Recombinant Human Placenta Growth Factor (PGF) Protein (hFc)

Name: Recombinant Human Placenta Growth Factor (PGF) Protein (hFc)
Brand: Beta LifeScience
SKU: BLC-06330P
Price: 349.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins, Recombinant proteins holiday sale

Price Save $143

Size

100ug

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Product Overview

Description	Recombinant Human Placenta Growth Factor (PGF) Protein (hFc) is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P49763
Target Symbol	PGF
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-hFc
Target Protein Sequence	LPAVPPQQWALSAGNGSSEVEVVPFQEVWGRSYCRALERLVDVVSEYPSEVEHMFSPSCVSLLRCTGCCGDENLHCVPVETANVTMQLLKIRSGDRPSYVELTFSQHVRCECRPLREKMKPERRRPKGRGKRRREKQRPTDCHLCGDAVPRR
Expression Range	19-170aa
Protein Length	Partial
Mol. Weight	45.1 kDa
Research Area	Cardiovascular
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 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: Hs.252820
Tissue Specificity	While the three isoforms are present in most placental tissues, PlGF-2 is specific to early (8 week) placenta and only PlGF-1 is found in the colon and mammary carcinomas.

Gene Functions References

low serum level associated with stillbirth 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

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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.

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