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The Anti-EGFR Protein A Scaffold molecule is a specific affinity ligand selected against the extra cellular domain of EGFR. The molecule can advantageously be used for fluorescence and immunohistochemical studies of EGFR-expression on cells and frozen tissue sections. Staining of paraffin embedded tissues is not recommended. The Anti-EGFR Protein A Scaffold molecule is modified with a unique C-terminal cysteine for directed single-point chemical modification, facilitating labeling with fluorescent dyes, biotin or coupling to matrices.
Fluorescence and immunohistochemical staining of cells and frozen tissue sections, flow cytometry.
Anti-EGFR Protein A scaffold molecule binds to the extracellular domain of human epidermal growth factor receptor (EGFR, ErbB). Cross reactivity with other species has not been tested.
At +4°C is recommended for lyophilized protein. For reconstituted protein in physiological buffer, short-term storage at +4°C is recommended. For long-term storage, the protein solution should be aliquoted and then stored at -20°C. There is no decrease i
The Epidermal Growth Factor Receptor (EGFR, ErbB) is a cell surface glycoprotein of approximately 135 kDa (unglycosylated). There are several alternatively spliced forms of EGFR including a secreted soluble form. The EFGR belongs to the family tyrosine kinase receptors which are characterized by an extracellular ligand-binding domain, a single transmembrane and an intracellular domain responsible for transducing the signal. The receptor dimerizes upon binding to EGFR and the transduced signal stimulates cell growth and differentiation. The EGFR is over expressed or mutated in many types of cancers and the receptor as well as the down stream signaling molecules are subjects to several cancer therapeutic interventions.
ATP binding; MAP/ERK kinase kinase activity; actin filament binding; double-stranded DNA binding; epidermal growth factor receptor activity; identical protein binding.