Recombinant human PDGF CC protein is a Human Fragment protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
M V V D L N L L T E E V R L Y S C T P R N F S V S I R E E L K R T D T I F W P G C L L V K R C G G N C A C C L H N C N E C Q C V P S K V T K K Y H E V L Q L R P K T G V R G L H K S L T D V A L E H H E E C D C V C R G S T G G
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.
SCDGF, UNQ174/PRO200, PDGFC, Platelet-derived growth factor C, PDGF-C, Fallotein, Spinal cord-derived growth factor, VEGF-E
Recombinant human PDGF CC protein is a Human Fragment protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
Greater than 98% by SDS-PAGE gel and HPLC analyses.
Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.
Belongs to the PDGF/VEGF growth factor family.
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.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Endotoxin level is less than 0.1 ng per µg (1EU/µg).
Platelet-Derived Growth Factor CC (PDGF-CC) is a member of the PDGF family consisting of homodimeric and heterodimeric isoforms. PDGF-CC with a mass of approximately 44 kDa partakes in various cellular processes. It primarily expresses in fibroblasts endothelial cells and some types of neurons. PDGF-CC functions by binding to tyrosine kinase receptors specifically PDGFRαα and PDGFRαβ where it triggers intracellular signaling pathways.
PDGF-CC influences cell proliferation migration and survival particularly in the context of vascular development and remodeling. It acts as a powerful growth factor for mesenchymal cells and plays a role in embryonic development. PDGF-CC forms a functional complex after proteolytic activation which is essential for its receptor-binding capacity. This factor significantly regulates angiogenesis and wound healing processes.
PDGF-CC is integral to the PDGF signaling pathway and is involved in the PI3K/AKT signaling pathway. These pathways promote cellular growth survival and proliferation. PDGF-CC's interaction with PDGF receptors primarily PDGFRα facilitates these biological functions. In these pathways PDGF-CC interacts with other proteins such as PI3K and AKT connecting it to broader cellular response networks.
PDGF-CC has been associated with fibrotic diseases and certain cancers. Its overexpression or dysregulation can contribute to pathological fibrosis through excessive tissue repair. PDGF-CC is also linked to glioblastoma a type of brain cancer where abnormal PDGF signaling leads to tumor progression. PDGF-CC interacts with PDGFRα in these disease contexts highlighting its contribution to disease mechanisms when dysregulated.
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