Recombinant Mouse Platelet-Derived Growth Factor Subunit B (PDGFB) Protein (His), Active

Name: Recombinant Mouse Platelet-Derived Growth Factor Subunit B (PDGFB) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05922P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Platelet-Derived Growth Factor Subunit B (PDGFB) Protein (His), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined in a cell proliferation assay using BALB/c 3T3 cells is less than 40 ng/ml.
Uniprotkb	P31240
Target Symbol	PDGFB
Synonyms	Pdgfb; SisPlatelet-derived growth factor subunit B; PDGF subunit B; PDGF-2; Platelet-derived growth factor B chain; Platelet-derived growth factor beta polypeptide; Proto-oncogene c-Sis
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	C-6His
Complete Sequence	SLGSLAAAEPAVIAECKTRTEVFQISRNLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRASQVQMRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETIVTPRPVT
Expression Range	82-190aa
Protein Length	Full Length of Mature Protein
Mol. Weight	13.4 kDa
Research Area	Cancer
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm Filtered 4 mM HCl
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.
Protein Families	PDGF/VEGF growth factor family
Database References	KEGG: mmu:18591 STRING: 10090.ENSMUSP00000000500 UniGene: PMID: 28699690 The PDGFB-overexpressing murine tumors closely cluster with human proneural and mesenchymal subtypes, as well as PDGFRA-amplified at both the RNA and protein expression levels. These models can be generated in fully immunocompetent mixed or C57BL/6 genetic background mice, and therefore can easily be incorporated into preclinical studies for cancer cell-specific or immune cell-targeting drug discovery studies. PMID: 28836293 Myeloid cell-derived PDGF contributes to vascular neotissue formation by regulating macrophage apoptosis, smooth muscle cell proliferation and extracellular matrix deposition. PMID: 28524773 These results demonstrate the requirement of lymphatic endothelial cells-autonomous PDGFB expression and retention for smooth muscle cell recruitment to lymphatic vessels. PMID: 28851707 Mechanical strain stimulates vasculogenesis of embryonic stem cells by the intracellular messengers ROS, NO and calcium as well as by upregulation of angiogenesis guidance molecules and the angiogenic growth factors VEGF, FGF-2 and PDGF-BB. PMID: 27725190 PDGF-B-PDGFRbeta signaling plays a significant role in the development of adipose tissue neovascularization. PMID: 28122789 data suggest that the stronger fibrotic effect generated by Pdgfa overexpression was mediated by Pdgfralpha in cardiac interstitial mesenchymal cells PMID: 27816607 loss-of-function mutations in PDGFB or PDGFRB cause Primary Familial Brain Calcification. PMID: 26599395 High PDGFB expression is associated with liver fibrosis. PMID: 24801603 Increased expression of STAT5b + PDGFB led to increased expression of downstream STAT5b targets. PMID: 25302990 Platelets produce PDGFB to activate stellate cells and promote fibrosis in MDR2-null mice. PMID: 25173753 The endogenous levels of PDGF-BB, increases CD31(hi)endomucin(hi) vessel number and stimulates bone formation in ovariectomy mice. PMID: 25282358 These findings thus implicate a novel role of PDGF-BB in the migration of pericytes, resulting in loss of pericyte coverage from the endothelium with a subsequent breach of the blood-brain barrier PMID: 25164676 The signaling pathways of VEGF and PDGF are crucial mediators for determining proliferation of endothelial cells and oligodendrocytes in the neurohypophysis of adult mice. PMID: 24860149 Our findings demonstrate, for the first time, that Shh is involved in PDGF-BB-induced smooth muscle cell migration and recruitment of mural cells into neovessels PMID: 24472833 Tumor PDGF-BB expression levels determine dual effects of anti-PDGF drugs on vascular remodelling and metastasis. PMID: 23831851 Mutations in the gene encoding PDGF-B cause brain calcifications in humans and mice. PMID: 23913003 endothelium, via Dll4 and PDGF-BB, induces a fate switch in adjacent skeletal myoblasts PMID: 23477786 Development of the retina is severely disturbed in transgenic mice in which PDGF-B was over-expressed . PMID: 22880002 PDGF-B signaling in trophoblasts was identified as a key component of the unique placental hematopoietic microenvironment that protects hematopoietic stem cells from