Recombinant Human VEGFR1 Protein (C-Fc)

Name: Recombinant Human VEGFR1 Protein (C-Fc)
Brand: Beta LifeScience
SKU: BL-0106NP
Availability: InStock

BL-0106NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, Buy cytokines, chemokines, and growth factors for research online, Car-nk targets proteins, 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

Description	Recombinant Human Vascular Endothelial Growth Factor Receptor 1 is produced by our Mammalian expression system and the target gene encoding Ser27-Asn756 is expressed with a human IgG1 Fc tag at the C-terminus.
Accession	P17948
Synonym	Vascular endothelial growth factor receptor 1; VEGFR-1; Fms-like tyrosine kinase 1; FLT-1; Tyrosine-protein kinase FRT; Tyrosine-protein kinase receptor FLT; Vascular permeability factor receptor
Gene Background	Human Vascular endothelial growth factor receptor 1(VEGFR-1, FLT-1) is a member of the the class III subfamily of receptor tyrosine kinases (RTKs) and Tyr protein kinase family and CSF-1/PDGF receptor subfamily. VEGFR-1 is widely expressed in human tissues including normal lung, placenta, liver, kidney, heart and brain tissues. It is specifically expressed in most of the vascular endothelial cellsand peripheral blood monocytes. VEGFR-1 contains seven Ig-like C2-type domains and one protein kinase domain. VEGFR-1is an essential receptor tyrosine kinase and plays an important role in theregulation of VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. It is also mediators of neurotrophic activity and regulators of hematopoietic development. VEGFR-1 is a receptor for VEGF, VEGFB and PGF. It has a tyrosine-protein kinase activity. Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF.It may play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells and promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. VEGFR-1 can also promote PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro).
Molecular Mass	109.3 KDa
Apmol Mass	150-190 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 5%Trehalose, 5%Mannitol, 0.01%Tween80, pH7.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Biologically active. Please contact us to obtain bioactivity data.
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. Acts as a positive regulator of postnatal retinal hyaloid vessel regression (Ref.11). May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1.; Phosphorylates PLCG.; May function as decoy receptor for VEGFA.; May function as decoy receptor for VEGFA.; May function as decoy receptor for VEGFA.; Has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion.
Subcellular Location	[Isoform 1]: Cell membrane; Single-pass type I membrane protein. Endosome. Note=Autophosphorylation promotes ubiquitination and endocytosis.; [Isoform 2]: Secreted.; [Isoform 3]: Secreted.; [Isoform 4]: Secreted.; [Isoform 5]: Cytoplasm.; [Isoform 6]: Cytoplasm.; [Isoform 7]: Cytoplasm.
Protein Families	Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
Database References	HGNC: 3763 OMIM: 165070 KEGG: hsa:2321 STRING: 9606.ENSP00000282397 UniGene: PMID: 29497919 Serum sFlt-1 can be used as a prognostic marker to predict the occurrence of complications of preeclampsia. PMID: 30032672 The ratio of sFlt-1/sEGFR could be used as a novel candidate biochemical marker in monitoring the severity of preterm preeclampsia. sEndoglin and sEGFR may be involved in the pathogenesis of small for gestational age in preterm preelampsia. PMID: 30177039 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 dynamic regulation of mVEGFR1 stability and turnover in blood vessels impacts angiogenesis PMID: 28589930 Study shows that soluble VEGF receptor 1 (sVEGFR-1/ soluble fms-like tyrosine kinase 1 [sFlt-1]) showed a cytotoxic effect on BeWo cells. Results suggest that sFLT-1 could be therapeutic for malignant tumors. PMID: 28322131 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 sFlt1 was produced in significant amounts by preeclamptic peripheral blood mononuclear leukocytes, and ex vivo studies show that the placenta induces this over-expression. In contrast, exposure to PBMCs appears to decrease sFlt1 