EGFR, soluble

CAT: 0209-S01-040SSize: 10 µgDry Ice: NoHazardous: No
CAT#:0209-S01-040SSize:10 µg
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AVAILABILITY: InStock
24/48H Stock Items & 2 to 6 Weeks non Stock Items.
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Description
Recombinant human soluble EGFR is produced as a glycosylated monomeric protein with a mass of approximately 70 kDa in insect cells. The epidermal growth factor receptor (EGFR) subfamily of receptor tyrosine kinases comprises four members: EGFR (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 EGFR gene encodes a 1210 amino acid (aa) residue precursor with a 24aa putative signal peptide, a 621aa extracellular domain, a 23aa transmembrane domain, and a 542aa cytoplasmic domain. EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis.
Synonyms
EGF receptor; EGFR; ERBB; HER1; mENA; ERBB1; PIG61
NCBI Gene ID
1956
UniProt
P00533
Accession Number
NP_005219
Accession Number mRNA
NM_005228
Chromosomal Location
7p12
Reactivity
Human
Cross Reactivity
Human
Label
Strep-Tag
Sequence
LEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPS
Assay Protocol
The lyophilized sEGFR is soluble in water and most aqueous buffers. The lyophilized sEGFR should be reconstituted in water or PBS to a concentration of not lower than 50µg/ml.
Purity
~ 90% by SDS-PAGE
Bioactivity
Measured by its ability to bind to immobilized recombinant human EGF in a functional ELISA.
Length
629
Form
Lyophilized
Buffer
PBS
Reconstitution
Water
Molecular Weight
~ 85.0 kDa
Storage Conditions
Lyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted sEGFR should be stored in working aliquots at -20°C. Avoid repeated freeze-thaw cycles!
Host or Source
Insect cells

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