InVivoMAb mouse IgG2b isotype control, unknown specificity
Product Description
Specifications
| Isotype | Mouse IgG2b, κ |
|---|---|
| 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 cell culture supernatant in an animal-free facility |
| Purification | Protein G |
| RRID | AB_1107791 |
| Molecular Weight | 150 kDa |
| 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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Turnis, M. E., et al (2016). "Interleukin-35 Limits Anti-Tumor Immunity" Immunity 44(2): 316-329.
PubMed
Regulatory T (Treg) cells pose a major barrier to effective anti-tumor immunity. Although Treg cell depletion enhances tumor rejection, the ensuing autoimmune sequelae limits its utility in the clinic and highlights the need for limiting Treg cell activity within the tumor microenvironment. Interleukin-35 (IL-35) is a Treg cell-secreted cytokine that inhibits T cell proliferation and function. Using an IL-35 reporter mouse, we observed substantial enrichment of IL-35(+) Treg cells in tumors. Neutralization with an IL-35-specific antibody or Treg cell-restricted deletion of IL-35 production limited tumor growth in multiple murine models of human cancer. Limiting intratumoral IL-35 enhanced T cell proliferation, effector function, antigen-specific responses, and long-term T cell memory. Treg cell-derived IL-35 promoted the expression of multiple inhibitory receptors (PD1, TIM3, LAG3), thereby facilitating intratumoral T cell exhaustion. These findings reveal previously unappreciated roles for IL-35 in limiting anti-tumor immunity and contributing to T cell dysfunction in the tumor microenvironment.
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Barreira da Silva, R., et al (2015). "Dipeptidylpeptidase 4 inhibition enhances lymphocyte trafficking, improving both naturally occurring tumor immunity and immunotherapy" Nat Immunol 16(8): 850-858.
PubMed
The success of antitumor immune responses depends on the infiltration of solid tumors by effector T cells, a process guided by chemokines. Here we show that in vivo post-translational processing of chemokines by dipeptidylpeptidase 4 (DPP4, also known as CD26) limits lymphocyte migration to sites of inflammation and tumors. Inhibition of DPP4 enzymatic activity enhanced tumor rejection by preserving biologically active CXCL10 and increasing trafficking into the tumor by lymphocytes expressing the counter-receptor CXCR3. Furthermore, DPP4 inhibition improved adjuvant-based immunotherapy, adoptive T cell transfer and checkpoint blockade. These findings provide direct in vivo evidence for control of lymphocyte trafficking via CXCL10 cleavage and support the use of DPP4 inhibitors for stabilizing biologically active forms of chemokines as a strategy to enhance tumor immunotherapy.
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Le Saout, C., et al (2014). "Chronic exposure to type-I IFN under lymphopenic conditions alters CD4 T cell homeostasis" PLoS Pathog 10(3): e1003976.
PubMed
HIV infection and the associated chronic immune activation alter T cell homeostasis leading to CD4 T cell depletion and CD8 T cell expansion. The mechanisms behind these outcomes are not totally defined and only partially explained by the direct cytopathic effect of the virus. In this manuscript, we addressed the impact of lymphopenia and chronic exposure to IFN-alpha on T cell homeostasis. In a lymphopenic murine model, this interaction led to decreased CD4 counts and CD8 T cell expansion in association with an increase in the Signal Transducer and Activator of Transcription 1 (STAT1) levels resulting in enhanced CD4 T cell responsiveness to IFN-alpha. Thus, in the setting of HIV infection, chronic stimulation of this pathway could be detrimental for CD4 T cell homeostasis.
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Lamere, M. W., et al (2011). "Regulation of antinucleoprotein IgG by systemic vaccination and its effect on influenza virus clearance" J Virol 85(10): 5027-5035.
PubMed
Seasonal influenza epidemics recur due to antigenic drift of envelope glycoprotein antigens and immune evasion of circulating viruses. Additionally, antigenic shift can lead to influenza pandemics. Thus, a universal vaccine that protects against multiple influenza virus strains could alleviate the continuing impact of this virus on human health. In mice, accelerated clearance of a new viral strain (cross-protection) can be elicited by prior infection (heterosubtypic immunity) or by immunization with the highly conserved internal nucleoprotein (NP). Both heterosubtypic immunity and NP-immune protection require antibody production. Here, we show that systemic immunization with NP readily accelerated clearance of a 2009 pandemic H1N1 influenza virus isolate in an antibody-dependent manner. However, human immunization with trivalent inactivated influenza virus vaccine (TIV) only rarely and modestly boosted existing levels of anti-NP IgG. Similar results were observed in mice, although the reaction could be enhanced with adjuvants, by adjusting the stoichiometry among NP and other vaccine components, and by increasing the interval between TIV prime and boost. Importantly, mouse heterosubtypic immunity that had waned over several months could be enhanced by injecting purified anti-NP IgG or by boosting with NP protein, correlating with a long-lived increase in anti-NP antibody titers. Thus, current immunization strategies poorly induce NP-immune antibody that is nonetheless capable of contributing to long-lived cross-protection. The high conservation of NP antigen and the known longevity of antibody responses suggest that the antiviral activity of anti-NP IgG may provide a critically needed component of a universal influenza vaccine.
Product Citations
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Adenovirus phagocytosis by neutrophils triggers a pro-inflammatory response.
In PLoS Pathog on 1 April 2026 by Laurans, S., Huerre, S., et al.
