Recombinant Human PDGF-CC (RMPP-00231562)
Cat. No.: RMPP-00231562
Category: Growth Factors & Cytokines
INQUIRY
5 μg
20 μg
The platelet-derived growth factor (PDGF) family of heparin-binding growth factors consists of five known members, denoted PDGF-AA, PDGF-BB, PDGF-AB, PDGF-CC and PDGF-DD. The mature and active form of these proteins, an anti-parallel, disulfide-linked dimer of two 12-14 kDa, polypeptide chains, is obtained thro μgh proteolytic processing of biologically inactive precursor proteins, which contain an N-terminal CUB domain and a PDGF/VEGF homologous domain. The PDGFs interact with two related protein tyrosine kinase receptors, PDGFR-α and PDGFR-β, and are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and certain tumor cells. They play an important role in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubules' epithelial cell development. Mature PDGFs are stored in platelet α-granules, and are released upon platelet activation. PDGF-AA, -AB, -BB and –CC signal primarily thro μgh the PDGFR-α receptor, whereas PDGF-DD interacts almost exclusively with the PDGFR-β receptor. Recombinant Human PDGF-CC is a 25.0 kDa protein consisting of two identical disulfide-linked, 112 amino acid, polypeptide chains.
Product Features
| Source | E.coli |
|---|---|
| Purity | ≥ 98% by SDS-PAGE gel and HPLC analyses. |
| Nature | Recombinant |
| Endotoxin Level | < 1 Eu/μg |
| Cross Reactivity | Human, Mouse |
Protein Information
| UniProt ID | Q9NRA1 |
|---|---|
| Molecular Weight | 25 kDa |
| Sequence | MVVDLNLLTE EVRLYSCTPR NFSVSIREEL KRTDTIFWPG CLLVKRCGGN CACCLHNCNE CQCVPSKVTK KYHEVLQLRP KTGVRGLHKS LTDVALEHHE ECDCVCRGST GG |
| Sequence Similarities | Belongs to the PDGF/VEGF growth factor family. Contains 1 CUB domain. |
| Protein Length | Full length protein |
| Cellular Localization | Cytoplasm. Secreted. Nucleus. Cytoplasmic granule. Sumoylated form is predominant in the nucleus. Stored in alpha granules in platelets. Membrane associated when bound to receptors. |
| Tissue Specificity | Expressed 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. |
| Developmental Stage | In the fetal kidney, detected in the developing mesangium, ureteric bud epithelium and the undifferentiated mesenchyme (at protein level). |
| Function | Potent 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. |
| Post-translational Modifications | Proteolytic 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. |
Storage & Shipping
| Shipping and Storage | Shipped on Dry Ice. |
|---|
For research use only. Not for clinical use.
