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Product Overview

Clone: SPM322

In the presence of inorganic orthophosphate, it catalyzes the reversible phospholytic cleavage of thymidine and deoxyuridine to their corresponding bases and 2 deoxyribose-1-phosphate. It is both chemotactic and mitogenic for endothelial cells and a non-heparin binding angiogenic factor present in platelets. Its enzymatic activity is crucial for angiogenic activity (metabolite is angiogenic). Higher levels of serum TP/PD-ECGF are observed in cancer patients. It is also involved in transformation of fluoropyrimidines, cytotoxic agents used in the treatment of a variety of malignancies, into active cytotoxic metabolites (e.g. 5 -deoxy-5-fluorouridine to 5-FU). High intra-cellular levels of TP/PD-ECGF are associated with increased chemosensitivity to such antimetabolites.

Specifications

Species

Mouse.

Immunogen

Recombinant full-length human Thymidine Phosphorylase (TP / PD-ECGF) protein.

Clone

SPM322.

Isotype:

IgG1.

Species Reactivity

Reacts with human, mouse, and rat. Others not known.

Positive Control

HUVEC cells. Breast, bladder, lung, or Kaposi Tumors.

Specificity

Recognizes a protein of 55kDa (in vivo 110kDa homodimer), identified as platelet-derived endothelial growth factor (PD-ECGF), same as thymidine phosphorylase (TP) or gliostatin.

Cellular Localization

Cytoplasmic and Nuclear.

Ordering Information

Format:

Volume:

  • Classification
  • RUO
  • Catalogue Number
  • G0574RP