Recombinant EGFR Antibody
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.
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Description
Product Specs
QVQLKQSGPGLVQPSQSLSITCTVSGFSLTNYGVHWVRQSPGKGLEWLGVIWSGGNTDYNTP
FTSRLSINKDNSKSQVFFKMNSLQSNDTAIYYCARALTYYDYEFAYWGQGTLVTVSAASTKG
PSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSS
VVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPK
PKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTV
LHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVK
GFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEAL
HNHYTQKSLSLSPGK.
Light chain
DILLTQSPVILSVSPGERVSFSCRASQSIGTNIHWYQQRTNGSPRLLIKYASESISGIPSRF
SGSGSGTDFTLSINSVESEDIADYYCQQNNNWPTTFGAGTKLELKRTVAAPSVFIFPPSDEQ
LKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADY
EKHKVYACEVTHQGLSSPVTKSFNRGEC.
Product Science Overview
The human epidermal growth factor receptor (EGFR) is a transmembrane protein that plays a crucial role in the regulation of cell growth, survival, proliferation, and differentiation. It is a member of the ErbB family of receptors, which includes four closely related receptors: EGFR (ErbB1), HER2 (ErbB2), HER3 (ErbB3), and HER4 (ErbB4) . Aberrations in EGFR signaling are often associated with various types of cancers, making it a significant target for cancer therapy.
EGFR consists of an extracellular ligand-binding domain, a single transmembrane helix, and an intracellular tyrosine kinase domain . Upon binding with its specific ligands, such as epidermal growth factor (EGF) or transforming growth factor-alpha (TGF-α), EGFR undergoes dimerization and autophosphorylation, which triggers a cascade of downstream signaling pathways involved in cellular processes .
Recombinant anti-EGFR antibodies are engineered proteins designed to specifically bind to the EGFR, inhibiting its activity and thereby blocking the signaling pathways that lead to tumor growth and proliferation . These antibodies can be produced using various expression systems, including bacterial, yeast, insect, and mammalian cells .
One notable example is cetuximab (Erbitux), a recombinant chimeric monoclonal antibody that targets the extracellular domain of EGFR . Cetuximab binds to EGFR with high affinity, preventing the binding of natural ligands and promoting receptor internalization and degradation . This inhibition of EGFR signaling can lead to reduced tumor cell proliferation and increased apoptosis.
The production of recombinant anti-EGFR antibodies involves the insertion of the gene encoding the antibody into an expression vector, which is then introduced into a suitable host cell line . The host cells are cultured under optimal conditions to express the antibody, which is subsequently purified using techniques such as affinity chromatography and size-exclusion chromatography .
For instance, recombinant dimeric IgA antibodies against EGFR have been produced using Chinese hamster ovarian (CHO)-K1 cells . These antibodies were purified by anti-human κ and anti–His-tag affinity, as well as size-exclusion chromatography, resulting in a homogenous preparation of highly pure IgA dimers .
Recombinant anti-EGFR antibodies have shown significant promise in the treatment of various cancers, including colorectal cancer, head and neck cancer, and non-small cell lung cancer . By targeting EGFR, these antibodies can inhibit tumor growth, enhance the efficacy of chemotherapy and radiotherapy, and improve patient outcomes .
In addition to cetuximab, other anti-EGFR antibodies such as panitumumab and necitumumab have been developed and approved for clinical use . These antibodies differ in their structure, binding affinity, and clinical applications, but they all share the common goal of targeting EGFR to combat cancer.
