Recombinant Human PDGF Protein

Name: Recombinant Human PDGF Protein
Brand: Beta LifeScience
SKU: BL-1249SG
Availability: InStock

Collections: All products, Buy cytokines, chemokines, and growth factors for research online, Growth factors and receptors for advanced research, High-quality recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	NP_148983
Synonym	PDGF1; PDGFA; PDGF-A
Background	PDGF is a member of the platelet-derived growth factor family which is mitogenic factors for cells of mesenchymal origin and is characterized by a motif of eight cysteines. PDGF is a cationic glycoprotein consisting of homo- or heterodimers of polypeptide chains A and/or B and a potent mitogen for connective tissue cells and exerts its function by interacting with 2 related receptor tyrosine kinases, PDGFRA and PDGFRB (1). PDGF A and B chain mRNA in mesenchymal-appearing intimal cells and endothelial cells, respectively, of atherosclerotic plaques. Moreover PDGF receptor mRNA was localized predominantly in the plaque intima (2).
Description	Recombinant human full length PDGF was produced in E. coli system and purified by proprietary chromatographic techniques.
Source	E.coli
AA Sequence	Full Length
Molecular Weight	~17 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human PDGF Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB.
Subcellular Location	Secreted. Note=Released by platelets upon wounding.
Protein Families	PDGF/VEGF growth factor family
Database References	HGNC: 8799 OMIM: 173430 KEGG: hsa:5154 STRING: 9606.ENSP00000346508 UniGene: PMID: 30340644 Hypomethylation at a CpG site in PDGFA (encoding platelet-derived growth factor alpha) and PDGFA overexpression are both associated with increased T2 diabetes risk, hyperinsulinemia, increased insulin resistance, and increased steatohepatitis risk. PMID: 29728363 PDGFA was down-regulated in the malignant Middle Cerebral Artery Infarction. PMID: 28828208 this study uncovers a novel mechanism of the Nrf2/PDGFA regulatory loop that is crucial for AKT-dependent hepatocellular carcinoma progression PMID: 27588483 Tumor cell induced mesenchymal stromal cell chemotaxis appears to be mediated through paracrine secretion of PDGF-AA. PMID: 27931212 PDGFAA in tumor drainage and HER2 in peripheral vein blood may have roles in synchronous liver metastasis of colorectal cancer PMID: 28275303 Insulin treatment caused sustained Akt activity, whereas EGF or PDGF-AA promoted transient signaling; PDGF-BB produced sustained responses at higher concentrations.Transient responses to EGF were caused by negative feedback at the receptor level, as a second treatment yielded minimal responses, whereas parallel exposure to IGF-I caused full Akt activation PMID: 27044757 these findings suggest that IGFBP-3 suppresses transcription of EGR1 and its target genes bFGF and PDGF through inhibiting IGF-1-dependent ERK and AKT activation. PMID: 27521890 Based on a luciferase reporter assay, plateletderived growth factorA (PDGFA) was identified as a direct target gene of miR375. Additionally, overexpression of PDGFA significantly reversed the effect of miR375 on cell migration and invasion in oral squamous cell carcinoma cell. PMID: 28000902 The highest PDGF AA levels were found in mothers of fetuses with hypoplastic left heart syndrome . These findings may be useful in screening for congenital heart defects (CCHDs) and offer insight into their association with nuchal translucency PMID: 28323386 Low concentration of PDGF-AB showed synergism with IFN-alpha in IFN-beta and -gamma induction. PMID: 24063997 downregulated Rab5a led to slowed cell growth, decreased numbers of migrated cells, decreased numbers of cells at the G0G1 phase and a higher apoptosis rate. However, PDGF significantly rescued these phenomena caused by siRNA against Rab5a PMID: 27666726 There are four platelet-derived growth factor (PDGF) genes (PDGFA, PDGFB, PDGFC and PDGFD) that reside on chromosomes 7, 22, 4 and 11. PMID: 28267575 TLR-stimulated pancreatic cancer cells were specifically investigated for activated signaling pathways of VEGF/PDGF and anti-apoptotic Bcl-xL expression as well as tumor cell growth. PMID: 27941651 Nox4 and Duox1/Duox2 mediate redox activation of mesenchymal cell migration by PDGF. PMID: 27110716 In contrast to platelet-derived growth factor, all urokinase isoforms induced secretion of MMP-9 by mesenchymal stromal cells. PMID: 27783304 Normalization of bone marrow microenvironment is paralleled by decreased expression of TIMP and PDGFA. PMID: 26708839 in primary cultures of glioma stemlike cells that EGR1 contributes to stemness marker expression and proliferation by orchestrating a PDGFA-dependent growth-stimulatory loop. PMID: 27002148 These findings implicate DNA hypomethylation as a specific factor in mediating overexpression of genes associated with Biliary Atresia (BA) and identify PDGFA as a new candidate in BA pathogenesis. PMID: 27010479 Human uPAR activation and its association with beta1-integrin are required for PDGF-AB-induced migration. PMID: 26420039 PDGF-AA impairs endothelium-dependent vasodilation and PDGF-AA mediates