Recombinant Human Platelet-Derived Growth Factor Receptor Beta (PDGFRB) Protein (His-GST)

Name: Recombinant Human Platelet-Derived Growth Factor Receptor Beta (PDGFRB) Protein (His-GST)
Brand: Beta LifeScience
SKU: BLC-06858P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Platelet-Derived Growth Factor Receptor Beta (PDGFRB) Protein (His-GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P09619
Target Symbol	PDGFRB
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-GST
Target Protein Sequence	GTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGFHGLRSPLDTSSVLYTAVQPNEGDNDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQDEPEPEPQLELQVEPEPELEQLPDSGCPAPRAEAEDSFL
Expression Range	901-1106aa
Protein Length	Partial
Mol. Weight	54.6 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	Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor.
Subcellular Location	Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. Note=After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.
Protein Families	Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
Database References	HGNC: 8804 OMIM: 131440 KEGG: hsa:5159 STRING: 9606.ENSP00000261799 UniGene: PMID: 28555080 Study demonstrated that LRIG2 promoted the PDGFRBinduced proliferation of glioblastoma multiforme cells in vitro and in vivo through regulating the PDGFRB signalingmediated cell cycle progression. PMID: 30015847 High expression of PDGFR-beta in prostate cancer stroma is independently associated with clinical and biochemical prostate cancer recurrence. PMID: 28233816 Study investigated the more detailed mechanism for this cis-interaction of Necl-5 with the PDGF receptor beta. Necl-5 contains three Ig-like domains and the PDGF receptor beta contains five Ig-like domains at their extracellular regions; showed that the third Ig-like domain of Necl-5 cis-interacted with the fifth Ig-like domain of the PDGF receptor beta. PMID: 29431243 Study revealed that high PDGFRbeta expression in cancer tissue was an independent marker of poor prognosis relating to recurrence in patients with colorectal cancer. PMID: 29498405 Melatonin reinforces the anticancer activity of sorafenib by downregulation of PDGFR-beta/STAT3 signaling pathway and melatonin receptor (MT)-mediated STAT3. PMID: 29953970 High GLI2 or PDGFRB expression is associated with unfavorable survival in GC patients. GLI2 can induce PDGFRB expression in GC cells via directly binding to its promoter. In addition, the GLI2-PDGFRB axis might be an important signaling pathway modulating CSC properties of GC cells. PMID: 28975979 The cell surface PDGFRB is a major link between high glucose and its effectors Hif1a and TGFB for induction of diabetic mesangial cell hypertrophy. PMID: 28951244 describes three unique PDGFRB fusions in childhood B- or T-ALL. All three PDGFRB fusion partners have previously been reported to be implicated in hematopoiesis and immune responses PMID: 28552906 These findings indicated that miR-518b may function as a tumor suppressor by targeting PDGFRB in the occurrence and development of GBM. PMID: 28849154 Data show that an equilibrium mixture of two unusual end-insertion G-quadruplexes forms in a native promoter sequence and appears to be the molecular recognition for platelet derived growth factor receptor beta (PDGFR-beta) downregulation. PMID: 29288770 Case Report: heterozygous PDGFRB mutation in a family presenting with multicentric autosomal dominant infantile myofibromatosis. PMID: 28417142 anlotinib inhibits the activation of VEGFR2, PDGFRbeta and FGFR1 as well their common downstream ERK signaling PMID: 29454091 PDGFRB is not a major causative gene of primary familial brain calcification in Chinese population. PMID: 28298627 These findings indicate that the levels of phosphorylated PDGFR-beta are decreased in endothelial progenitor cells with the in vitro expansion process, which impairs their angiogenic potential by inhibiting PI3K/Akt signaling. PMID: 28487975 This review showed that PDGFRB was one of the common gene involved included with brain calcification PMID: 28162874 Data indicate a positive association between LETM1 up-regulation, YAP1 nuclear localization and high PDGFB expression. PMID: 27556512 This is the first report of a Korean family that carries a PDGFRB mutation potentially responsible for supernumerary premolars. Our results demonstrate the power of next-generation sequencing in rapidly determining the genetic aetiology of numerical tooth abnormalities. PMID: 28393601 Genetic analyses indicated a platelet derived growth factor receptor beta (PDGFRB) gene missense heterozygous germline mutation in a newborn boy, and his sister suffered from skull base tumor with same genotype and histology. PMID: 28183292 Here we report on a special case of a Ph-like acute lymphoblastic leukemia patient who had a variant ATF7IP/PDGFRB fusion. In this case, a variant fusion was created between ATF7IP exon 9 (instead of exon 13) and PDGFRB exon 11, resulting in the loss of 411 nucleotides and 137 amino acids in the ATF7IP/PDGFRB fusion cDNA and its encoded chimeric protein, respectively. PMID: 29133777 Data show that MLLT11/AF1q-induced PDGFR signaling enhanced STAT3 activity through Src kinase activation. PMID: 27259262 In conclusion, a specific class of mutations in PDGFRB causes a clinically recognizable syndromic form of skeletal overgrowth. PMID: 28639748 Suggest the association of activation of Akt-mTOR pathway proteins and PDGFR-beta