Cetuximab CAS 205923-56-4
Introduction：Basic information about Cetuximab CAS 205923-56-4, including its chemical name, molecular formula, synonyms, physicochemical properties, and safety information, etc.
Cetuximab Basic informationApplications Immunogen Background
| Product Name: | Cetuximab |
| Synonyms: | CETUXIMAB;Hsdb 7454;Immunoglobulin G1, anti-(human epidermal growth factor receptor) (human-mouse monoclonal C225 gamma1-chain), disulfide with human-mouse monoclonal C225 kappa-chain, dimer;Unii-pqx0D8J21j;CetuxiMab(C225);EGFR antibody;IMC 225;Cetuximab (anti-EGFR) |
| CAS: | 205923-56-4 |
| MF: | C107H179N35O36S7 |
| MW: | 2756.23406 |
| EINECS: | |
| Product Categories: | |
| Mol File: | 205923-56-4.mol |
Cetuximab Chemical Properties
| storage temp. | Store at 4°C, do not freeze |
| form | Liquid |
| color | Colorless to light yellow |
| InChIKey | HBMCYCKNGADUQP-CFIKXUEXSA-N |
Safety Information
| Hazardous Substances Data | 205923-56-4(Hazardous Substances Data) |
| Description | Cetuximab, a human/mouse chimeric monoclonal antibody that blocks the EGFR,was launched for use in combination with irinotecan in the treatment of patients with colorectal cancer who no longer respond to standard chemotherapytreatment with irinotecan. Cetuximab is obtained by chimerization of M225, amurine anti-EGFR antibody; specifically heavy and light chains of the murineantibody are cloned and adapted for expression with constant regions of the humankappa light chain and human gamma1 heavy chain. It is produced by mammalian(suspension) cells in serum-free medium, purified by protein A affinity chromatography,ion-exchange chromatography, and gel filtration. Cetuximab binds specificallyto EGFR on both normal and tumor cells. Overexpression of the human EGFR isdetected in many cancers, including those of the colon and rectum. The binding ofcetuximab to EGFR prevents growth factors from binding to the receptor, therebyinhibiting cell growth and inducing apoptosis. The therapeutic regimen of cetuximabconsists of an initial loading dose of 400 mg/m2 administered as a 120-min IVinfusion, followed by weekly maintenance dose of 250 mg/m2 infused over 60 min.The steady-state plasma concentrations of cetuximab are reached by the third weeklyinfusion and the mean elimination half-life is 114 h. Cetuximab is eliminated bybinding to EGFRs in various tissues, followed by internalization of the antibody-EGFR complex. Systemic clearance of the antibody is saturated at higher doses, andthis appears to correlate with saturation of EGFR binding. In a multicenter clinicaltrial in more than 300 patients with advanced metastatic colorectal cancer,combination therapy with cetuximab and irinotecan produced response in morethan half of the patients, shrinking tumors in 23% and stopping tumor growth in anadditional 33% of the patients. The most common adverse reactions associated withcetuximab were acneform rash, asthenia/malaise, fever, nausea, abdominal pain,constipation and vomiting. Serious adverse events such as infusion reaction, fever,sepsis, kidney failure, dehydration and diarrhea were experienced by ＜10% of thepatients. |
| Originator | ImClone (US) |
| Uses | Treatment of EGF receptor-expressing cancers(monoclonal antibod. |
| Brand name | Erbitux |
| Mechanism of action | Cetuximab, a monoclonal antibody, binds to the extracellular domain of the EGFR, which is overexpressed in many human cancers, including head, neck, and colorectal types. This process prevents the EGFR from binding with its endogenous ligand, blocking the receptor-dependent transduction pathway and providing many antitumor effects involving cell-cycle arrest, induction of apoptosis, inhibition of angiogenesis, inhibition of metastasis, internalization, and downregulation of the EGFR, and enhancement of the sensitivity to radiochemotherapy[1]. |
| Clinical Use | Monoclonal antibody: Treatment of EGFR-expressing metastatic colorectal cancer in combination with irinotecan after failure of irinotecan-including cytotoxic therapy Treatment of head and neck cancer |
| Toxicology | The majority of skin toxicities were mild to moderate, symptomatic treatments were effective in controlling them. The skin discomfort caused by cetuximab can affect the quality of life temporarily; with long term treatment, severity of skin toxicity may decrease. |
| Drug interactions | Potentially hazardous interactions with other drugs Avoid with live vaccines. |
| Metabolism | Several pathways have been described that may contribute to the metabolism of antibodies. All of these pathways involve the biodegradation of the antibody to smaller molecules, i.e. small peptides or amino acids. |
| Applications | EGFR antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Recommended dilution range for Western blot analysis is 1:500 ~ 1000. Recommended starting dilution is 1:500. |
| Immunogen | Anti-human EGFR mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EGFR amino acids 424-605 purified from E. coli. |
| Background | The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis. |
| References | [1] W Bou-Assaly, S Mukherji. “Cetuximab (erbitux).” American Journal of Neuroradiology 31 4 (2010): 626–7. |
Cetuximab Preparation Products And Raw materials