production by preeclamptic placenta. PMID: 29674197 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 These results showed that arginase controlled sFlt-1 elevation to some extent. PMID: 29548823 These results suggest that VM formation is increased by EBVLMP1 via VEGF/VEGFR1 signaling and provide additional information to clarify the role of EBVLMP1 in nasopharyngeal carcinoma (NPC)pathophysiology PMID: 29749553 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 VEGFA activates VEGFR1 homodimers and AKT, leading to a cytoprotective response, whilst abluminal VEGFA induces vascular leakage via VEGFR2 homodimers and p38 PMID: 29734754 metformin's dual effect in hyperglycemia-chemical hypoxia is mediated by direct effect on VEGFR1/R2 leading to activation of cell migration through MMP16 and ROCK1 upregulation, and inhibition of apoptosis by increase in phospho-ERK1/2 and FABP4, components of VEGF signaling cascades PMID: 29351188 Additionally, LVsFlt1MSCs inhibited tumor growth and prolonged survival in an hepatocellular carcinoma (HCC)mouse model via systemic injection. Overall, the present study was designed to investigate the potential of LVsFlt1MSCs for antiangiogenesis gene therapy in HCC. PMID: 28849176 Review of the role of dysregulation at the Fms-like tyrosine kinase 1 locus in the fetal genome (likely in the placenta) in conferring genetic predisposition to preeclampsia. PMID: 29138037 VEGF and VEGFR1 levels in different regions of the normal and preeclampsia placentae. PMID: 28770473 High PlGF and/or low sFlt-1/PlGF may be used to diagnose Peripartum Cardiomyopathy. PMID: 28552862 Results demonstrate that short-activating RNA targeting the flt-1 promoter increased sFlt-1 mRNA and protein levels, while reducing VEGF expression. This was associated with suppression of human umbilical vascular endothelial cell (HUVEC) proliferation and cell cycle arrest at the G0/G1 phase. HUVEC migration and tube formation were also suppressed by Flt a-1. PMID: 29509796 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 Study showed that term deliveries, higher soluble fms-like tyrosine kinase 1 (sFlt1) concentrations were associated with a smaller uterine artery resistance indices (RI) at the subsequent visit. For preterm delivery, higher sFlt1 concentrations were associated with a larger uterine artery RI. PMID: 28335685 elevated 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 This prospective observational study compare urine nephrin:creatinine ratio (NCR, ng/mg) with serum soluble fms-like tyrosine kinase-1:placental growth factor ratio (FPR, pg/pg) for preeclampsia (PE) prediction among unselected asymptomatic pregnant women in 2(nd) trimester. PMID: 27874074 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 Serum from type 2 diabetics reduced Akt/VEGFR-1 protein expression in endothelial progenitor cells. PMID: 28732797 The VEGF/sVEGF-R1 ratio in follicular fluid on the day of oocyte retrieval in women undergoing IVF procedure, regardless of the type of stimulation protocol, might predict the risk of developing ovarian hyperstimulation syndrome (OHSS). To the best of our knowledge this is the first paper in the literature to show interplay among VEGF, EG-VEGF and sVEGF-R1 and the correlation between their concentration and OHSS risk. PMID: 28820403 plasma level not associated with placenta size PMID: 28613009 the difference between the pro- (VEGF165a) and antiangiogenic (VEGF165b) VEGF isoforms and its soluble receptors for severity of diabetic retinopathy, is reported. PMID: 28680264 detectable amounts are produced by endometrial stromal cells (ESC)); expression is turned off during decidualization; ESC decidualization and resulting sFlt1 expression are a reversible phenomenon PMID: 28494174 High sFlt-1 concentrations may account for diminished maternal serum PlGF levels. PMID: 28494189 upregulated tenfold in preeclamptic tissue PMID: 28067578 upregulation of sVEGFR-1 with concomitant decline of PECAM-1 and sVEGFR-2 levels in preeclampsia compared to normotensive pregnancies, Irrespective of the HIV status PMID: 28609170 In patients with hypertensive disorders