and pathological processes, including cancer. While PAC1R has been reported to act as either an oncogene or a tumor suppressor in a context-dependent manner, its role in neuroblastoma remains largely unexplored. In this study, we identify PAC1R as being selectively overexpressed in neuroblastoma and strongly associated with poor patient prognosis, supporting its potential as a prognostic biomarker. Functionally, PAC1R activation by PACAP38 promoted neuroblastoma cell proliferation and migration through distinct G protein signaling pathways. Pharmacological inhibition and CRISPR/Cas9-mediated gene knockout revealed that proliferation is mediated by the Gαs/EPAC/AKT-ERK axis, whereas migration requires cooperative signaling through Gα12/13- and Gαq-dependent activation of the RhoA-ROCK pathway. Comprehensive signaling analyses using TRUPATH and BRET-based biosensors demonstrated broad activation of Gαs, Gαq/11, and Gα13 by PACAP38 and PACAP27, while maxadilan and VIP displayed biased agonism toward Gαs and Gα15. β-Arrestin recruitment assays further showed that PACAP38 exhibits greater potency and efficacy than PACAP27. Among three PAC1R inhibitors tested, AMG-301, a clinical-stage monoclonal antibody, most effectively inhibited PAC1R-mediated G protein activation, calcium mobilization, RhoA signaling, proliferation, and migration. Together, these findings establish PAC1R as a functionally significant and druggable target in neuroblastoma, highlight its context-dependent signaling plasticity, and support the rationale for PAC1R-targeted therapeutic strategies in high-risk neuroblastoma.
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Preclinical characterisation of the protective capacity of an anti-nucleoprotein hRSV monoclonal antibody.
In EBioMedicine on 1 January 2026 by Farías, M. A., Andrade, C. A., et al.
PubMed
The human respiratory syncytial virus (hRSV) is a pathogen of global concern, causing significant morbidity and mortality, mainly in preterm infants. To date, all licenced monoclonal antibodies (mAbs) developed against hRSV have targeted its surface fusion or pre-fusion protein (F-hRSV).