premature differentiation. PMID: 22387002 define a previously unidentified mechanism of PDGF-BB-induced tumor angiogenesis and provide compelling evidence for the key role of EPO in mediating PDGF-BB-induced angiogenesis, tumor growth and hematopoiesis PMID: 22138754 TGFbeta and PDGF-B have important roles in modulating myofibroblast generation in the mouse cornea after haze-associated injury. PMID: 21978952 PDGF-BB induces ASM hyperplasia and changes in lung mechanics in mice PMID: 21216974 this is the first study to connect PDGF-B-induced changes in hepatic sinusoidal transport to changes in insulin action, demonstrating a link between PDGF-B signaling and insulin sensitivity. PMID: 21673305 Data show that PDGF-B depletion by RNAi caused GICs to lose their tumor-initiating capacity. PMID: 21677873 PDGF-BB stimulates cultured cardiomyocytes to synthesize the extracellular matrix component hyaluronan via HAS2 PMID: 21200430 Overexpression of platelet-derived growth factor-B accelerates liver cancer development in chemically induced liver carcinogenesis. PMID: 20506153 PDGF-B-driven gliomagenesis can occur in the absence of the proteoglycan NG2 PMID: 20939912 a tightly regulated expression of PDGF during embryogenesis is required for normal brain development and function in mice. PMID: 20643125 PDGF has a role in induction of the synaptic plasticity gene Arc/Arg3.1 PMID: 20452974 The COL1A1-PDGFB fusion gene is the most characteristic cytogenic anomaly in DFSP. PMID: 20133221 study to examine the potential role of PDGF-B in an experimental model of peritoneal fibrosis PMID: 19896531 results show that osteoclasts regulate osteoblasts directly and suggest that PDGF BB is a key factor in bone remodeling PMID: 11811556 PDGF-B chain transformation of NIH3T3 cells requires activation of NF-kappaB PMID: 11855867 endothelium-restricted ablation of PDGF-B generates viable mice with variation in the density of pericytes throughout the CNS; data suggest that a reduction of the pericyte density is sufficient to cause retinopathy in mice PMID: 12169633 Blockade transiently delays but does not prevent fibrous cap formation in ApoE null mice PMID: 12368212 PDGF is an important effector molecule in postnatal retinal development. PMID: 12528182 retention of PDGF-B in microvessels is essential for proper recruitment and organization of pericytes and for renal and retinal function in adult mice PMID: 12897053 Endothelial and nonendothelial sources of PDGF-B regulate pericyte recruitment and influence vascular pattern formation in tumors. PMID: 14561699 PDGF-BB stimulation of fibroblast-collagen interactions is mediated by the alphavbeta3 integrin when beta1 integrin function is impaired. PMID: 14644167 In vitro cultures supporting the spontaneous generation of functional cardiac myocytes from murine BMCs demonstrated induced expression of PDGF)-A and -B. PDGF-AB enhances the generation of BMC-derived cardiac myocytes in mouse hearts. PMID: 14963008 Imatinib reduces PDGFB by treating the atherosclerosis or by an autocrine loop linking PDGF signal transduction to PDGF expression. PDGF plays a central role in the complex interplay of cytokines & growth factors leading to a vicious circle. PMID: 14988091 expression and potential role of platelet-derived growth factor-BB (PDGF-BB) and its receptor, PDGF receptor beta (PDGFR-beta), during testis cord formation PMID: 14996938 PDGF-B provides a key switch from cell death to survival induced by TNF PMID: 15735680 syngenic mice deficient of PDGF-B leading to a defect in the recruitment of perivascular cells PMID: 15838875 PDGF-BB induces phosphorylation of alphaB-crystallin via p38 MAP kinase during myocardial infarction PMID: 15907784 Our studies identify two independent negative immune regulatory pathways-PDGF-B and SOCS-that may help limit lesion expansion. PMID: 16127167 PDGF-BB and TGF-beta1 binding to intact alpha2M is specific, involving a defined region of the alpha2M subunit PMID: 16641085 platelet-derived growth factor B has a role in anti-vascular endothelial growth factor therapy in multiple models of ocular neovascularization PMID: 16723717 PDGF-B overexpression causes liver fibrosis without significantly upregulating TGF-beta1, suggesting a TGF-beta-independent mechanism. PMID: 16842882

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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.