Recombinant Human PlGF Protein

Name: Recombinant Human PlGF Protein
Brand: Beta LifeScience
SKU: BL-1696SG
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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	N/A
Host Species	Human
Accession	P49763
Synonym	PGF, PGLF
Background	Human PlGF, or Placental Growth Factor, is part of the PDGF/VEGF family and contains the 8 cysteine residues conserved in the family. It can be alternately spliced into three different mature forms. PGF is typically found as a disulfide linked dimer which is highly glycosylated. It is a key molecule involved in vasculogenesis and angiogenesis, especially during embryogenesis. It also induces the activation of monocytes, as well as their migration and production of inflammatory cytokines. It is primarily expressed by the placental trophoblast during pregnancy, but is also expressed in villious trophoblasts, decidual cells, erythroblasts, keratinocytes, and somewhat in endothelial cells. PGF signals by binding VEGF R1, and competes with VEGF for binding. Recombinant PlGF is a 15.0 kDa protein.
Description	Recombinant Human PlGF was produced in E. coli. This protein is purified with our unique purification methods.
Source	E.coli
Molecular Weight	15.0 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 PlGF 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 active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. It binds to the receptor FLT1/VEGFR-1. Isoform PlGF-2 binds NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent manner. Also promotes cell tumor growth.
Subcellular Location	Secreted. Note=The three isoforms are secreted but PlGF-2 appears to remain cell attached unless released by heparin.
Protein Families	PDGF/VEGF growth factor family
Database References	HGNC: 8893 OMIM: 601121 KEGG: hsa:5228 STRING: 9606.ENSP00000451040 UniGene: PMID: 28714317 sFlt-1/PLGF was positively correlated with the severity of preterm preeclampsia. PMID: 30177039 The relationship between PlGF and preeclampsia differed in women with obesity according to gestational diabetes status, which may suggest different mechanistic pathways to preeclampsia. PMID: 30177064 A contingent strategy of measuring the sFlt-1/PlGF ratio at 24-28weeks in women previously selected by clinical factors and uterine artery Doppler enables an accurate prediction of preeclampsia/fetal growth restriction. PMID: 30177066 modest correlation of serum-free PlGF-1 with placental volume and uterine artery Doppler pulsatility index PMID: 28714779 PGF expression may have a role in lymphatic invasion, poorer response to chemotherapy and unfavorable prognosis of patients with serous epithelial ovarian cancer PMID: 29643276 A single measurement of sFlt-1/PlGF ratio at third trimester to predict pre-eclampsia and intrauterine growth retardation occurring after 34weeks of pregnancy. PMID: 29674192 The levels of sFlt-1, PlGF, and the sFlt-1/PlGF ratio in pre-eclamptic women with an onset at < 32 weeks were sig- ni fi cantly di ff erent from those in women with an onset at >/=32-33 weeks. PMID: 29674208 In urban Mozambican women with symptoms and/or signs suggestive of preeclampsia, low maternal plasma PlGF concentrations are associated with increased risks of adverse pregnancy outcomes, especially early delivery and stillbirth. PMID: 29523269 An sFlt-1:PlGF ratio above 655 is not predictive of impaired perinatal outcomes, and insufficiently reliable for predicting outcomes in cases with clinical signs of preeclampsia. PMID: 29523274 The maternal sFlt-1 to PlGF ratio in women with hypertensive disorders in pregnancy carries prognostic value for the development of preeclampsia. PMID: 29523275 Lower umbilical cord PlGF levels are associated with lower birth weight, deviating fetal growth patterns, and a higher odds of fetal growth retardation. PMID: 28926825 Data suggest that circulating PGF levels fall by nearly one quarter during term labor (but not during elective caesarean section). PMID: 29277266 The cross-talk between tumor-associated macrophages and NSCLC cells via PLGF/Flt-1 and TGFbeta receptor signaling may promote the growth and vascularization of NSCLC. PMID: 29991059 PlGF level showed an inversely proportional effect on the foetal weight. PMID: 28326518 Recombinant hPlGF-2 significantly improved contractile function and reduced LV end-systolic and end-diastolic volume indices with a concomitant increase in capillary and arteriolar density in ischemic myocardium, without aggravating atherosclerosis. PMID: 28397162 these data suggest that PlGF may increase non-small cell lung cancer metastasis through SRp40-mediated mRNA splicing of VEGF. PMID: 28861767 The present study investigated the interplay of VEGF-A165a isoform, the anti-angiogenic VEGF-A165b, placental growth factor (PIGF) and their receptors, VEGFR1 and VEGFR2, on junctional occupancy of VE-cadherin and macromolecular leakage in human endothelial monolayers and the perfused placental microvascular bed. PMID: 29054861 PIGF enhances TLR-signaling upstream of IKK and contributes to an exaggerated pathologic pro-inflammatory