FGF1 Protein, Human, Recombinant
5699.38 EUR
In Stock
quantity
Produktdetaljer
Katalognummer: 544 - MBS8119946-5x1mg
Produktkategori: Företag och industri > Vetenskap och laboratorium
Gentaur
Storlek: 5x1mg
300-061
Human MesP1 Recombinant Protein
ES-cell-based cardiovascular repair requires an in-depth understanding of the molecular mechanisms underlying the differentiation of cardiovascular ES cells. A candidate cardiovascular-fate inducer is the bHLH transcription factor MesP1. As one of the earliest markers, it is expressed specifically in almost all cardiovascular precursors and is required for cardiac morphogenesis. It was shown that MesP1 is a key factor sufficient to induce the formation of ectopic heart tissue in vertebrates and increase cardiovasculogenesis by ES cells. Electrophysiological analysis showed all subtypes of cardiac ES-cell differentiation. MesP1 overexpression and knockdown experiments revealed a prominent function of MesP1 in a gene regulatory cascade, causing Dkk-1-mediated blockade of canonical Wnt-signalling. Independent evidence from ChIP and in vitro DNA-binding studies, expression analysis in wild-type and MesP knockout mice, and reporter assays confirm that Dkk-1 is a direct target of MesP1.
732.75 €
300-071
Human VEGF121 Recombinant Protein
Human Vascular Endothelial Growth Factor121 (VEGF121), a 18 kDa protein consisting of 121 amino acid residues is produced as a homodimer. VEGF is a polypeptide growth factor and a member of the platelet-derived growth factor family. It is a specific mitogen for vascular endothelial cells and a strong angiogenic factor in vivo. Two high-affinity tyrosine kinase receptors for VEGF121 have been identified, VEGFR-1 (FLT-1), and VEGFR-2 (KDR). Consistent with the endothelial cell-specific action of VEGF121, expression of both receptor genes has been found predominantly but not exclusively on endothelial cells. Expression of VEGFR-1 was also found on human monocytes, neutrophils (PMNs), bovine brain pericytes and villous and extravillous trophoblasts. In addition to its action as a mitogen it is a potent vascular permeability factor (VPF) in vivo, and a chemoattractant molecule for monocytes and endothelial cells. Five different proteins are generated by differential splicing: VEGF121, VEGF145, VEGF165, VEGF189 and VEGF206. The most abundant form is VEGF165. Whereas VEGF121 and VEGF165 are secreted proteins, VEGF145, VEGF189 and VEGF206 are strongly cell-associated. The isoforms VEGF145, VEGF165 and VEGF189 bind to heparin with high affinity. VEGF121 is apparently a homo-dimer, but preparations of VEGF show some heterogeneity on SDS gels depending on the secretion of different forms and the varying degrees of glycosylation. All dimeric forms posses’ similar biological activities but the bioavailability is very different. There is good evidence that heterodimeric molecules between the different isoforms exist and that different cells and tissues express different VEGF isoforms. The other members of this increasing growth factor family are VEGF-B, -C, -D, -E and PlGF.
418.12 €
300-071S
Human VEGF121 Recombinant Protein
Human Vascular Endothelial Growth Factor121 (VEGF121), a 18 kDa protein consisting of 121 amino acid residues is produced as a homodimer. VEGF is a polypeptide growth factor and a member of the platelet-derived growth factor family. It is a specific mitogen for vascular endothelial cells and a strong angiogenic factor in vivo. Two high-affinity tyrosine kinase receptors for VEGF121 have been identified, VEGFR-1 (FLT-1), and VEGFR-2 (KDR). Consistent with the endothelial cell-specific action of VEGF121, expression of both receptor genes has been found predominantly but not exclusively on endothelial cells. Expression of VEGFR-1 was also found on human monocytes, neutrophils (PMNs), bovine brain pericytes and villous and extravillous trophoblasts. In addition to its action as a mitogen it is a potent vascular permeability factor (VPF) in vivo, and a chemoattractant molecule for monocytes and endothelial cells. Five different proteins are generated by differential splicing: VEGF121, VEGF145, VEGF165, VEGF189 and VEGF206. The most abundant form is VEGF165. Whereas VEGF121 and VEGF165 are secreted proteins, VEGF145, VEGF189 and VEGF206 are strongly cell-associated. The isoforms VEGF145, VEGF165 and VEGF189 bind to heparin with high affinity. VEGF121 is apparently a homo-dimer, but preparations of VEGF show some heterogeneity on SDS gels depending on the secretion of different forms and the varying degrees of glycosylation. All dimeric forms posses’ similar biological activities but the bioavailability is very different. There is good evidence that heterodimeric molecules between the different isoforms exist and that different cells and tissues express different VEGF isoforms. The other members of this increasing growth factor family are VEGF-B, -C, -D, -E and PlGF.