Recombinant Phospho-EGFR (Tyr1173) Monoclonal Antibody (AN302101L)
For research use only.
| Verified Samples |
Verified Samples in WB: A431, A431+EGF (200ng/mL 15 min) Verified Samples in IF: (A) A431, (B) A431 + EGF (200 ng/mL, 15min) |
| Dilution | WB 1:1000, IF 1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB, IF |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Peptide. This information is proprietary to PTMab |
| Abbre | Phospho-EGFR (Tyr1173) |
| 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 |
170 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 | Endosome, Nucleus, Membrane |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Signal Transduction, Cancer |
| Clone No. | A825 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand bindingresults in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation.Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the activestate enzyme, and providing a binding surface for substrate proteins. c-Src is involved in phosphorylation of EGFR at Tyr845. The SH2 domainof PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling. Phosphorylation of EGFR at Tyr1045creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation. TheGRB2 adaptor protein binds activated EGFR at phospho-Tyr1068. A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide adocking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation. Phosphorylation of EGFR at specificserine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylatedby CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation. |
Other Clones
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Unconjugated
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