$ 720.00
Details
The Human ErbB3 (HER3) ELISA quantitates Hu HER3 in human serum, plasma, or cell culture medium. The assay will exclusively recognize both natural and recombinant Hu HER3. Principle of the method The Human HER3 solid-phase sandwich ELISA (enzyme-linked immunosorbent assay) is designed to measure the amount of the target bound between a matched antibody pair. A target-specific antibody has been pre-coated in the wells of the supplied microplate. Samples, standards, or controls are then added into these wells and bind to the immobilized (capture) antibody. The sandwich is formed by the addition of the second (detector) antibody, a substrate solution is added that reacts with the enzyme-antibody-target complex to produce measurable signal. The intensity of this signal is directly proportional to the concentration of target present in the original specimen. Rigorous validation Each manufactured lot of this ELISA kit is quality tested for criteria such as sensitivity, specificity, precision, and lot-to-lot consistency. See manual for more information on validation.ErbB3 (c-erbB-3/HER-3) is a member of the type I family of growth factor receptors and binds to ligands in the heregulin family. ErbB3 is over-expressed in a variety of tumors in the prostate, bladder, breast, stomach, pancreas, and colon. Heregulin and EGF stimulate tyrosine phosphorylation of c-erbB-3 to different extents. The ErbB3 gene is located on the long arm of human chromosome 12 (12q13) and is transcribed into a 6.2kb mRNA which is translated into a 160/180kDa glycoprotein. The ErbB3 gene encodes a transmembrane receptor tyrosine kinase due to alternative splicing and forms heterodimers with other EGF receptor family members that have kinase activity. Heterodimerization leads to the activation of pathways that lead to cell proliferation or differentiation. Alternate transcriptional splice variants encoding different isoforms of ErbB3 have been characterized. One ErbB3 isoform lacks the intermembrane region, is secreted outside the cell, and acts to modulate the activity of the membrane-bound form. Additional splice variants have also been reported, but they have not been thoroughly characterized.
