Biotinylated Human VEGFR2 Protein (C-6His-Avi)

Name: Biotinylated Human VEGFR2 Protein (C-6His-Avi)
Brand: Beta LifeScience
SKU: BL-2652NP
Availability: InStock

BL-2652NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Antibody / cell therapy targets, Avi-tagged proteins, Biotinylated proteins, Car-nk targets proteins, Car-t cell therapy targets, Cytokines and growth factors, Featured biotinylated protein molecules, Growth factors and receptors, 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	Biotinylated Recombinant Human Vascular Endothelial Growth Factor Receptor 2 is produced by our Mammalian expression system and the target gene encoding Ala20-Glu764 is expressed with a 6His, Avi tag at the C-terminus.
Accession	P35968
Synonym	Vascular endothelial growth factor receptor 2; KDR; VEGFR-2; Fetal liver kinase 1; FLK-1; Kinase insert domain receptor; Protein-tyrosine kinase receptor flk-1
Gene Background	Human Vascular endothelial growth factor receptor 2(KDR, VEGFR-2) is a member of the class III subfamily of receptor tyrosine kinases (RTKs). KDR is involved in a number of fundamental biological processes such as the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. It also plays an essential role in promoting proliferation, survival, migration and differentiation of endothelial cells, reorganization of the actin cytoskeleton. VEGFR2 is identified as the receptor for VEGF and VEGFC and an early marker for endothelial cell progenitors, whose expression is restricted to endothelial cells in vivo.The adaptor protein SHB has been shown to interact with VEGFR2 in receptor tyrosine kinase signaling. In addition, VEGFR2 is able to interact with HIV-1 extracellular Tat protein upon VEGF activation, and seems to enhance angiogenesis in Kaposi's sarcoma lesions. VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis.
Molecular Mass	86.1 KDa
Apmol Mass	120-150 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% 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, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC.
Subcellular Location	Cell junction. Endoplasmic reticulum. Cell membrane.; [Isoform 1]: Cell membrane; Single-pass type I membrane protein. Cytoplasm. Nucleus. Cytoplasmic vesicle. Early endosome. Note=Detected on caveolae-enriched lipid rafts at the cell surface. Is recycled from the plasma membrane to endosomes and back again. Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation. VEGFA binding triggers internalization and translocation to the nucleus.; [Isoform 2]: Secreted.; [Isoform 3]: Secreted.
Protein Families	Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
Database References	HGNC: 6307 OMIM: 191306 KEGG: hsa:3791 STRING: 9606.ENSP00000263923 UniGene: Hs.479756
Associated Diseases	Hemangioma, capillary infantile (HCI)
Tissue Specificity	Detected in cornea (at protein level). Widely expressed.

