Human PDGF-D Alexa Fluor® 750-conjugated Antibody Summary
Ser250-Arg370
Accession # Q9GZP0.1
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
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Preparation and Storage
Background: PDGF-D
The platelet-derived growth factor (PDGF) family consists of four disulfide-linked homodimers and one heterodimer (PDGF-AB). These proteins regulate diverse cellular functions through interactions with PDGF R alpha and R beta (1, 2). Mature PDGF-DD associates with PDGF R beta and triggers signaling through PDGF R beta homodimers and PDGF R alpha / beta heterodimers (3‑5). The human PDGF-DD cDNA encodes a 370 amino acid (aa) precursor that includes a 23 aa signal sequence, one CUB domain, and one PDGF/VEGF domain (3, 4). The PDGF/VEGF domain shares 27‑35% aa sequence identity with the corresponding regions of other PDGF family members. Human PDGF-DD shares 87% aa sequence identity with mouse and rat PDGF-DD. PDGF-DD is secreted as a100 kDa latent homodimer which is activated by proteolysis to release a 35 kDa bioactive protein containing the PDGF/VEGF homology domain (3,4,6,7). A splice variant of PDGF-DD has a 6 aa deletion near the N-terminus. A 72 aa deletion within the PDGF/VEGF domain generates an inactive protein in mouse but has not been detected in human (8). PDGF-DD is widely expressed in embryonic and adult tissues (3, 9, 10), and PDGF R beta is expressed in a generally complementary pattern (9, 11, 12). PDGF-DD functions as a growth factor for renal artery smooth muscle cells and lens epithelial cells, and as a macrophage chemoattractant (5, 9‑11). PDGF-DD is overexpressed in and contributes to several disease states, including renal and hepatic fibrosis, mesangial proliferative glomerulopathy, pulmonary lymphoid infiltration, and many cancers (6, 11‑15). PDGF-DD functions in both paracrine and autocrine manners (6, 7, 14).
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