Recombinant Human Platelet-Derived Growth Factor Subunit B (PDGFB) Protein (His-SUMO)

Name: Recombinant Human Platelet-Derived Growth Factor Subunit B (PDGFB) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-07892P
Price: 240.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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100ug

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Product Overview

Description	Recombinant Human Platelet-Derived Growth Factor Subunit B (PDGFB) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P01127
Target Symbol	PDGFB
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	SLGSLTIAEPAMIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQLRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETVAAARPVT
Expression Range	82-190aa
Protein Length	Full Length of Mature Protein
Mol. Weight	28.3 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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 proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA.
Subcellular Location	Secreted. Note=Released by platelets upon wounding.
Protein Families	PDGF/VEGF growth factor family
Database References	HGNC: 8800 OMIM: 190040 KEGG: hsa:5155 STRING: 9606.ENSP00000330382 UniGene: PMID: 29168174 Treating HepG2 cells with hepatotoxicants resulted in a significant increase in mRNA expression of platelet-derived growth factor BB (PDGF-BB) and transforming growth factor beta (TGFbeta). PMID: 29558627 The morphology and immunophenotype of all 6 cases was analogous to those with the canonical COL1A1-PDGFB fusion; none of the cases showed fibrosarcomatous transformation. This study illustrates that the COL6A3-PDGFD fusion product is rare in dermatofibrosarcoma protuberans, and associated with an apparent predilection for breast PMID: 30014607 PDGF-B expression was found in ovarian tumor microvessels in 72% of cases. High expression of PDGF in pericapillary cells was strongly associated with high expression of this marker in cancer cells. Significant correlations between PDGF-B and nestin expression in malignant tumor microvessels were also found. PMID: 28397199 SOX7 transcription factor mediates PDGF-BB-induced IL-33 expression. PMID: 27150562 High expression of PDGF-BB may be involved in the pathogenesis of Graves' disease. CCR2-positive macrophages may induce the expression of PDGF-BB through HIF-1alpha signal. PMID: 29319128 rhPDGF-BB promoted the proliferation of hADSCs via miR-363/PI3K/Akt pathway, indicating that rhPDGF-BB combined with ADSCs could treat Achilles tendinitis via miR-363/PI3K/Akt pathway. PMID: 28766166 This study identifies the mbPDGF-BB in cell derived extracellular vesicles as a relevant mediator of diabetes-associated vascular smooth muscle cell resistance to apoptosis. PMID: 29386225 This review showed that PDGFB was one of the common gene involved included with brain calcification. PMID: 28162874 Rare Skin Tumor Dermatofibrosarcoma Protuberans (DFSP) is characterized by the translocation of the PDGFB gene to the collagen 1A1 gene. PMID: 28940884 Transglutaminase type 2 affects cell migration through post-translational modification of PDGF-BB. PMID: 27633721 PDGF-B rs1800818 polymorphism might play a role in mediating the susceptibility to severe fever with thrombocytopenia syndrome in Chinese individuals. PMID: 27147565 PDAP-1 as an effecter of PDGF signaling in glioma cells PMID: 27448842 High PDGFB expression is associated with gastric cancer. PMID: 28423550 We observed that regenerating and necrotic muscle fibers in muscle biopsy samples from Duchenne muscular dystrophy patients expressed PDGF-BB. PMID: 28618254 Elevated PDGFB expression was noted in 29% of patients with papillary renal cell carcinoma. PMID: 27989785 high-throughput affinity plasma proteomic profiling is a valuable research strategy to identify potential candidate biomarkers for thrombosis-related disorders, and our study suggests a novel association of PDGFB plasma levels with venous thromboembolism. PMID: 27742707 High PDGFB expression is associated with glioma. PMID: 26951930 A cell-autonomous positive-signaling circuit is associated with the PDGF-NO-ID4-regulatory axis in glioblastoma cells. PMID: 28327358 SphK1 is regulated by PDGF-BB in pulmonary artery smooth muscle cells via the transcription factor Egr-1, promoting cell proliferation. PMID: 27099350 PDGF-BB regulates the proliferation and differentiation of human melanocytes in a differentiation-stage-specific manner. PMID: 27289338 this study shows that the expression of PDGFB is significantly downregulated in keloid fibroblasts compared to normal human fibroblasts PMID: 27465069 this study demonstrated that knockdown of SCARA5 inhibits PDGFBBinduced HASMC proliferation and migration through suppression of the PDGF signaling pathway. PMID: 27035566 The simultaneous action of PDGF-B/PDGFRbeta