Gene Functions References

The findings indicate that miR-203a inhibits hepatocellular carcinoma cell invasion, metastasis, and angiogenesis by negatively targeting HOXD3 and suppressing cell signaling through the VEGFR pathway. PMID: 29402992
these results indicate that sFlt-1 up-regulation by VEGF may be mediated by the VEGF/Flt-1 and/or VEGF/KDR signaling pathways. PMID: 29497919
miR424 may target VEGFR2 and inhibit Hemangioma derived endothelial cell growth. PMID: 30132564
VEGFR2 is regulated by deSUMOylation during pathological angiogenesis. PMID: 30120232
This study shows that decreasing the ratio of glutathione to oxidized glutathione with diamide leads to enhanced protein S-glutathionylation, increased reactive oxygen species (ROS) production, and enhanced VEGFR2 activation. PMID: 30096614
Study confirmed prognostic effect of EGFR and VEGFR2 for recurrent disease and survival rates in patients with epithelial ovarian cancer. PMID: 30066848
none of the investigated VEGFR-2 gene polymorphisms was found to be an independent prognostic marker for infantile hemangioma. PMID: 29984822
These results suggest functional interactions among ATX, VEGFR-2, and VEGFR-3 in the modulation of hemovascular and lymphovascular cell activation during vascular development. PMID: 30456868
miR-195 suppresses cell proliferation of ovarian cancer cells through regulation of VEGFR2 and AKT signaling pathways. PMID: 29845300
Thioredoxin-interacting protein (TXNIP) is highly induced in retinal vascular endothelial cells under diabetic conditions. Data (including data from studies using knockout mice) suggest that TXNIP in retinal vascular endothelial cells plays role in diabetic retinal angiogenesis via VEGF/VEGFR2 and Akt/mTOR signaling. PMID: 29203232
Inhibition of FPR1 and/or NADPH oxidase functions prevents VEGFR2 transactivation and the triggering of the downstream signalling cascades. PMID: 29743977
VEGFA activates VEGFR1 homodimers and AKT, leading to a cytoprotective response, whilst abluminal VEGFA induces vascular leakage via VEGFR2 homodimers and p38 PMID: 29734754
association of rs519664[T] in TTC39B on 9p22 with endometriosis, is reported. PMID: 27453397
VEGF, VEGFR2 and GSTM1 polymorphisms in outcome of multiple myeloma patients treated with thalidomide-based regimens PMID: 28665417
In the in vitro tests, JFD-WS effectively inhibited HUVEC proliferation, migration, tube formation and VEGFR2 phosphorylation. Additionally, JFD-WS inhibited the formation of blood vessels in chick chorioallantoic membrane. While inhibiting the xenograft tumor growth in experimental mice, JFD-WS decreased the plasma MUC1 levels PMID: 29436685
The effects of Platelet-rich plasma on vascular endothelial growth factor receptor-2 (VEGFR2) and CD34 expression were evaluated using real-time PCR, flow cytometry, western blot, immunocytochemistry and pathological study, as were carried out in both human umbilical endothelial cell culture and rat skin PMID: 28948378
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
Single nucleotide polymorphism of VEGFR2 is associated with relapse in gastroenteropancreatic neuroendocrine neoplasms. PMID: 29787601
Our data showed that ampelopsin inhibited angiogenesis with no cytotoxicity by suppressing both VEGFR2 signaling and HIF-1alpha expression. These results suggest that Hovenia dulcis Thunb. and its active compound ampelopsin exhibit potent antiangiogenic activities and therefore could be valuable for the prevention and treatment of angiogenesis-related diseases including cancer. PMID: 29039561
Authors demonstrated that when VEGFR2 was inhibited, NRP-1 appeared to regulate RAD51 expression through the VEGFR2-independent ABL-1 pathway, consequently regulating radiation sensitivity. In addition, the combined inhibition of VEGFR2 and NRP-1 appears to sensitize cancer cells to radiation. PMID: 29777301
We found that depletion of FGD5 in microvascular cells inhibited their migration towards a stable VEGFA gradient. Furthermore, depletion of FGD5 resulted in accelerated VEGFR2 degradation, which was reverted by lactacystin-mediated proteasomal inhibition. Our results thus suggest a mechanism whereby FGD5 sustains VEGFA signaling and endothelial cell chemotaxis via inhibition of proteasome-dependent VEGFR2 degradation. PMID: 28927665
ATG5 and phospho-KDR expression was strongly associated with the density of vasculogenic mimicry in tumors and poor clinical outcome. PMID: 28812437
Increased expression of VEGFR2 correlated with differentiation. PMID: 28854900
DDA exhibits anti-angiogenic properties through suppressing VEGF-A and VEGFR2 signaling PMID: 27517319