of pregnancy, those in the highest tertile of mean arterial pressure had the highest serum levels of sFlt1 and sEng. PMID: 28609171 likely that in early onset pre-eclampsia, increased maternal sFlt-1 concentrations are the primary reason for diminished maternal serum-free PlGF levels PMID: 28609172 Based on these data, we conclude that the rs9943922 SNP in the FLT1 gene does not result in a large difference in FLT1 protein levels, regardless of whether it is the soluble or the membrane bound form. PMID: 28949775 Report sensitivity of sFlt-1/PlGF ratio for diagnosis of preeclampsia and fetal growth restriction. PMID: 28501276 Our study suggests that "migration" of the placenta is derived from placental degeneration at the caudal part of the placenta, and sFlt-1 plays a role in this placental degeneration. PMID: 29409879 the association of VEGFR1 rs9582036 and rs9554320 with the outcome of sunitinib in mRCC patients did not reach the threshold for statistical significance, and therefore, both genetic variants have limited use as biomarkers for prediction of sunitinib efficacy. PMID: 27901483 Placental sFLT-1 expression is upregulated in approximately 28% of non-preeclamptic pregnancies complicated by small for gestational age infants. These pregnancies showed increased placental vascular pathology, more umbilical Doppler abnormalities, and earlier delivery with lower birthweight PMID: 28454690 This study demonstrated that the baseline of sFlt-1 was significantly correlated with soft neurologic signs and right entorhinal volume but not other baseline clinical/brain structural measures in patient with psychosis. PMID: 27863935 By comparing in vivo data with immunohistochemical analysis of excised tumors we found an inverse correlation between 99mTc-VEGF165 uptake and VEGF histologically detected, but a positive correlation with VEGF receptor expression (VEGFR1). PMID: 28498441 sFLT-1 represents a link between angiogenesis, endothelial dysfunction, and subclinical atherosclerosis. Measurement of sFLT-1 as a marker of vascular dysfunction in beta-TI may provide utility for early identification of patients at increased risk of cardiopulmonary complications. PMID: 28301910 Icrucumab and ramucirumab are recombinant human IgG1 monoclonal antibodies that bind vascular endothelial growth factor (VEGF) receptors 1 and 2 (VEGFR-1 and -2), respectively. VEGFR-1 activation on endothelial and tumor cell surfaces increases tumor vascularization and growth and supports tumor growth via multiple mechanisms, including contributions to angiogenesis and direct promotion of cancer cell proliferation. PMID: 28220020 sFLT-1 e15a splice variant is seen only in humans and is principally expressed in the placenta, making it likely to be the variant chiefly responsible for the clinical features of early-onset pre-eclampsia. (Review) PMID: 27986932 significant reduction in sVEGFR-1 levels after renal denervation procedure for hypertension PMID: 27604660 Cases with high MDSC infiltration, which was inversely correlated with intratumoral CD8(+) T-cell infiltration, exhibited shorter overall survival. In a mouse model, intratumoral MDSCs expressed both VEGFR1 and VEGFR2. VEGF expression in ovarian cancer induced MDSCs, inhibited local immunity, and contributed to poor prognosis PMID: 27401249 Circulating tissue transglutaminase is associated with sFlt-1, soluble endoglin and VEGF in the maternal circulation of preeclampsia patients, suggesting that tTG may have a role in the pathogenesis of PE. PMID: 27169826 The authors observed direct damage caused by sFLT1 in tumour cells. They exposed several kinds of cells derived from ovarian and colorectal cancers as well as HEK293T cells to sFLT1 in two ways, transfection and exogenous application. The cell morphology and an lactate dehydrogenase assay revealed cytotoxicity. PMID: 27103202

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.

📧 inquiry@betalifesci.com 📞 +1(201) 888-7983

Contact Us Now for Inquiries, Orders, and Questions

Recombinant Human VEGFR1 Protein (C-Fc)

Recombinant Human VEGFR1 Protein (C-Fc)

Product Overview

Target Details

FAQs