and VEGF165b on the same type of receptor may explain the resistance to antiangiogenic therapy, which depends on the degree of modulation of PDGFRbeta phosphorylation. PMID: 27127135 The expression of angiogenesis markers VEGF-A, VEGFR, PDGFbetabeta, PDGFR, CCND1 and CA9 was assessed by immunohistochemistry and correlated with overall survival and progression-free survival in patients with renal cell carcinoma undergoing therapy with Sunitinib, but no correlation was found between expression of angiogenesis markers and clinical outcome. PMID: 28011500 ore than 65% of cases had PDGF-BB mRNA amplification, confirming immunohistochemical results. We herein validated PDGF-BB as a potential therapeutic and prognostic tool of ovarian cancer aggressiveness. PMID: 27807074 Case Report: congenital atrophic dermatofibrosarcoma protuberans with COL1A1-PDGFB rearrangement. PMID: 26932148 Placental endothelial cell-derived PDGF-BB recruits human placental multipotent mesenchymal stromal cells involved in vascular development via PDGFR-beta/STAT3 activation PMID: 26353894 Suggest that PDGF-B signaling may play a role in endothelial and cardiomyocyte recovery from ischemia reperfusion injury after heart transplantation. PMID: 26371596 Lessons from SLC20A2, PDGFB, and PDGFRB mutation carriers. Three causative genes have been identified: SLC20A2, PDGFRB and, recently, PDGFB, whose associated phenotype has not yet been extensively studied. PMID: 26129893 loss-of-function mutations in PDGFB or PDGFRB cause Primary Familial Brain Calcification. PMID: 26599395 Three factor model revealed significant gene-gene interaction for PDGFB +286A>G, PDGFB +1135A>C and HER2 Ile165Val SNPs with GBC. Protein-protein interaction showed significant association of PDGFB and HER2 with EGFR receptor signaling pathway. PMID: 26320430 Regulation of Hyaluronan (HA) Metabolism Mediated by HYBID (Hyaluronan-binding Protein Involved in HA Depolymerization, KIAA1199) and HA Synthases in Growth Factor-stimulated Fibroblasts. PMID: 26518873 Electron microscopy structure of PDGFRB [a full-length human platelet-derived growth factor receptor], in complex with its ligand PDGF-B. PMID: 26463591 TM expression in corneal epithelium was modulated during the corneal wound healing process, and may be regulated by PDGF-BB. In addition, rTMD23 has therapeutic potential in corneal injury PMID: 25816372 Our results demonstrated that PDGF-B tumor growth and progression in clear cell renal cell carcinoma PMID: 25766258 PDGFB and IL18R1 represent plausible candidates for studying the pathophysiology of these disorders in the context of TLR4 activation PMID: 25327457 TAZ promotes neuroblastoma cell proliferation and tumorigenicity through up-regulating the expression of PDGF-beta genes. PMID: 25940705 Phloretin inhibits PDGF-BB-induced thoracic aorta smooth muscle cell proliferation and migration. PMID: 25945863 COL1A1-PDGFbeta translocation is specific to dermatofibrosarcoma protuberans. Platelet-derived growth factor may have acted in an autocrine manner to cause cell division, which may have led to the development of dermatofibrosarcoma protuberans PMID: 25924890 the present study, demonstrated for the first time, to the best of our knowledge, that ligustrazine downregulated PDGF-BB-induced VSMC proliferation and migration partly, at least, through inhibiting the activation of the ERK and P38 MAPK signaling. PMID: 25738255 cytoplasmic expression of VEGF, VEGFR2, PDGF-B, and PDGFR-beta in RCC tumour cells is different in various pathologic stage and cell type. Notably, VEGF and PDGF-B expression are higher in papillary than in clear cell renal cell carcinoma. PMID: 25550804 COL1A1-PDGFB is a useful and accurate tool in diagnosing DFSP[ Dermatofibrosarcoma protuberans ] in Koreans. PMID: 25683993 Significant diurnal variations in platelet counts and TGF-b1 and PDGF-BB levels were not observed in platelet-rich plasma. PMID: 24878758 Report lowered PDGF-BB levels in acute pancreatitis and increased PDGF-BB levels in chronic pancreatitis. PMID: 25278706 rhPDGF-BB delivery on a collagen scaffold enhanced cellular proliferation and angiogenesis during the early phase of healing after rotator cuff repair. PMID: 25349036 The mutation of PDGFB cause primary familial brain calcifications. PMID: 25212438 Gain of PDGFB is associated with response to therapy in metastatic renal cell carcinoma. PMID: 24524969 These results suggest that PDGF-BB promotes pulmonary artery smooth muscle cells proliferation and survival, which is likely to be mediated via the JNK pathway. PMID: 24804810 PDGFB hypomethylation is a favourable prognostic biomarker in primary myelofibrosis. PMID: 25498506

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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.

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