InVivoSIM anti-human EGFR (Cetuximab Biosimilar)

Catalog #SIM0002
Product Citations:
2
Clone:
Cetuximab
Reactivities:
Human

$224.00 - $7,752.00

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  • 100 mg - $7,752.00
  • 50 mg - $4,356.00
  • 25 mg - $3,030.00
  • 5 mg - $868.00
  • 1 mg - $224.00
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Product Details

This non-therapeutic biosimilar antibody uses the same variable regions from the therapeutic antibody Cetuximab making it ideal for research use. This Cetuximab biosimilar reacts with human EGFR (epidermal growth factor receptor) also known as ErbB-1. EGFR is a 170 kDa cell-surface receptor and belongs to the ErbB family of receptors. EGFR signaling is activated upon binding one of its ligands including epidermal growth factor (EGF), transforming growth factor α (TGF α), Amphiregulin, and heparin binding-EGF (HB-EGF). Upon activation, EGFR transitions from an inactive monomeric form to an active homodimer. This initiates several downstream signal transduction cascades including the MAPK, Akt and JNK pathways, leading to DNA synthesis and cell proliferation. EGFR overexpression or constitutive activation are associated with many cancers. For this reason, anti-EGFR monoclonal antibody mediated immunotherapies are currently being explored as cancer treatments. Cetuximab inhibits tumor cell proliferation by blocking the interaction of EGF with EGFR.

Specifications

Isotype Human IgG1
Recommended Isotype Control(s) RecombiMAb human IgG1 isotype control, anti-hen egg lysozyme
Recommended Dilution Buffer InVivoPure pH 7.0 Dilution Buffer
Conjugation This product is unconjugated. Conjugation is available via our Antibody Conjugation Services.
Immunogen Human EGFR (ErbB1)
Reported Applications EGFR blockade
ELISA
Flow Cytometry
Formulation PBS, pH 7.0
Contains no stabilizers or preservatives
Endotoxin <1EU/mg (<0.001EU/μg)
Determined by LAL gel clotting assay
Aggregation <5%
Determined by SEC
Purity >95%
Determined by SDS-PAGE
Sterility 0.2 µm filtration
Production Purified from cell culture supernatant in an animal-free facility
Purification Protein A
RRID AB_2894723
Molecular Weight 150 kDa
Murine Pathogen Tests Ectromelia/Mousepox Virus: Negative
Hantavirus: Negative
K Virus: Negative
Lactate Dehydrogenase-Elevating Virus: Negative
Lymphocytic Choriomeningitis virus: Negative
Mouse Adenovirus: Negative
Mouse Cytomegalovirus: Negative
Mouse Hepatitis Virus: Negative
Mouse Minute Virus: Negative
Mouse Norovirus: Negative
Mouse Parvovirus: Negative
Mouse Rotavirus: Negative
Mycoplasma Pulmonis: Negative
Pneumonia Virus of Mice: Negative
Polyoma Virus: Negative
Reovirus Screen: Negative
Sendai Virus: Negative
Theiler’s Murine Encephalomyelitis: Negative
Storage The antibody solution should be stored at the stock concentration at 4°C. Do not freeze.
in vitro EGFR blockade
Linde IL, Prestwood TR, Qiu J, Pilarowski G, Linde MH, Zhang X, Shen L, Reticker-Flynn NE, Chiu DK, Sheu LY, Van Deursen S, Tolentino LL, Song WC, Engleman EG. (2023). "Neutrophil-activating therapy for the treatment of cancer" Cancer Cell 41(2):356-372.e10. PubMed

Despite their cytotoxic capacity, neutrophils are often co-opted by cancers to promote immunosuppression, tumor growth, and metastasis. Consequently, these cells have received little attention as potential cancer immunotherapeutic agents. Here, we demonstrate in mouse models that neutrophils can be harnessed to induce eradication of tumors and reduce metastatic seeding through the combined actions of tumor necrosis factor, CD40 agonist, and tumor-binding antibody. The same combination activates human neutrophils in vitro, enabling their lysis of human tumor cells. Mechanistically, this therapy induces rapid mobilization and tumor infiltration of neutrophils along with complement activation in tumors. Complement component C5a activates neutrophils to produce leukotriene B4, which stimulates reactive oxygen species production via xanthine oxidase, resulting in oxidative damage and T cell-independent clearance of multiple tumor types. These data establish neutrophils as potent anti-tumor immune mediators and define an inflammatory pathway that can be harnessed to drive neutrophil-mediated eradication of cancer.

