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The Human Granulocyte-Colony Stimulating Factor(Hu G-CSF) ELISA quantitates Hu G-CSF in human serum, plasma, cell culture supernatants or other body fluids. The assay will exclusively recognize both natural and recombinant Hu G-CSF. Principle of the method The Human G-CSF 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 or controls are then added into these wells and bind to the immobilized (capture) antibody. The sandwich is formed by the binding of the second (detector) antibody to the target on a different epitope from the capture antibody. An antibody conjugated with enzyme binds the formed sandwich. After incubation and washing steps to rid the microplate of unbound substances, 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.G-CSF (Granulocyte colony stimulating factor) is a naturally occurring cytokine that stimulates the production and antibacterial function of neutrophils and monocytes. Human G-CSF is an 18.8 kDa protein containing 175 amino acid residues, and a soluble isoform of the G-CSF receptor has been described. The pleotropic cytokine is produced by activated monocytes, macrophages, endothelial cells, fibroblasts, astrocytes, osteoblasts and bone marrow cells. G-CSF has been shown to have specific effects on the proliferation, differentiation and activation of hematopoietic cells. G-CSF is also expressed by various transformed cells such as carcinoma cells and myeloblastic leukemia cells. G-CSF is encoded by two distinct DNA sequences, resulting in a full size, high activity and a shorter, low activity isoform of G-CSF. G-CSF is highly conserved among species and has been shown to exert its biological functions through interaction with its receptor expressed on the surface of hematopoietic progenitors, neutrophilic granulocytes and certain carcinoma cell lines. Clinical use of G-CSF has been approved for several therapeutic applications, treatment of neonatal infections, therapy of acute myocardial infarction, granulocyte transfusion in patients with neutropenia, in severe infections and sepsis, therapy in chronic autoimmune neutropenia, treatment of acute myeloid leukemias, Sweet's syndrome and AIDS. Further, G-CSF has been shown to be a marker protein for different carcinomas such as bladder cancer and dysfunction of the protein has been linked to Kostmann Syndrome.