state in response to activation of maternal and fetal mononuclear phagocytes by specific TLR agonists PMID: 28635072 Lower PIGF and higher PAPP-A and free beta-hCG levels were found in the fetal circulation of near-term severe preeclamptic pregnancies PMID: 27809614 The early variations of PIGF and soluble fms-like tyrosine kinase-1 concentrations in newly pregnant obstetric antiphospholipid syndrome (oAPS) may help to detect patients at low risk of placenta-mediated complications (PMC). PMID: 28126966 There is a significant negative correlation between the concentration of sFLt-1 and PIGF in normal pregnancy. PMID: 26434493 knockdown of PIGF in spheroid body cells derived from two gastric cancer cell lines reduced in vitro tumorigenicity and stemness properties of spheroid body cells such as self-renewal ability, colony forming, migratory, and MMPs activities and decreased ability to differentiation and angiogenesis PMID: 27735991 Data showed that sFlt-1/PIGF ratio increases with volume overload and persistent hypoxia after surgery with CHD. PMID: 25388629 Glioma cell-released PIGF can induce Bregs to suppress CD8(+) T cell activities. PMID: 25450457 VEGF/PIGF levels were higher in neonates exposed to pre-eclampsia, and there was a significant negative correlation between birth weight and VEGF/PIGF levels. PMID: 25354293 In chronic kidney patients not yet on dialysis, higher serum level of PIGF are associated with increased mortality, but not cardiovascular events. PMID: 25128974 Soluble flt1 is increased in preeclampsia and is associated with decreased levels of bioactive PIGF. PMID: 24166749 In high-risk patients the sFlt1/PIGF ratio can be used for an individual risk assessment with regard to PE, HELLP syndrome or IUGR. Serial measurements permit a risk-adapted prenatal care of these patients PMID: 24595913 Gene expression revealed up-regulation of pro-angiogenic (PGF), anti-apoptotics (BAG-1, BCL-2), heart development (TNNT2, TNNC1) and extracellular matrix remodelling (MMP-2, MMP-7) genes in SM. PMID: 18805052 In contrast to the effects of hypoxia on PIGF expression in other cells, hypoxia suppresses transcription of PIGF in trophoblasts. Regulation of PIGF transcription under hypoxic conditions is independent of HIF-1. PMID: 19712973 Antibodies to PIGF may possibly be used as angiogenesis inhibitors. PMID: 18466718 Human donor myocardium and biopsies from allografts without fibrin deposits express PIGF. PMID: 19201345 anlalysis of levels of circulating PIGF, SDF-1 and sVCAM-1 in patients with systemic lupus erythematosus PMID: 17964973 These data suggest that mechanical stretch of bronchial airway epithelial cells induces iNOS expression and induces PIGF release in an erk1/2 activation-dependent manner. PMID: 17028267 Neither the hyperpermeability in response to simultaneous stimulation of VEGFR-1 and VEGFR-2 nor VEGFR-1-mediated severe inflammation was associated with VEGF-E(NZ7)/PIGF-induced angiogenesis. PMID: 16794222 Overexpression of VEGF but not PIGF exacerbated the lipopolysaccharide-mediated toxic effects, supporting a pathophysiological role for VEGF in mediating the sepsis phenotype. PMID: 16702604 Therapeutically administered human PIGF-1 demonstrates a desirable biological activity for promoting the growth of functionally relevant vasculature in mice. PMID: 16702473 IL-17A, IL-17B, IL-17F and IL-23 in systemic lupus erythematosus patients were examined and the correlation between levels of the investigated cytokines and VEGF, PIGF, as well as number of endothelial cells, was investigated. PMID: 23661335 Maternal serum sFlt-1 and PlGF are markedly decreased in threatened miscarriage patients. PMID: 21448460 High PlGF and/or low sFlt-1/PlGF may be used to diagnose Peripartum Cardiomyopathy. PMID: 28552862 In this context, our results demonstrate that D16F7 markedly inhibits chemotaxis and invasiveness of GBM cells and patient-derived GBM stem cells (GSCs) in response to VEGF-A and PlGF, suggesting that VEGFR-1 might represent a suitable target that deserves further investigation for GBM treatment. PMID: 28797294 reduced in preeclampsia and fetal growth restriction PMID: 27865093 Studied serum levels of soluble fms-like tyrosine kinase-1 (sFlt-1) and placental growth factor (PlGF) as markers for early diagnosis of preeclampsia. PMID: 29267975 A high sFlt-1/PlGF ratio was associated with adverse outcomes and a shorter duration to delivery in early-onset fetal growth restriction. PMID: 28737473 HIV status had no effect on serum level PMID: 28627965 low plasma levels at 19-25 and 26-31 weeks of gestation were independent risk factors for a small placenta at >/=35 weeks PMID: 28613009 Data suggest that expression of PGF is down-regulated in placental trophoblasts from pregnancies complicated by fetal growth retardation compared with control placentas. PMID: 28676532 placental expression not altered by placental dysfunction PMID: 28494189 Report sensitivity of sFlt-1/PlGF ratio for diagnosis of preeclampsia and fetal growth restriction. PMID: 28501276

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.