BMP4-induced adverse effect on endothelial cell function through SMAD1/5- and SMAD4-dependent mechanisms. PMID: 26769046 The development and severity of age-related cataracts was related to the secretion and expression of PDGF-alpha. PMID: 26535645 PDGF and TGFbeta1 regulate acute respiratory distress syndrome-associated lung fibrosis through distinct signaling pathway-mediated activation of fibrosis-related proteins. PMID: 26088859 Demonstrate a novel positive regulatory feedback loop between FoxM1 and the PDGF-A/AKT signaling pathway, which contributes to breast cancer cell growth and tumorigenesis. PMID: 25869208 There was evidence for the involvement of PDGF, IGF-1, and EGF in primary pulmonary hypoplasia. PDGF deficiency plays a certain role in secondary pulmonary hypoplasia PMID: 26841646 MIC-1 and PDGF-A expression is elevated in both prostate tumors and structurally intact adjacent tissues. PMID: 25767870 review elucidates the role of tumor stroma interactions, the roles of PDGF receptor signaling in cancer-associated fibroblasts via alteration of stromal matrix composition and the mitogenic effects of cancer-derived PDGFs. PMID: 23944365 Silencing the Col4-alpha1 gene or disrupting integrin engagement by blocking the antibody reduced the expression of platelet-derived growth factor A (PDGF-A), a potent chemotactic factor for fibroblasts. PMID: 25686533 our findings showed how FoxM1 activates expression of PDGF-A and STAT3 in a pathway required to maintain the self-renewal and tumorigenicity of glioma stem-like cells. PMID: 25832656 Patients with Graves ophthalmopathy had significantly higher serum levels of PDGF-AA than controls. Immunosuppressive therapy removed differences. PMID: 25140996 AVP stimulates myofibroblast proliferation and induces PDGFA secretion, implying that PDGFA mediates local myofibroblast proliferation by an autocrine feedback loop and regulates epithelial proliferation and permeability by a paracrine mechanism. PMID: 25085844 VEGF, PDGF, and TGF-beta1 concentrations in platelets may be associated with prognosis of breast cancer. PMID: 25379550 both VEGF and PDGF were significantly downregulated after completing a full CMP rush IgE desensitization. PMID: 24995287 PDGFA is a SOX11 direct target gene upregulated in MCL cells whose inhibition impaired SOX11-enhanced in vitro angiogenic effects on endothelial cells PMID: 25092176 demonstrated that PDGFRA activation supported tumor cell proliferation PMID: 24480986 PDGF positively modulates the TGF-beta-induced osteogenic differentiation of hMSCs through synergistic crosstalk between MEK- and PI3K/Akt-mediated signaling PMID: 24378341 The suppressive effects of PDGF-BB on Ca(2+) overload in neurons were more potent than those of PDGF-AA. PMID: 24454980 The mRNA expressions of the proangiogenic growth factors VEGF, PDGF, bFGF and their receptors (VEGFR1, VEGFR2, PDGFRA, PDGFRB, FGFR1, FGFR2) were measured and compared in gastric ulcers of cirrhotic patients. PMID: 23620752 our studies establish that loss of SMAD1/5 leads to upregulation of PDGFA in ovarian granulosa cells PMID: 22964636 Platelet-derived growth factor-A and vascular endothelial growth factor-C might induce intimal proliferation in pulmonary arteries and contribute to the development of pulmonary tumor thrombotic microangiopathy. PMID: 23536282 show that VEGF was down-regulated while platelet-derived growth factor-A (PDGF-A) was up-regulated when IFN-alpha treatment was re-initiated. PMID: 23025904 Findings suggest a role for brain derived neurotropic factor (BDNF) and platelet derived growth factors PDGF-AA in the patho-physiological mechanism of cerebrovascular disease in sickle cell anemia (SCA). PMID: 22704695 Results suggest that PDGFA may be used for cholangiocarcinoma prognosis and/or as diagnostic candidate marker. PMID: 22733151 Pdgf signaling potentiates Wnt2-Wnt7b signaling to promote high levels of Wnt activity in mesenchymal progenitors that is required for proper development of endoderm-derived organs, such as the lung PMID: 22949635 Significant positive correlation was seen between serum PDGF-AB & microvascular density in multiple myeloma, & between pre- & post-treatment patients. PDGF-AB plays a role in a complex cytokine network inducing bone marrow neovascularization. PMID: 21919032 Somatostatin and somatostatin analogues reduce PDGF-induced endometrial cell proliferation and motility PMID: 22588000 The kidney takes part in the elimination of IL-6 and PDGF from systemic circulation. The kidney does not take part in the elimination of TGF-beta. PMID: 22617683 analysis of astrocyte-specific expression patterns associated with the PDGF-induced glioma microenvironment PMID: 22393407 Our study was the first to show that CSF PDGF-AA is related to disease duration in relapsing-remitting multiple sclerosis. PMID: 21771201 SiO(2) may affect the expression of PDGF and synthesis of collagen through alveolar macrophage mediation and participate in the formation of lung fibrosis. PMID: 19493486

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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