Protein protein interaction immunofluorescence result.
Representative image of Proximity Ligation Assay of protein-protein interactions between TGFA and ERBB2. HeLa cells were stained with anti-TGFA rabbit purified polyclonal antibody 1:1200 and anti-ERBB2 mouse monoclonal antibody 1:50. Each red dot represents the detection of protein-protein interaction complex. The images were analyzed using an optimized freeware (BlobFinder) download from The Centre for Image Analysis at Uppsala University.
Antibody pair set content: 1. TGFA rabbit purified polyclonal antibody (20 ug) 2. ERBB2 mouse monoclonal antibody (40 ug) *Reagents are sufficient for at least 30-50 assays using recommended protocols.
Store reagents of the antibody pair set at -20°C or lower. Please aliquot to avoid repeated freeze thaw cycle. Reagents should be returned to -20°C storage immediately after use.
Transforming growth factors (TGFs) are biologically active polypeptides that reversibly confer the transformed phenotype on cultured cells. TGF-alpha shows about 40% sequence homology with epidermal growth factor (EGF; MIM 131530) and competes with EGF for binding to the EGF receptor (MIM 131550), stimulating its phosphorylation and producing a mitogenic response.[supplied by OMIM
This gene encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized. [provided by RefSeq