|Detection of Mouse PD-ECGF/Thymidine Phosphorylase by Western Blot. Western blot shows lysates of L1210 mouse lymphocytic leukemia cell line. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Mouse PD‑ECGF/Thymidine Phosphorylase Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7568) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for PD‑ECGF/Thymidine Phosphorylase at approximately 50 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
TYMP (Thymidine phosphorylase/TP; also [PD]-ECGF/platelet-derived endothelial cell growth factor, gliostatin and TdRPase) is a 50-55 kDa member of the pyrimidine-nucleoside phosphorylase family of enzymes. TYMP/TP is both a cytosolic and secreted molecule that is expressed by a variety of cell types, including, macrophages, hepatocytes, endometrial gland epithelium, vascular smooth muscle and endothelial cells. It has also been found in select tumor cell types, and via an angiogenic activity, has been proposed to promote tumor growth. TYMP converts thymidine to thymine and 2-deoxy-ribose-1P, and it is the 2-deoxy-ribose component that is believed to promote endothelial cell migration (but not proliferation). This may be due to the fact that 2-deoxy-ribose induces reactive oxygen species, which drive the production of angiogenic factors, and that 2-deoxy-ribose also activates endothelial cell integrins. Mouse TYMP is 471 amino acids (aa) in length. It contains a phosphorylase domain (aa 96-348), followed by a C-terminal region (aa 374-448). Although TYMP circulates, there is no definitive signal sequence. TYMP is known to form homodimers. Full-length mouse TYMP (aa 1-471) shares 80% and 92% aa sequence identity with human and rat TYMP, respectively.
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