    • Cancer Research
    • ,
    • Immunology and Microbiology
    A highly potent anti-VISTA antibody KVA12123 - a new immune checkpoint inhibitor and a promising therapy against poorly immunogenic tumors.

    In Frontiers in Immunology on 28 December 2023 by Iadonato, S., Ovechkina, Y., et al.

    PubMed

    Immune checkpoint therapies have led to significant breakthroughs in cancer patient treatment in recent years. However, their efficiency is variable, and resistance to immunotherapies is common. VISTA is an immune-suppressive checkpoint inhibitor of T cell response belonging to the B7 family and a promising novel therapeutic target. VISTA is expressed in the immuno-suppressive tumor microenvironment, primarily by myeloid lineage cells, and its genetic knockout or antibody blockade restores an efficient antitumor immune response. Fully human monoclonal antibodies directed against VISTA were produced after immunizing humanized Trianni mice and single B cell sequencing. Anti-VISTA antibodies were evaluated for specificity, cross-reactivity, monocyte and T cell activation, Fc-effector functions, and antitumor efficacy using in vitro and in vivo models to select the KVA12123 antibody lead candidate. The pharmacokinetics and safety profiles of KVA12123 were evaluated in cynomolgus monkeys. Here, we report the development of a clinical candidate anti-VISTA monoclonal antibody, KVA12123. KVA12123 showed high affinity binding to VISTA through a unique epitope distinct from other clinical-stage anti-VISTA monoclonal antibodies. This clinical candidate demonstrated high specificity against VISTA with no cross-reactivity detected against other members of the B7 family. KVA12123 blocked VISTA binding to its binding partners. KVA12123 induced T cell activation and demonstrated NK-mediated monocyte activation. KVA12123 treatment mediated strong single-agent antitumor activity in several syngeneic tumor models and showed enhanced efficacy in combination with anti-PD-1 treatment. This clinical candidate was engineered to improve its pharmacokinetic characteristics and reduce Fc-effector functions. It was well-tolerated in preclinical toxicology studies in cynomolgus monkeys, where hematology, clinical chemistry evaluations, and clinical observations revealed no indicators of toxicity. No cytokines associated with cytokine release syndrome were elevated. These results establish that KVA12123 is a promising drug candidate with a distinct but complementary mechanism of action of the first generation of immune checkpoint inhibitors. This antibody is currently evaluated alone and in combination with pembrolizumab in a Phase 1/2 open-label clinical trial in patients with advanced solid tumors. Copyright © 2023 Iadonato, Ovechkina, Lustig, Cross, Eyde, Frazier, Kabi, Katz, Lance, Peckham, Sridhar, Talbaux, Tihista, Xu and Guillaudeux.

    • FC/FACS
    • ,
    • Mus musculus (House mouse)
    • ,
    • Cancer Research
    Neutrophil-activating therapy for the treatment of cancer.

    In Cancer Cell on 13 February 2023 by Linde, I. L., Prestwood, T. R., et al.

    PubMed

    Despite their cytotoxic capacity, neutrophils are often co-opted by cancers to promote immunosuppression, tumor growth, and metastasis. Consequently, these cells have received little attention as potential cancer immunotherapeutic agents. Here, we demonstrate in mouse models that neutrophils can be harnessed to induce eradication of tumors and reduce metastatic seeding through the combined actions of tumor necrosis factor, CD40 agonist, and tumor-binding antibody. The same combination activates human neutrophils in vitro, enabling their lysis of human tumor cells. Mechanistically, this therapy induces rapid mobilization and tumor infiltration of neutrophils along with complement activation in tumors. Complement component C5a activates neutrophils to produce leukotriene B4, which stimulates reactive oxygen species production via xanthine oxidase, resulting in oxidative damage and T cell-independent clearance of multiple tumor types. These data establish neutrophils as potent anti-tumor immune mediators and define an inflammatory pathway that can be harnessed to drive neutrophil-mediated eradication of cancer. Copyright © 2023 Elsevier Inc. All rights reserved.