Mouse Anti-Human EGFR
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| Cat-Nr. | 101-M386 |
| Size | 100 µg |
| Price | 380 € |
| Category | Monoclonal Antibody |
| Clone Nr. | (#5S21) |
| Isotype | IgG2 |
| Species Reactivity | Human |
| Formulation | lyophilized |
| Buffer | PBS |
| Reconstitution | Centrifuge vial prior to opening. Reconstitute the antibody with 500 µl sterile PBS and the final concentration is 200 µg/ml. |
| Stability and Storage | Lyophilized samples are stable for 2 years from date of receipt when stored at -70°C. Reconstituted antibody can be aliquoted and stored frozen at < -20°C for at least six months without detectable loss of activity. |
| Preparation | This antibody was produced from a hybridoma (mouse myeloma fused with spleen cells from a mouse) immunized with human recombinant EGF-R extracellular domain (also called erythroblastic leukemia viral oncogene homolog 1 (ErbB1). The IgG2 fraction of culture supernatant was purified by Protein G affinity chromatography. |
| Antigen | Human recombinant EGF-R EC domain |
| Application | WB |
| Synonyms | EGF receptor; EGFR; ERBB; HER1; mENA; ERBB1; PIG61 |
| Description | 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, HER2), ErbB3 (HER3), and ErbB4 (HER4). All family members are type I transmembrane glycoproteins that have 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 α, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2α in the absence of a coreceptor. Ligand binding induces EGF R homodimerization as well as heterodimerization 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. |
| Uniprot ID | P00533 |
| Protein RefSeq | NP_005219 |
| mRNA RefSeq | NM_005228 |
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