in fibrosarcomatous transformation of dermatofibrosarcoma protuberans. PMID: 28711648 High PDGFRB expression is associated with gastric cancer. PMID: 28423550 Authors identified gain-of-function PDGFRB mutations in the majority of multifocal infantile myofibromatosis cases, shedding light on the mechanism of disease development, which is reminiscent of multifocal venous malformations induced by TIE2 mutations. PMID: 28334876 findings not only confirm the important role of R853 in establishing the resistant phenotype of the mutant NDEL1-PDGFRB, but also underline the potential of protein modelling for prediction of sensitivity and resistance to TKI treatment. PMID: 27573554 A novel mutation in PDGFRB [NM_002609.3:c.1699A > G, p.Lys567Glu] was identified in infantile myofibromatosis patients. PMID: 28286173 Identify PDGFRbeta as a driver in activating Akt/mTORC1 nexus for high glucose-mediated expression of collagen I (alpha2) in proximal tubular epithelial cells, which contributes to tubulointerstitial fibrosis in diabetic nephropathy. PMID: 28424212 Higher expression of PDGFR-Beta is related to more serious dural penetration of clival chordomas. PMID: 27506406 Targeted next-generation DNA sequencing identified PDGFRB alterations in all cases of myopericytomatosis and conventional myopericytoma tested (5 cases each), including mutations in 4 cases of myopericytomatosis (N666K in 3; Y562-R565 deletion in 1 case) and 3 myopericytomas (Y562C, K653E, and splice acceptor deletion in 1 case each), as well as low-level PDGFRB amplification in 2 cases of myopericytomatosis and 4 myoperi PMID: 28505006 Elevated PDGFRB expression was noted in 20.7% of patients with papillary renal cell carcinoma. PMID: 27989785 Imatinib in myeloid/lymphoid neoplasms with eosinophilia and rearrangement of PDGFRB in chronic or blast phase PMID: 28725989 inhibition of any internalization mechanism impaired activation of STAT3 but not of other downstream effectors of PDGFRbeta. PMID: 27980069 this is the first study reporting apparently somatic recurrent PDGFRB mutations as molecular driver events in the majority of sporadic infantile and adult solitary myofibromas PMID: 27776010 results demonstrate that miR-9 and miR-200 play opposite roles in the regulation of the vasculogenic ability of triple-negative breast cancer, acting as facilitator and suppressor of PDGFRbeta, respectively PMID: 27402080 Among 15 childhood ALL patients with EBF1-PDGFRB fusion proteins, the fusion arose from interstitial deletion of 5q33 (n = 11), balanced rearrangement (n = 2), or complex rearrangement (n = 2). PMID: 26872634 Previously unrecognised associations between renal cell carcinoma survival and the absolute levels, and variability, of perivascular PDGFR-beta. PMID: 27931046 This study suggested that epithelial-mesenchymal transition process can be triggered by the PDGF-D/PDGFRb axis in tongue squamous cell carcinoma, and then involved in the tumor cell invasion via activation of p38/AKT/ERK/ epithelial-mesenchymal transition pathway. PMID: 27507215 that a loss of KAI1/CD82 and an increase in PDGFR expression in gliomas relate to a progressive tumor growth PMID: 27764516 identified PDGFRbeta as a novel marker of stromal activation in oral squamous cell carcinoma; PDGFRbeta was found to be the highest-ranking receptor protein genome-wide PMID: 27128408 PDGFR-positive myeloid neoplasms are rare. Marked leukocytosis with marked eosinophilia has been rarely described in myeloid neoplasms associated with PDGFR rearrangement. PMID: 28209946 Stromal expression of PDGFRbeta increased with increasing histologic grade of breast phyllodes tumor. PDGFR stromal positivity was associated with shorter overall survival. PMID: 27881889 The expression level of PDGFRB in glioblastoma multiforme pericytes from the microvascular proliferation was significantly higher than that in GBM tumor cells. miRNAs targeting PDGFRB were downregulated in microvascular proliferation. PMID: 26857280 PDGFRB gene rearrangement is associated with transformation from atypical chronic myeloid leukemia to chronic myelomonocytic leukemia. PMID: 26881541 Results suggested that increased bFGF upregulates the expression of PDGFRbeta and may enhance PDGFRbeta-mediated pericyte functions after brain ischemia PMID: 26569132 Data suggest that cross-talk between PDGFb-dependent beta-catenin activation and Wnt signaling increases pulmonary artery smooth muscle cell proliferation in idiopathic pulmonary arterial hypertension; proliferation is not increased in normal cells. PMID: 26787464 The KIT and PDGFRB mutations were predicted to be pathogenic using in silico analysis, whereas the ERBB2 mutation was predicted to be benign.. the patient was treated with pazopanib and achieved a partial response that lasted for 7.5 months PMID: 26483058 These molecular insights confirm that mutant PDGFRB is indeed the driver mutation in PDGFRB rearranged myeloid neoplasms, consistent with the robust treatment responses with imatinib. PMID: 26662677 PDGFs could exert their mechanism of action through an autocrine/paracrine effect on granulosa and theca cells mediated by PDGFRs. PMID: 25937181 Soluble platelet-derived growth factor receptor-beta is a biomarker of brain pericyte injury and blood-brain barrier dysfunction. PMID: 26407747

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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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