PeproTech PDGF-AA Polyclonal Antibody, PeproTech®, Invitrogen™

Description

AA Sequence of recombinant protein: SIEEAVPAV CKTRTVIYEI PRSQVDPTSA NFLIWPPCVE VKRCTGCCNT SSVKCQPSRV HHRSVKVAKV EYVRKKPKLK EVQVRLEEHL ECACATTSLN PDYREEDTGR PRESGKKRKR KRLKPT. Preparation: Produced from sera of rabbits immunized with highly pure Recombinant Human PDGF-AA. Anti-Human PDGF-AA-specific antibody was purified by affinity chromatography employing an immobilized Human PDGF-AA matrix. Sandwich ELISA: To detect Human PDGF-AA by sandwich ELISA (using 100 μL/well antibody solution) a concentration of 0.5-2.0 μg/mL of this antibody is required. This antigen affinity purified antibody, in conjunction with PeproTech Biotinylated Anti-Human PDGF-AA (500-P46Bt) as a detection antibody, allows the detection of at least 0.2-0.4 ng/well of Recombinant Human PDGF-AA. Western Blot: To detect hPDGF-AA by Western Blot analysis this antibody can be used at a concentration of 0.1-0.2 μg/mL. Used in conjunction with compatible secondary reagents the detection limit for Recombinant hPDGF-AA is 1.5-3.0 ng/lane, under either reducing or non-reducing conditions.

Platelet-derived growth factor (PDGF) was discovered as a major mitogenic factor present in serum but absent from plasma. It was found to be secreted from the alpha -granules of platelets activated during the coagulation of blood to form serum. Subsequent studies have demonstrated that PDGF is not one molecule but three, each a dimeric combination of two distinct but structurally related peptide chains designated A and B. The dimeric isoforms PDGF-AA, AB and BB are differentially expressed in various cell types and their effects are mediated through two distinct receptors, termed alpha and beta. Differences exist in isoform binding to each receptor. In general, PDGF isoforms are potent mitogens for connective tissue cells, including dermal fibroblasts, glial cells, arterial smooth muscle cells and some epithelial and endothelial cells. In addition to its activity as a mitogen, PDGF is chemotactic for fibroblasts, smooth muscle cells, neutrophils and mononuclear cells. Other reported activities for PDGF include stimulation of granule release by neutrophils and monocytes, facilitation of steroid synthesis by Leydig cells, stimulation of neutrophil phagocytosis, inhibition of natural killer (NK) cell activity, stimulation of collagen synthesis, modulation of thrombospondin expression and secretion, stimulation of collagenase activity and secretion, induction of contraction of rat aorta strips in vitro, and transient induction of T cell IL-2 secretion accompanied by a down-regulation of IL-4 and IFN-gamma production, temporary effects that may allow clonal expansion of antigen-activated B and T helper lymphocytes prior to differentiation. PDGF also appears to be ubiquitous in neurons throughout the CNS, where it is suggested to play an important role in neuron survival and regeneration, and in mediation of glial cell proliferation and differentiation.