Recombinant Phospho-EGF Receptor (Tyr1068) Monoclonal Antibody (AN300009L)
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For research use only.
| Verified Samples | Verified Samples in WB: Hela |
| Dilution | WB 1:1000-1:10000, |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB |
| Clonality | Rabbit Monoclonal |
| Immunogen | A synthetic peptide corresponding to the residues around Tyr1068 of Human Phospho-EGF Receptor |
| Abbre | EGFR |
| Synonyms | PIG, HER, Proto-oncogene c-ErbB, Receptortyrosine-protein kinase erbB, Receptor tyrosine-protein kinase erbB, NISBD, EGFR, ERBB, ERBB1, HER1, NISBD2, PIG61, mENA, ErbB-1, Receptortyrosine-protein kinase erbB-1, Epidermal growth factor receptor, Proto-oncogene c-ErbB-1, Receptor tyrosine-protein kinase erbB-1, NISBD2, epidermal growth factor receptor, ERBB, ERBB1, HER1, mENA, NISBD2, PIG61, Avian erythroblastic leukemia viral (v erb b) oncogene homolog, Cell growth inhibiting protein 40, Cell proliferation inducing protein 61, EGF R, Epidermal growth factor receptor (avian erythroblastic leukemia viral (v erb b) oncogene homolog), Epidermal growth factor receptor (erythroblastic leukemia viral (v erb b) oncogene homolog avian), ErbB1, ERBB, erb-b2 receptor tyrosine kinase 1, Errp, Oncogen ERBB, Receptor tyrosine protein kinase ErbB 1, SA7, Species antigen 7, Urogastrone, v-erb-b Avian erythroblastic leukemia viral oncogen homolog, wa2, Wa5 |
| Swissprot | |
| Calculated MW | 134 kDa |
| Observed MW |
180-220 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Membrane, Endosome, Endoplasmic reticulum membrane, Golgi apparatus membrane, Nucleus membrane, Secreted. |
| Tissue Specificity | Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers. |
| Concentration | 1 mg/mL |
| Buffer | 10 mM sodium HEPES, 150 mM NaCl, 100 μg/mL protein protectant, 50% glycerol, pH 7.5 |
| Purification Method | Protein A |
| Research Areas | Signal Transduction, Cancer |
| Clone No. | 2B12 |
| Conjugation | Unconjugated |
| Storage | This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles. |
| Shipping | Ice bag |
| background | The epidermal growth factor receptor (EGFR) subfamily of receptor tyrosine kinases comprises four members: EGFR (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 EGFR 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. 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 alpha 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. |
Other Clones
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