Is the Recombinant Human PlGF Protein (Catalog # 264-PGB) specific to a particular isoform?

Name: Recombinant Human PlGF Protein
Brand: R&D Systems
SKU: 264-PGB
Price: 334 USD

Yes, this protein is from isoform PlGF-131, which is also known as PlGF-1 based on Accession # P49763-2 (https://www.ncbi.nlm.nih.gov/protein?term=P49763-2).

Recombinant Human PlGF Protein

R&D Systems, Inc. a Bio-Techne Brand

Catalog # 264-PGB

Citations (29)

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Key Product Details

Source:	E. coli
Accession #:	NP_001193941.1
Structure / Form:	Disulfide-linked homodimer
Applications:	Bioactivity

View Full Technical Details for Recombinant Human PlGF Protein

Product Specifications for Recombinant Human PlGF Protein

Source	E. coli-derived human PlGF protein Ala21-Arg149
Purity	>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin level	<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis	Ala21
Predicted Molecular Mass	15 kDa
SDS-PAGE	12-15 kDa, reducing conditions
Activity	Measured by its binding ability in a functional ELISA. When Recombinant Human VEGF R1/Flt‑1 Fc Chimera (Catalog # 3516-FL) is immobilized at 0.5 μg/mL, 100 μL/well, the concentration of Recombinant Human PlGF that produces 50% of the optimal binding response is approximately 0.75-4.5 ng/mL.

Scientific Data Examples for Recombinant Human PlGF Protein

	When Recombinant Human VEGF R1/Flt-1 Fc Chimera (3516-FL) is immobilized at 0.5 μg/mL, 100 μL/well, the concentration of Recombinant Human PlGF (Catalog # 264-PGB) that produces 50% of the optimal binding response is approximately 0.75-4.5 ng/mL.

Formulation, Preparation and Storage

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

264-PGB

Carrier

Formulation	Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Reconstitution	Reconstitute at 200 μg/mL in 4 mM HCl.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 to -70 °C under sterile conditions after reconstitution.

264-PGB/CF

Carrier Free

Formulation	Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Reconstitution	Reconstitute at 200 μg/mL in 4 mM HCl.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: PlGF

Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines (1, 2). Alternative splicing results in at least three human mature PlGF forms containing 131 (PlGF-1), 152 (PlGF-2), and 203 (PlGF-3) amino acids (aa) respectively (1, 2). Only PlGF-2 contains a highly basic heparin-binding 21 aa insert at the C-terminus (1). Human PlGF-1 shares 56%, 55%, 74% and 95% aa identity with the comparable isoform of mouse, rat, canine, and equine PlGF, respectively. PlGF is mainly found as variably glycosylated, secreted, 55-60 kDa disulfide linked homodimers (3). Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes, and some endothelial cells (1, 4-6). Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia (7). However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia (8). PlGF binds and signals through VEGF R1/Flt-1 but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2-mediated angiogenesis (1, 4, 8, 9). However, PlGF (especially PlGF-1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2 (3, 4). PlGF-2, but not PLGF-1, shows heparin-dependent binding of Neuropilin (Npn)-1 and Npn-2 (10, 11). PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound, bone fracture, and cardiac repair, but also contribute to inflammation in active sickle cell disease and atherosclerosis (5, 6, 8, 12-15). PlGF can also inhibit TIMP3 expression in the spleen, leading to immune triggering of hypertension (16).

Item	Value
References	Hauser, S. and H.A. Weich (1993) Growth Factors 9:259. Maglione, D. et al. (1993) Oncogene 8:925. Eriksson, A. et al. (2002) Cancer Cell 1:99. Ribatti, D. (2008) Angiogenesis 11:215. Oura, H. et al. (2003) Blood 101:560. Roncal, C. et al. (2010) Cardiovasc. Res. 86:29. Levine, R.J. et al. (2004) N. Engl. J. Med. 350:672. Carmeliet, P. et al. (2001) Nat. Med. 7:575. Autiero, M. et al. (2003) Nat. Med. 9:936. Migdal, M. et al. (1998) J. Biol. Chem. 273:22272. Cheng, L. et al. (2004) J. Biol. Chem. 279:30654. Perelman, N. et al. (2003) Blood 102:1506. Cianfarani, F. et al. (2006) Am. J. Pathol. 169:1167. Maes, C. et al. (2006) J. Clin. Invest. 116:1230. Iwasaki, H. et al. (2011) PLoS One 6:e24872. Carnevale, D. et al. (2014) Immunity 41:737.
Long Name	Placenta Growth Factor
Entrez Gene IDs	5228 (Human); 18654 (Mouse)
Alternate Names	D12S1900, PGF, PGFL, PLGFplacental growth factor-like, PlGF, PlGF-2, SHGC-10760, placenta growth factor, placental growth factor, placental growth factor, vascular endothelial growth factor-related protein

