VEGFR2 Human
Vascular Endothelial Growth Factor Receptor-2 Human Recombinant
Cat. No.
BT21886
Source
Insect Cells.
Synonyms
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
Soluble VEGFR-2 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide having a molecular mass of 116 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.
The sKDR is purified by proprietary chromatographic techniques.
The sKDR is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Endothelial cells rely on three distinct vascular endothelial growth factor (VEGF) receptors, all of which belong to the receptor tyrosine kinases (RTKs) family. These receptors, VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4), are primarily found on endothelial cells, with VEGFR-1 also present on monocytes. Structurally, they share seven immunoglobulin-like extracellular domains, a single transmembrane region, and an intracellular split tyrosine kinase domain. While VEGFR-2's affinity for VEGF is lower compared to VEGFR-1, it exhibits superior signaling activity. Notably, VEGFR-2 plays a crucial role in endothelial cell proliferation by mediating mitogenic activity. Interestingly, the flt-1 gene undergoes differential splicing, resulting in a soluble variant of VEGFR-1 (sVEGFR-1). However, no naturally occurring soluble forms of VEGFR-2 have been identified. Importantly, the interaction between VEGF165 and VEGFR-2 relies on the presence of heparin.
Description
Produced in a baculovirus expression system, Recombinant Human Soluble VEGFR-2 is a monomeric, glycosylated polypeptide with a molecular weight of 116 kDa. This soluble receptor protein encompasses the first 7 extracellular domains, which are sufficient for ligand binding. The purification of sKDR is achieved through proprietary chromatographic methods.
Physical Appearance
White, lyophilized powder, sterile-filtered.
Formulation
KDR was lyophilized from a sterile solution at a concentration of 1 mg/ml. The solution contained 25 mM MES (pH 5.5) and 100 mM NaCl.
Solubility
For reconstitution of lyophilized VEGFR2, it is recommended to use sterile water at a minimum concentration of 100 µg/ml. The reconstituted solution can then be further diluted into other aqueous solutions as needed.
Stability
Lyophilized VEGFR-2 remains stable at room temperature for up to 3 weeks. However, for extended storage, it is recommended to store the lyophilized powder desiccated at temperatures below -18°C. After reconstitution, FLK1 should be stored at 4°C for 2-7 days. For long-term storage, it is advisable to store at temperatures below -18°C. The addition of a carrier protein, such as 0.1% HSA or BSA, is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% as assessed by SDS-PAGE analysis.
Synonyms
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
Source
Insect Cells.
Amino Acid Sequence
ASVGLPSVSLD LPRLSIQKDI LTIKANTTLQ ITCRGQRDLD WLWPNNQSGS EQRVEVTECS DGLFCKTLTI PKVIGNDTGA YKCFYRETDL ASVIYVYVQD YRSPFIASVS DQHGVVYITE NKNKTVVIPC LGSISNLNVS LCARYPEKRF VPDGNRISWD SKKGFTIPSY MISYAGMVFC EAKINDESYQ SIMYIVVVVG YRIYDVVLSP SHGIELSVGE KLVLNCTART ELNVGIDFNW EYPSSKHQHK KLVNRDLKTQ SGSEMKKFLS TLTIDGVTRS DQGLYTCAAS SGLMTKKNST FVRVHEKPFV AFGSGMESLV EATVGERVRI PAKYLGYPPP EIKWYKNGIP LESNHTIKAG HVLTIMEVSE RDTGNYTVIL TNPISKEKQS HVVSLVVYVP PQIGEKSLIS PVDSYQYGTT QTLTCTVYAI PPPHHIHWYW QLEEECANEP SQAVSVTNPY PCEEWRSVED FQGGNKIEVN KNQFALIEGK NKTVSTLVIQ AANVSALYKC EAVNKVGRGE RVISFHVTRG PEITLQPDMQ PTEQESVSLW CTADRSTFEN LTWYKLGPQP LPIHVGELPT PVCKNLDTLW KLNATMFSNS TNDILIMELK NASLQDQGDY VCLAQDRKTK KRHCVVRQLT VLERVAPTIT GNLENQTTSI GESIEVSCTA SGNPPPQIMW FKDNETLVED SGIVLKDGNR NLTIRRVRKE DEGLYTCQAC SVLGCAKVEA FFIIEGA.
Product Science Overview
Structure and Function
VEGFR2 is composed of several domains:
- Extracellular domain: This domain contains immunoglobulin-like loops that are responsible for binding to the Vascular Endothelial Growth Factor (VEGF) ligands.
- Transmembrane domain: This hydrophobic segment anchors the receptor in the cell membrane.
- Intracellular domain: This domain possesses tyrosine kinase activity, which is crucial for signal transduction.
Upon binding to its ligand, VEGF, VEGFR2 undergoes dimerization and autophosphorylation on specific tyrosine residues within the intracellular domain. This activation triggers a cascade of downstream signaling pathways that promote endothelial cell proliferation, migration, and survival .
Role in Angiogenesis
VEGFR2 is the primary mediator of VEGF-induced angiogenic signaling. The interaction between VEGF and VEGFR2 is essential for:
- Endothelial cell proliferation: VEGFR2 activation stimulates the division and growth of endothelial cells.
- Endothelial cell migration: It promotes the movement of endothelial cells to sites where new blood vessels are needed.
- Survival of endothelial cells: VEGFR2 signaling helps in the maintenance and survival of these cells under various physiological and pathological conditions .
Therapeutic Implications
Given its pivotal role in angiogenesis, VEGFR2 is a significant target for anti-angiogenic therapies, particularly in cancer treatment. Inhibiting VEGFR2 can effectively reduce tumor growth by restricting the blood supply to the tumor. Several therapeutic strategies have been developed to target VEGFR2, including:
Recombinant VEGFR2
Recombinant VEGFR2 refers to the receptor produced through recombinant DNA technology. This involves inserting the gene encoding VEGFR2 into a suitable expression system, such as mammalian cells, to produce the receptor in vitro. Recombinant VEGFR2 is used extensively in research to study its structure, function, and role in angiogenesis. It is also employed in screening assays to identify potential inhibitors or activators of VEGFR2 signaling .
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