PubMed
Adenoviruses are common pathogens that have been engineered and used for medical purposes. While their recognition by innate immune cells such as macrophages and dendritic cells is well characterized, interactions with neutrophils remain poorly understood. Using cytometry,confocal and electron microscopy, we showed that neutrophils bind to antibody-coated adenoviruses and engulf them in a phagosome. Single-cell transcriptomic approach reveals that adenovirus phagocytosis activates a specific transcriptional program in neutrophils. It also triggers calcium entry, reactive oxygen species production in the phagosome and CXCL8 release. Moreover, 4 hours after adenovirus incubation, 50% of neutrophils undergo calcium- and RIPK3-dependent cell death, accompanied by Neutrophil Extracellular Trap emission. This rapid cell death impaired complete viral degradation after 3 hours, allowing residual adenoviruses to retain genomic expression potential in target cells Thus, our data suggest that, during adenoviral infection, the neutrophil response may promote a pro-inflammatory environment that could damage host tissues.
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Enterococcus faecalis impairs IGSF9-dependent C1q degradation to accelerate MAFLD-HCC progression.
In Gut Microbes Rep on 30 March 2026 by Jiang, Q., Li, J., et al.
PubMed
The global increase in metabolic associated fatty liver disease (MAFLD)-related hepatocellular carcinoma (HCC) necessitates urgent investigation of its underlying mechanisms. Our study reveals that high fat diet (HFD)-induced gut dysbiosis enriches Enterococcus faecalis, a potential carcinogenic bacterium. Mechanistically, which suppresses hepatic IGSF9 expression, exacerbating liver injury (elevated ALT/AST/ALP), steatosis, fibrosis, and HCC susceptibility. Clinically, reduced hepatic IGSF9 correlates with poor prognosis, particularly in MAFLD-HCC patients. Mechanistically, IGSF9 binds C1QC and E3 ubiquitin ligases (NEDD4/UBE3A) to promote C1QC ubiquitination and degradation; IGSF9 deficiency leads to pathogenic C1q accumulation, accelerating MAFLD progression. Importantly, early interventions targeting this axis - including Bifidobacterium pseudolongum supplementation, overexpressing IGSF9, and C1q neutralization - effectively prevented MAFLD-HCC progression in preclinical models. These findings provide preliminary evidence that the E. faecalis/IGSF9/C1q axis could be involved in MAFLD-HCC, with IGSF9 may serve as both a prognostic biomarker and therapeutic target, which worth further exploration in future studies.
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Inhibition of cell surface GRP78 and activated α2M interaction attenuates kidney fibrosis.
In JCI Insight on 22 December 2025 by Trink, J., Nmecha, I. K., et al.
PubMed
We recently showed that cell surface translocation of the endoplasmic reticulum-resident protein GRP78, when bound by activated α 2-macroglobulin (α2M*), induces pro-fibrotic responses in glomerular mesangial cells in response to high glucose and regulates activation of the pro-fibrotic cytokine transforming growth factor-β1 (TGF-β1), implicating a pathogenic role in glomerulosclerosis. Interstitial fibrosis, largely mediated by proximal tubular epithelial cells (PTEC) and renal fibroblasts, develops later in kidney disease and correlates with functional decline. Here we investigated whether interstitial fibrosis was mediated by cell surface GRP78 (csGRP78)/α2M*. High glucose and TGF-β1 increased csGRP78 and α2M* in PTEC and renal fibroblasts, and their inhibition prevented fibrotic protein production. Interestingly, for TGF-β1, this depended on inhibition of noncanonical signaling through YAP/TAZ, with Smad3 activation unaffected. In vivo, type 1 diabetic Akita mice overexpressing TGF-β1 were treated with either a neutralizing antibody for csGRP78 (C38) or α2M* (Fα2M) or an inhibitory peptide blocking csGRP78/α2M* interaction, and mice with unilateral ureteral obstruction were treated with Fα2M or inhibitory peptide. Consistently, inhibition by antibody or peptide attenuated fibrosis and pro-fibrotic signaling. These findings show an important role for csGRP78/α2M* in mediating tubulointerstitial fibrosis in both diabetic and nondiabetic kidney disease and support their inhibition as a potential antifibrotic therapeutic intervention.
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Targeting chaperone-mediated autophagy inhibits properties of glioblastoma stem cells and restores anti-tumor immunity.
In Nat Commun on 13 December 2025 by Li, Y., Sheng, M., et al.
PubMed
Chaperone-mediated autophagy (CMA) is a selective autophagic process essential for maintaining cellular quality and responding to stress. Dysregulation of the CMA pathway is increasingly recognized in various cancers, yet the mechanisms behind CMA hyperactivation in cancer cells remain unclear. Here, we show that CMA is upregulated in patient-derived glioblastoma stem cells (GSCs), indicated by a significant increase in the lysosomal abundance of the CMA receptor, lysosome-associated membrane protein 2 A (LAMP2A). This increase results from MST4-mediated phosphorylation of LAMP2A, enhancing its stability and promoting homotrimer formation while inhibiting degradation by Cathepsin A. CMA supports GSC proliferation and self-renewal by activating mTORC1 through the selective degradation of its negative regulators, TSC1 and TSC2. Additionally, CMA is involved in epigenetic silencing of the cGAS-STING pathway, promoting tumor immune escape via lysosomal degradation of the DNA demethylase TET3. Inhibition of CMA synergizes with immune checkpoint therapy in glioblastoma models, highlighting a potential therapeutic target.