Citations for Recombinant Human PlGF Protein (29)

Showing 1 - 10 of 29 citations Showing All

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Citations are publications that use Bio-Techne products. Selected citations for Recombinant Human PlGF Protein include:

Species: Human
Sample Types: Whole Cells
Applications: Bioassay

T Matsuyama et al. (2021), Complement activation by an angiogenic imbalance leads to systemic vascular endothelial dysfunction: A new proposal for the pathophysiology of preeclampsia Journal of reproductive immunology, 145(0):103322.
PMID: 33887508
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

S Jauhiainen et al. (2019), Axon Guidance-Related Factor FLRT3 Regulates VEGF-Signaling and Endothelial Cell Function Front Physiol, 10(0):224.
PMID: 30930791
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

H Nagano et al. (2019), VEGFR-1 Regulates EGF-R to Promote Proliferation in Colon Cancer Cells Int J Mol Sci, 20(22).
PMID: 31717527
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo

Y Zhang et al. (2018), Treatment with placental growth factor attenuates myocardial ischemia/reperfusion injury PLoS ONE, 13(9):e0202772.
PMID: 30212490
Species: Human
Sample Types: Recombinant Protein
Applications: ELISA (Capture)

JM Gu et al. (2018), Blockade of placental growth factor reduces vaso-occlusive complications in murine models of sickle cell disease Exp. Hematol., 0(0).
PMID: 29337222
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

D Wu et al. (2017), Elevated expression of placental growth factor is associated with airway-wall vascular remodelling and thickening in smokers with asthma Sci Rep, 7(0):43017.
PMID: 28220848
Species: Rat
Sample Types: Whole Cells
Applications: Bioassay

X Li et al. (2017), Placental growth factor silencing ameliorates liver fibrosis and angiogenesis and inhibits activation of hepatic stellate cells in a murine model of chronic liver disease J. Cell. Mol. Med., 0(0).
PMID: 28378526
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

(2016), Hypoxia-induced responses by endothelial colony-forming cells are modulated by placental growth factor Stem Cell Res Ther, 7(1):173.
PMID: 27899144
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Li C et al. (2015), MicroRNA 648 Targets ET-1 mRNA and is cotranscriptionally regulated with MICAL3 by PAX5. Mol Cell Biol, 35(3):514-28.
PMID: 25403488
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Hou H et al. (2014), Elastase induces lung epithelial cell autophagy through placental growth factor: a new insight of emphysema pathogenesis. Autophagy, 10(9):1509-21.
PMID: 24988221
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Park et al. (2014), Interaction of mesenchymal stem cells with fibroblast-like synoviocytes via cadherin-11 promotes angiogenesis by enhanced secretion of placental growth factor. J Immunol, 192(7):3003-10.
PMID: 24574497
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Tannetta D et al. (2013), Characterisation of syncytiotrophoblast vesicles in normal pregnancy and pre-eclampsia: expression of Flt-1 and endoglin. PLoS ONE, 8(2):e56754.
PMID: 23437230
Species: Human
Sample Types: Recombinant Protein
Applications: Binding Assay

Goyal A et al. (2011), Endorepellin, the angiostatic module of perlecan, interacts with both the alpha2beta1 integrin and vascular endothelial growth factor receptor 2 (VEGFR2): a dual receptor antagonism. J. Biol. Chem., 286(29):25947-62.
PMID: 21596751
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Patel N et al. (2010), Placenta growth factor (PlGF), a novel inducer of plasminogen activator inhibitor-1 (PAI-1) in sickle cell disease (SCD). J. Biol. Chem., 285(22):16713-22.
PMID: 20351105
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Brave SR et al. (2010), Placental growth factor neutralising antibodies give limited anti-angiogenic effects in an in vitro organotypic angiogenesis model. Angiogenesis, 13(4):337-47.
PMID: 20953695
Species: Guinea Pig
Sample Types: In Vivo
Applications: In Vivo

