|Application ||IHC-P, WB, E|
|Other Accession||Q8CI19, Q9I946, Q9UL22|
|Calculated MW||39029 Da|
|Antigen Region||74-103 aa|
|Other Names||Platelet-derived growth factor C, PDGF-C, Fallotein, Spinal cord-derived growth factor, SCDGF, VEGF-E, Platelet-derived growth factor C, latent form, PDGFC latent form, Platelet-derived growth factor C, receptor-binding form, PDGFC receptor-binding form, PDGFC, SCDGF|
|Target/Specificity||This PDGFC antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 74-103 amino acids from the N-terminal region of human PDGFC.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PDGFC Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Cytoplasm, cytosol. Secreted. Nucleus. Cytoplasmic granule. Cell membrane. Note=Sumoylated form is predominant in the nucleus (PubMed:15247255). Stored in alpha granules in platelets (PubMed:15061151).|
|Tissue Location||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.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Platelet-derived growth factor C (PDGFC) is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. PDGFC seems to form only homodimers, where the dimers are connected by disulfide bonds. It differs from the platelet-derived growth factor alpha (PDGFA) and beta (PDGFB) in having an unusual N-terminal domain, the CUB domain.
Fang, L., et al., Arterioscler. Thromb. Vasc. Biol. 24(4):787-792 (2004). Clark, H.F., et al., Genome Res. 13(10):2265-2270 (2003). Eitner, F., et al., J. Am. Soc. Nephrol. 14(5):1145-1153 (2003). Reigstad, L.J., et al., J. Biol. Chem. 278(19):17114-17120 (2003). Zwerner, J.P., et al., Oncogene 21(24):3847-3854 (2002).
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