The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Purity70 - 90% by HPLC.
- First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions. - If the peptide doesn’t dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer. - Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent. - Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised. - Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Information available upon request.
PDGFC latent form
PDGFC receptor-binding form
Platelet derived growth factor C
Platelet-derived growth factor C, receptor-binding form
Secretory growth factor like protein
Secretory growth factor like protein fallotein
Spinal cord derived growth factor
Spinal cord-derived growth factor
FunctionPotent mitogen and chemoattractant for cells of mesenchymal origin. Binding of this growth factor to its affinity receptor elicits a variety of cellular responses. Appears to be involved in the three stages of wound healing: inflammation, proliferation and remodeling. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. Acts as a specific ligand for alpha platelet-derived growth factor receptor homodimer, and alpha and beta heterodimer. Binding to receptors induces their activation by tyrosine phosphorylation. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintainance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function. Seems to be involved in palatogenesis.
Tissue specificityExpressed in the fallopian tube, vascular smooth muscle cells in kidney, breast and colon and in visceral smooth muscle of the gastrointestinal tract. Highly expressed in retinal pigment epithelia. Expressed in medulloblastoma. In the kidney, constitutively expressed in parietal epithelial cells of Bowman's capsule, tubular epithelial cells and in arterial endothelial cells (at protein level). Highly expressed in the platelets, prostate, testis and uterus. Higher expression is observed in uterine leiomyomata. Weaker expression in the spleen, thymus, heart, pancreas, liver, ovary cells and small intestine, and negligible expression in the colon and peripheral blood leukocytes.
Sequence similaritiesBelongs to the PDGF/VEGF growth factor family. Contains 1 CUB domain.
Developmental stageIn the fetal kidney, detected in the developing mesangium, ureteric bud epithelium and the undifferentiated mesenchyme (at protein level).
Post-translational modificationsProteolytic removal of the N-terminal CUB domain releasing the core domain is necessary for unmasking the receptor-binding epitopes of the core domain. Cleavage after basic residues in the hinge region (region connecting the CUB and growth factor domains) gives rise to the receptor-binding form. Cleaved by PLAT and PLG. Sumoylated by SUMO1. N-glycosylated.
Cellular localizationCytoplasm. Secreted. Nucleus. Cytoplasmic granule. Sumoylated form is predominant in the nucleus. Stored in alpha granules in platelets. Membrane associated when bound to receptors.