Matsunaga Y et al. (2009), VEGF-A and VEGF-F evoke distinct changes in vascular ultrastructure. Biochem. Biophys. Res. Commun., 379(4):872-5.
PMID: 19126400
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Ponticelli S et al. (2008), Modulation of angiogenesis by a tetrameric tripeptide that antagonizes vascular endothelial growth factor receptor 1. J. Biol. Chem., 283(49):34250-9.
PMID: 18922791
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Lin YL et al. (2007), Placental growth factor down-regulates type 1 T helper immune response by modulating the function of dendritic cells. J. Leukoc. Biol., 82(6):1473-80.
PMID: 17761954
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo

Zhang Z et al. (2007), alpha2beta1 integrin expression in the tumor microenvironment enhances tumor angiogenesis in a tumor cell-specific manner. Blood, 111(4):1980-8.
PMID: 18042800
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay

Mohamedali KA et al. (2006), Inhibition of prostate tumor growth and bone remodeling by the vascular targeting agent VEGF121/rGel. Cancer Res., 66(22):10919-28.
PMID: 17108129
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Cianfarani F et al. (2006), Placenta growth factor in diabetic wound healing: altered expression and therapeutic potential. Am. J. Pathol., 169(4):1167-82.
PMID: 17003476
Species: Mouse

Applications: In Vivo

Nozaki M et al. (2006), Loss of SPARC-mediated VEGFR-1 suppression after injury reveals a novel antiangiogenic activity of VEGF-A. J. Clin. Invest., 116(2):422-9.
PMID: 16453023
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Moreno MJ et al. (2006), Insulin-like growth factor binding protein-4 (IGFBP-4) is a novel anti-angiogenic and anti-tumorigenic mediator secreted by dibutyryl cyclic AMP (dB-cAMP)-differentiated glioblastoma cells. Glia, 53(8):845-57.
PMID: 16586492
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay

Dikov MM et al. (2005), Differential roles of vascular endothelial growth factor receptors 1 and 2 in dendritic cell differentiation. J. Immunol., 174(1):215-22.
PMID: 15611243
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo

Niida S et al. (2005), VEGF receptor 1 signaling is essential for osteoclast development and bone marrow formation in colony-stimulating factor 1-deficient mice. Proc. Natl. Acad. Sci. U.S.A., 102(39):14016-21.
PMID: 16172397
Species: Bovine
Sample Types: Whole Cells
Applications: Bioassay

Sun JF et al. (2005), Microvascular patterning is controlled by fine-tuning the Akt signal. Proc. Natl. Acad. Sci. U.S.A., 102(1):128-33.
PMID: 15611473
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo

Tamarat R et al. (2004), Impairment in ischemia-induced neovascularization in diabetes: bone marrow mononuclear cell dysfunction and therapeutic potential of placenta growth factor treatment. Am. J. Pathol., 164(2):457-66.
PMID: 14742252
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Maynard SE et al. (2003), Excess placental soluble fms-like tyrosine kinase 1 (sFlt1) may contribute to endothelial dysfunction, hypertension, and proteinuria in preeclampsia. J. Clin. Invest., 111(5):649-58.
PMID: 12618519
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo

Oura H et al. (2002), A critical role of placental growth factor in the induction of inflammation and edema formation. Blood, 101(2):560-7.
PMID: 12393422

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Showing 1 - 10 of 29 citations Showing All

FAQs for Recombinant Human PlGF Protein

Is the Recombinant Human PlGF Protein (Catalog # 264-PGB) specific to a particular isoform?

Yes, this protein is from isoform PlGF-131, which is also known as PlGF-1 based on Accession # P49763-2 (https://www.ncbi.nlm.nih.gov/protein?term=P49763-2).

Recombinant Human PlGF Protein

R&D Systems, Inc. a Bio-Techne Brand

Key Product Details

Customers also Viewed

Product Specifications for Recombinant Human PlGF Protein

Scientific Data Examples for Recombinant Human PlGF Protein

Formulation, Preparation and Storage

Carrier Free

264-PGB

Carrier

264-PGB/CF

Carrier Free

Reconstitution Calculator

Background: PlGF

Citations for Recombinant Human PlGF Protein (29)

FAQs for Recombinant Human PlGF Protein

Product Documents for Recombinant Human PlGF Protein

Product Datasheets

COA

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