SRP3028
EGF-receptor human
recombinant, expressed in CHO cells, ≥95% (SDS-PAGE), ≥95% (HPLC), suitable for cell culture
Synonym(s):
ErbB1
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
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biological source
human
recombinant
expressed in CHO cells
Assay
≥95% (HPLC)
≥95% (SDS-PAGE)
form
lyophilized
mol wt
97.5 kDa
packaging
pkg of 10 μg
technique(s)
cell culture | mammalian: suitable
impurities
<0.1 EU/μg endotoxin, tested
color
white to off-white
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... EGFR(1956)
General description
Epidermal growth factor receptor (EGFR, ErbB1) is a transmembrane protein that exerts tyrosine kinase activity upon ligand induced activation. EGFR can be activated by binding EGF or at least six other structurally related protein ligands, including transforming growth factor α (TGFα), heparin-binding EGF-like growth factor (HB-EGF), betacellulin (BTC), amphiregulin, epiregulin, and epigen. The gene encoding it is localized on human chromosome 7p11.2. Recombinant soluble human EGFR is a 621 amino acid glycoprotein comprising the extracellular domain of EGFR, and migrates at an apparent MW of 97.5 kDa by SDS-PAGE analysis under reducing conditions.
Biochem/physiol Actions
Upon activation by ligands, epidermal growth factor receptor (EGFR, ErbB1) initiates a signaling cascade which includes dimerization and internalization, tyrosine phosphorylation, DNA synthesis of target genes, and, ultimately, cell proliferation. EGFR signaling plays a role in the growth and differentiation of normal cells, but elevated EGFR activity is correlated with the development and pathogenesis of certain cancers.
Sequence
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 S
Physical form
Lyophilized from 10 mM Sodium Phosphate, pH 7.5.
Reconstitution
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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G N Gill et al.
Molecular and cellular endocrinology, 51(3), 169-186 (1987-06-01)
Epidermal growth factor (EGF) binds with high affinity and specificity to a single site on the external domain of its transmembrane receptor to activate the tyrosine protein kinase activity of its cytoplasmic portion. The EGF receptor gene is amplified and
K Helin et al.
Oncogene, 6(5), 825-832 (1991-05-01)
The epidermal growth factor receptor (EGF-R) C-terminus contains three conserved tyrosines (Y-1068, Y-1148, Y-1173) which are phosphorylated upon EGF activation. To clarify the functional role of these tyrosines, each has been mutated to phenylalanine and studied as single, double and
Nam Y Lee et al.
Protein science : a publication of the Protein Society, 15(5), 1142-1152 (2006-04-07)
The C-terminal phosphorylation domain of the epidermal growth factor receptor is believed to regulate protein kinase activity as well as mediate the assembly of signal transduction complexes. The structure and dynamics of this proposed autoregulatory domain were examined by labeling
Molecular mechanisms of resistance to the EGFR monoclonal antibody cetuximab.
Brand TM
Cancer Biology & Therapy, 11(9), 777-792 (2011)
A chromosomal region 7p11.2 transcript map: its development and application to the study of EGFR amplicons in glioblastoma.
Eley GD
Neuro-Oncology, 4(2), 86-94 (2002)
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