RCAN1.4 plays a novel role in regulating endothelial cell migration by establishing endothelial cell polarity in response to VEGF. PMID: 28271280
Anlotinib occupied the ATP-binding pocket of VEGFR2 tyrosine kinase. PMID: 29446853
the difference between the pro- (VEGF165a) and antiangiogenic (VEGF165b) VEGF isoforms and its soluble receptors for severity of diabetic retinopathy, is reported. PMID: 28680264
anlotinib inhibits the activation of VEGFR2, PDGFRbeta and FGFR1 as well their common downstream ERK signaling PMID: 29454091
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
by inhibiting the phosphorylation of VEGFR2, the P18 peptide ( functional fragment of pigment epithelial-derived factor (PEDF)modulates signalling transduction between VEGF/VEGFR2 and suppresses activation of the PI3K/Akt cascades, leading to an increase in mitochondrial-mediated apoptosis and anti-angiogenic activity. PMID: 28627623
VEGF increases arginine transport via modulation of CAT-1 in endothelial cells. This effect is exclusively dependent on KDR rather than Flt-1. PMID: 28478454
this study shows that glioma stem cells-derived exosomes promote the angiogenic ability of endothelial cells through miR-21/VEGF/VEGFR2 signal pathway PMID: 28410224
MEG3 regulated by HIF-1alpha is required to maintain VEGFR2 expression in endothelial cells and plays a vital role for VEGFA-mediated endothelial angiogenesis. PMID: 29391273
Overexpression of peroxiredoxin 2 and VEGFR2 in pterygium might be involved in the pathogenesis or recurrence of pterygium. The increase of VEGFR2 might be related to the increase of peroxiredoxin 2 in response to excessive reactive oxygen species from ultraviolet exposure. PMID: 28489720
KDR -604T > C (rs2071559) polymorphism showed no significant association with multiple sclerosis. PMID: 28401369
The up-regulation of NHERF1 induced by the exposure to hypoxia in colon cancer cells depends on the activation of VEGFR2 signaling. PMID: 27999191
JAM-C plays an important role in maintaining VEGR2 expression to promote retinal pigment epithelial cell survival under oxidative stress. PMID: 28203682
Data suggest that diabetic nephropathy is associated with diminished VEGF-A levels in the kidney; VEGF-A/VEGFR-2 signaling is influenced by the local milieu. [REVIEW] PMID: 27836681
this paper shows that cell-permeable iron inhibits vascular endothelial growth factor receptor-2 signaling and tumor angiogenesis PMID: 27589831
Eriocalyxin B inhibited VEGF-induced angiogenesis in HUVECs by suppressing VEGFR-2 signaling. PMID: 27756875
we found that the KDR fragment with domain 4 induced phosphorylation of VEGFR-2, as well as phosphorylation of downstream receptor kinases in HUVECs and VEGFR-2-positive breast cancer cells. PMID: 28303365
gremlin protects skin cells from UV damages via activating VEGFR2-Nrf2 signaling PMID: 27713170
Specificity protein 1 (Sp1) orchestrates the transcription of both VEGF and VEGFR2; hence, Sp1 could act as a therapeutic target. Here, we demonstrate that CF3DODA-Me induced apoptosis, degraded Sp1, inhibited the expression of multiple drivers of the blebbishield emergency program such as VEGFR2, p70S6K, and N-Myc through activation of caspase-3, inhibited reactive oxygen species; and inhibited K-Ras activation to abolis PMID: 28283889
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
REVIEW. the interplay among the ETS transcription factor ETV2, vascular endothelial growth factor, and its receptor VEGFR2/FLK1 is essential for hematopoietic and vascular development. Emerging studies also support the role of these three factors and possible interplay in hematopoietic and vascular regeneration. PMID: 28026128
DOT1L cooperates with transcription factor ETS-1 to stimulate the expression of VEGFR2, thereby activating ERK1/2 and AKT signaling pathways and promoting angiogenesis. PMID: 27626484
This study provides new insights into the mechanism of VEGFR2 dimerization and activation. PMID: 28847506
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
our results illustrated that CDK5-mediated KDR phosphorylation controls prolactin pituitary adenoma progression and KDR pSer-229 serves as a potential prognostic biomarker for both noninvasive and invasive pituitary adenomas. PMID: 27438154
Data indicate that simultaneous targeting of molecules that control distinct phases of angiogenesis, such as ALK1 and VEGFR, is a valid strategy for treatment of metastatic renal cell carcinoma (mRCC). PMID: 27248821

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.