| 货号 | MAB1560-500 |
| 别名 | FALLOTEIN; PDGF-C; platelet derived growth factor C; platelet-derived growth factor C; SCDGFSpinal cord-derived growth factor; secretory growth factor-like protein; VEGF-E | 全称 | Platelet-derived Growth Factor C |
| 反应种属 | Human |
| 应用 | Neutralization |
| 目标/特异性 | Detects human PDGF-C in direct ELISAs. In direct ELISAs, 100% cross-reactivity withrecombinant mouse PDGF-CC is observed, and no cross-reactivitywith recombinant human (rh) PDGF-AA, rhPDGF-AB, rhPDGF-BB, rhPDGF-D, orrecombinant rat PDGF-AB is observed. |
| 使用方法 | Neutralization: Measured by its ability to neutralize PDGF‑CC -induced proliferation in the NR6R‑3T3 mouse fibroblast cell line [Raines, E.W. et al. (1985) Methods Enzymol. 109:749]. The Neutralization Dose (ND50) is typically 0.6-3 ug/ml in the presence of 1 ug/mL Recombinant Human PDGF‑C (Catalog # 1687-CC). |
| 来源 | Monoclonal Mouse IgG2B Clone # 619346 |
| 产品组分 |
| 供应商 | R&D Systems |
| Entrez Gene IDs | 56034 (Human); 54635 (Mouse) |
| 纯化方式 | Protein A or G purified from hybridoma culture supernatant |
| 免疫原 | E.coli-derived recombinant human PDGF-C Val235-Gly345 Accession # Q9NRA1 |
| 内毒素水平 | <0.10 EU per 1 μg of the antibody by the LAL method. |
| 生物活性 | Human |
| 标记 | Unconjugated |
| 溶解方法 | Sterile PBS to a final concentration of 0.5 mg/mL. |
| 背景 | The platelet-derived growth factor (PDGF) family consists of proteins derived from four genes (PDGF-A, -B, -C, and -D) that form four disulfide-linked homodimers (PDGF-AA, -BB, -CC, and -DD) and one heterodimer (PDGF-AB) (1). These proteins regulate diverse cellular functions by binding to and inducing the homo- or hetero‑dimerization of two receptor tyrosine kinases (PDGF R alpha and R beta ). Within the PDGF family, PDGF-C and PDGF-D constitute a subgroup that shares similar structural organization (2, 3). Both proteins are secreted as inactive homodimeric latent growth factors. Each monomer has two distinct protein domains: an N-terminal CUB domain; and a C-terminal PDGF/VEGF homology domain that shares 27‑35% sequence identity with the corresponding regions of other PDGF family members. An 80‑90 amino acid residue hinge region connects the two domains. Sequential removal of the CUB domains in the homodimeric latent growth factor by extracellular proteolytic cleavage at the hinge region is required to release the bioactive PDGF/VEGF homology domain(1). Twelve cysteine residues are found within the PDGF/VEGF homology domain of PDGF-C, including the characteristic eight invariant cysteine residues involved in inter- and intra-chains disulfide-bonds needed for the formation of the cysteine-knot structure. Bioactive PDGF-CC binds with high-affinity to PDGF R alpha but not PDGF R beta and activates PDGF R alpha homodimerization (1). PDGF-CC has also been shown to activate PDGF R alpha beta heterodimers (1). PDGF-CC is expressed in multiple embryonic and adult cell types and tissues. During embryonic development, PDGF-CC is involved in ductal morphogenesis (4). PDGF-CC is a potent angiogenic factor that stimulates vessel growth in the mouse cornea pocket assay and in the CAM assay (5). It stimulates coronary artery smooth muscle cell proliferation and may play an important role in cardiovascular development and function (6). PDGF-CC is also expressed in many tumors and tumor cell lines and has a causative role in tumorigenesis (7). Mature human and mouse PDGF-C share 93.7% amino acid sequence identity. |
| 运输条件 | Blue Ice |
| 存放说明 | -20℃ |
| 参考文献 |
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Proliferation Induced by PDGF‑CC and Neutralization by Human PDGF‑C Antibody. Recombinant Human PDGF‑CC (Catalog # 1687-CC) induces proliferation in the NR6R‑3T3 mouse fibroblast cell line in a dose-dependent manner (orange line), as measured by Resazurin (Catalog # AR002). Proliferation elicited by Recombinant Human PDGF‑CC (1 ug/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Human PDGF‑C Monoclonal Antibody (Catalog # MAB1560). The ND50 is typically 0.6-3 ug/ml. |
