EGFR Human, CHO
| Epidermal Growth Factor Receptor, Receptor Tyrosine-Protein Kinase ErbB-1, Erb-B2 Receptor Tyrosine Kinase, Proto-Oncogene C-ErbB-1, EC 2.7.10.1, ERBB1, ERBB, HER1, Epidermal Growth Factor Receptor (Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog), Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog (Avian), Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog, Cell Proliferation-Inducing Protein 61, Cell Growth Inhibiting Protein 40, EC 2.7.10, NISBD2, PIG61, MENA. |
Description
EGFR produced in CHO cells is a single, glycosylated polypeptide chain containing 860 amino acids (25-645 a.a.) and having a molecular mass of 95.5 kDa (Migrates at 100-150 on SDS-PAGE under reducing conditions). EGFR is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
| The EGFR protein solution is provided at a concentration of 0.25 mg/ml and is formulated in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol. |
| Epidermal Growth Factor Receptor, Receptor Tyrosine-Protein Kinase ErbB-1, Erb-B2 Receptor Tyrosine Kinase, Proto-Oncogene C-ErbB-1, EC 2.7.10.1, ERBB1, ERBB, HER1, Epidermal Growth Factor Receptor (Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog), Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog (Avian), Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog, Cell Proliferation-Inducing Protein 61, Cell Growth Inhibiting Protein 40, EC 2.7.10, NISBD2, PIG61, MENA. |
| LEEKKVCQGT SNKLTQLGTF EDHFLSLQRM FNNCEVVLGN LEITYVQRNY DLSFLKTIQE VAGYVLIALN TVERIPLENL QIIRGNMYYE NSYALAVLSN YDANKTGLKE LPMRNLQEIL HGAVRFSNNP ALCNVESIQW RDIVSSDFLS NMSMDFQNHL GSCQKCDPSC PNGSCWGAGE ENCQKLTKII CAQQCSGRCR GKSPSDCCHN QCAAGCTGPR ESDCLVCRKF RDEATCKDTC PPLMLYNPTT YQMDVNPEGK YSFGATCVKK CPRNYVVTDH GSCVRACGAD SYEMEEDGVR KCKKCEGPCR KVCNGIGIGE FKDSLSINAT NIKHFKNCTS ISGDLHILPV AFRGDSFTHT PPLDPQELDI LKTVKEITGF LLIQAWPENR TDLHAFENLE IIRGRTKQHG QFSLAVVSLN ITSLGLRSLK EISDGDVIIS GNKNLCYANT INWKKLFGTS GQKTKIISNR GENSCKATGQ VCHALCSPEG CWGPEPRDCV SCRNVSRGRE CVDKCNLLEG EPREFVENSE CIQCHPECLP QAMNITCTGR GPDNCIQCAH YIDGPHCVKT CPAGVMGENN TLVWKYADAG HVCHLCHPNC TYGCTGPGLE GCPTNGPKIP SRSPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH. |
Product Science Overview
The 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 are receptor tyrosine kinases. EGFR is activated by binding to its specific ligands, such as epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-α).
EGFR is composed of an extracellular ligand-binding domain, a single transmembrane helix, an intracellular tyrosine kinase domain, and a C-terminal regulatory region. Upon ligand binding, EGFR undergoes dimerization, either as a homodimer or heterodimer with other ErbB family members. This dimerization activates the intrinsic kinase activity of the receptor, leading to autophosphorylation of specific tyrosine residues in the C-terminal domain. These phosphorylated tyrosines serve as docking sites for various signaling proteins, initiating multiple downstream signaling pathways, including the MAPK, PI3K/AKT, and JAK/STAT pathways.
Chinese Hamster Ovary (CHO) cells are widely used in biotechnology for the production of recombinant proteins, including human EGFR. Recombinant human EGFR produced in CHO cells is a glycosylated polypeptide chain containing 860 amino acids and has a molecular mass of approximately 95.5 kDa . The recombinant protein is expressed with a 239 amino acid hIgG-His tag at the C-terminus and is purified using proprietary chromatographic techniques .
Recombinant human EGFR is used in various research and therapeutic applications. It is utilized in studies to understand the molecular mechanisms of EGFR signaling and its role in cancer and other diseases. Additionally, recombinant EGFR is employed in drug discovery and development, particularly in the screening and evaluation of potential EGFR inhibitors for cancer therapy.
EGFR is overexpressed or mutated in various cancers, including non-small cell lung cancer, colorectal cancer, and glioblastoma. These alterations lead to aberrant activation of EGFR signaling pathways, promoting uncontrolled cell proliferation and survival. Targeting EGFR with specific inhibitors, such as tyrosine kinase inhibitors (TKIs) and monoclonal antibodies, has become a key therapeutic strategy in the treatment of EGFR-driven cancers.
