Recombinant Human PDGF-AA Protein (N-6His)

Beta LifeScience SKU/CAT #: BL-0285NP
BL-0285NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-0285NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human PDGF-AA Protein (N-6His)

Beta LifeScience SKU/CAT #: BL-0285NP
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Product Overview

Description Recombinant Human Platelet-derived Growth Factor AA is produced by our E.coli expression system and the target gene encoding Ser87-Thr211 is expressed with a 6His tag at the N-terminus.
Accession P04085
Synonym PDGFAA; PDGF-AA
Gene Background Platelet-derived growth factor subunit A (PDGFA), belongs to the PDGF/VEGF growth factor family. PDGFA is a secreted protein, stored in platelet alpha-granules and released by platelets upon wounding. PDGFA is potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. It plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. PDGFA is required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis, normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. It plays an important role in wound healing; Signaling is modulated by the formation of heterodimers with PDGFB.
Molecular Mass 15.9 KDa
Apmol Mass 16 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of 4mM HCl.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in 4mM HCl.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

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

Gene Functions References

  1. High PDGF expression is associated with cardiac fibrosis. PMID: 30340644
  2. 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
  3. PDGFA was down-regulated in the malignant Middle Cerebral Artery Infarction. PMID: 28828208
  4. this study uncovers a novel mechanism of the Nrf2/PDGFA regulatory loop that is crucial for AKT-dependent hepatocellular carcinoma progression PMID: 27588483
  5. Tumor cell induced mesenchymal stromal cell chemotaxis appears to be mediated through paracrine secretion of PDGF-AA. PMID: 27931212
  6. PDGFAA in tumor drainage and HER2 in peripheral vein blood may have roles in synchronous liver metastasis of colorectal cancer PMID: 28275303
  7. 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
  8. 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
  9. 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
  10. 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
  11. Low concentration of PDGF-AB showed synergism with IFN-alpha in IFN-beta and -gamma induction. PMID: 24063997
  12. 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
  13. 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
  14. 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
  15. Nox4 and Duox1/Duox2 mediate redox activation of mesenchymal cell migration by PDGF. PMID: 27110716
  16. In contrast to platelet-derived growth factor, all urokinase isoforms induced secretion of MMP-9 by mesenchymal stromal cells. PMID: 27783304
  17. Normalization of bone marrow microenvironment is paralleled by decreased expression of TIMP and PDGFA. PMID: 26708839
  18. 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
  19. 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
  20. Human uPAR activation and its association with beta1-integrin are required for PDGF-AB-induced migration. PMID: 26420039
  21. 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
  22. The development and severity of age-related cataracts was related to the secretion and expression of PDGF-alpha. PMID: 26535645
  23. PDGF and TGFbeta1 regulate acute respiratory distress syndrome-associated lung fibrosis through distinct signaling pathway-mediated activation of fibrosis-related proteins. PMID: 26088859
  24. 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
  25. 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
  26. MIC-1 and PDGF-A expression is elevated in both prostate tumors and structurally intact adjacent tissues. PMID: 25767870
  27. 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
  28. 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
  29. 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
  30. Patients with Graves ophthalmopathy had significantly higher serum levels of PDGF-AA than controls. Immunosuppressive therapy removed differences. PMID: 25140996
  31. 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
  32. VEGF, PDGF, and TGF-beta1 concentrations in platelets may be associated with prognosis of breast cancer. PMID: 25379550
  33. both VEGF and PDGF were significantly downregulated after completing a full CMP rush IgE desensitization. PMID: 24995287
  34. 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
  35. demonstrated that PDGFRA activation supported tumor cell proliferation PMID: 24480986
  36. PDGF positively modulates the TGF-beta-induced osteogenic differentiation of hMSCs through synergistic crosstalk between MEK- and PI3K/Akt-mediated signaling PMID: 24378341
  37. The suppressive effects of PDGF-BB on Ca(2+) overload in neurons were more potent than those of PDGF-AA. PMID: 24454980
  38. 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
  39. our studies establish that loss of SMAD1/5 leads to upregulation of PDGFA in ovarian granulosa cells PMID: 22964636
  40. 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
  41. 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
  42. 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
  43. Results suggest that PDGFA may be used for cholangiocarcinoma prognosis and/or as diagnostic candidate marker. PMID: 22733151
  44. 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
  45. 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
  46. Somatostatin and somatostatin analogues reduce PDGF-induced endometrial cell proliferation and motility PMID: 22588000
  47. 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
  48. analysis of astrocyte-specific expression patterns associated with the PDGF-induced glioma microenvironment PMID: 22393407
  49. Our study was the first to show that CSF PDGF-AA is related to disease duration in relapsing-remitting multiple sclerosis. PMID: 21771201
  50. 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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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