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- Email: info@nsjbio.com
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Platelet-derived endothelial cell growth factor (PD-ECGF), also known as thymidine phosphorylase (TYMP), is a multifunctional protein that links nucleotide metabolism with angiogenic signaling. PD-ECGF was originally identified based on its ability to stimulate endothelial cell migration and proliferation, and it is now recognized as the enzymatic protein TYMP, highlighting its dual role as both a metabolic enzyme and a pro-angiogenic factor. PD-ECGF Antibody, clone rTYMP/3444, is a recombinant monoclonal antibody developed to detect this protein in studies of vascular biology, tumor progression, and metabolic regulation.
As an enzyme, TYMP catalyzes the reversible conversion of thymidine into thymine and deoxyribose-1-phosphate, contributing to the pyrimidine salvage pathway and supporting nucleotide recycling in proliferating cells. This function is particularly relevant in rapidly dividing tissues and tumors, where efficient nucleoside metabolism is required to sustain DNA synthesis and cellular growth. However, the biological significance of PD-ECGF extends beyond its enzymatic activity.
PD-ECGF promotes angiogenesis through mechanisms that are independent of its catalytic function, enhancing endothelial cell chemotaxis, survival, and vascular network formation. Increased expression of PD-ECGF has been associated with elevated microvessel density in tumors, reflecting its role in supporting neovascularization. This angiogenic activity contributes to tumor growth by facilitating oxygen and nutrient delivery, as well as by influencing the tumor microenvironment through interactions with stromal and immune cells.
In tissues, PD-ECGF is expressed in endothelial cells, macrophages, fibroblasts, and tumor epithelial cells, where it localizes predominantly to the cytoplasm in line with its enzymatic role. Its expression is often upregulated under hypoxic conditions and in response to inflammatory signaling, further linking PD-ECGF to adaptive tissue responses and pathological remodeling. These features make it a valuable marker for studying both vascular biology and disease-associated changes in tissue architecture.
The dual identity of PD-ECGF as both a metabolic enzyme and an angiogenic factor distinguishes it from many other growth-associated proteins. Detection of PD-ECGF expression provides insight into the intersection of metabolism, vascular signaling, and tumor biology, supporting the use of a PD-ECGF Antibody in investigations of angiogenesis, cancer progression, and tissue remodeling processes.
Explore our Thymidine Phosphorylase Antibody - Angiogenesis and Nucleotide Metabolism Marker (TYMP/2890R) page for a broader view of TYMP expression in metabolism and tumor-associated angiogenesis.
Optimal dilution of the PD-ECGF Antibody / Angiogenesis and Endothelial Growth Factor Marker should be determined by the researcher.
Recombinant full-length human protein was used as the immunogen for the recombinant PD-ECGF antibody.
Store the PD-ECGF antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).
PD-ECGF antibody, TYMP antibody, Thymidine phosphorylase antibody, Platelet derived endothelial cell growth factor antibody, Gliostatin antibody, clone rTYMP/3444 antibody
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