FLT1 D7 Mouse

Vascular Endothelial Growth Factor Receptor-1 D1-7 Mouse Recombinant
Cat. No.
BT21321
Source
Insect Cells.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
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.
Shipped with Ice Packs
In Stock

Description

Soluble FLT1 Mouse Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric , polypeptide containing 965 amino acids. The monomers have a molecular mass of 130 kDa. The soluble receptor protein contains all 7 extracellular domains (Tyr23-Asn757), which contain all the information necessary for high affinity ligand binding.

Product Specs

Introduction
Vascular endothelial growth factor (VEGF) receptors are primarily found on endothelial cells and play a crucial role in angiogenesis (blood vessel formation). There are three main types: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). These receptors are tyrosine kinases, meaning they activate signaling pathways within cells upon VEGF binding. VEGFR-2 is particularly important for mediating the mitogenic effects of VEGF, leading to endothelial cell proliferation. While all three receptors are membrane-bound, a soluble form of VEGFR-1 (sVEGFR-1) exists, created by alternative splicing of the Flt-1 gene. sVEGFR-1 can bind to VEGF, potentially regulating its availability for binding to cell-surface receptors.
Description
This product consists of the extracellular domain of mouse VEGFR-1 (soluble FLT1), fused to the Fc region of human IgG1. It is produced in baculovirus as a disulfide-linked homodimer. Each monomer has a molecular weight of 130 kDa, comprising amino acids Tyr23-Asn757, encompassing all seven extracellular domains responsible for high-affinity VEGF binding.
Physical Appearance
White powder, sterile-filtered and lyophilized.
Formulation
Lyophilized from a sterile solution of 1 mg/ml in phosphate-buffered saline (PBS).
Solubility
Reconstitute the lyophilized FLT1 Fc/Chimera in PBS at a minimum concentration of 50 µg/ml. Further dilutions can be made in other aqueous solutions.
Stability
Lyophilized FLT-1 is stable for 3 weeks at room temperature. However, it is recommended to store desiccated below -18°C. After reconstitution, FLT1 can be stored at 4°C for 2-7 days. For long-term storage, store below -18°C with the addition of a carrier protein like HSA or BSA (0.1%). Avoid repeated freeze-thaw cycles.
Purity
Purity determined to be greater than 95% by SDS-PAGE.
Biological Activity
The biological activity of sVEGFR-1/Fc is assessed by its capacity to inhibit VEGF-driven proliferation of human umbilical vein endothelial cells.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Source
Insect Cells.
Amino Acid Sequence
YGSGSKLKVP ELSLKGTQHV MQAGQTLFLK CRGEAAHSWS LPTTVSQEDK RLSITPPSAC GRDNRQFCST LTLDTAQANH TGLYTCRYLP TSTSKKKKAE SSIYIFVSDA GSPFIEMHTD IPKLVHMTEG RQLIIPCRVT SPNVTVTLKK FPFDTLTPDG QRITWDSRRG FIIANATYKE IGLLNCEATV NGHLYQTNYL THRQTNTILD VQIRPPSPVR LLHGQTLVLN CTATTELNTR VQMSWNYPGK ATKRASIRQR IDRSHSHNNV FHSVLKINNV ESRDKGLYTC RVKSGSSFQS FNTSVHVYEK GFISVKHRKQ PVQETTAGRR SYRLSMKVKA FPSPEIVWLK DGSPATLKSA RYLVHGYSLI IKDVTTEDAG DYTILLGIKQ SRLFKNLTAT LIVNVKPQIY EKSVSSLPSP PLYPLGSRQV LTCTVYGIPR PTITWLWHPC HHNHSKERYD FCTENEESFI LDPSSNLGNR IESISQRMTV IEGTNKTVST LVVADSQTPG IYSCRAFNKI GTVERNIKFY VTDVPNGFHV SLEKMPAEGE DLKLSCVVNK FLYRDITWIL LRTVNNRTMH HSISKQKMAT TQDYSITLNL VIKNVSLEDS GTYACRARNI YTGEDILRKT EVLVRDSEAP HLLQNLSDYE VSISGSTTLD CQARGVPAPQ ITWFKNNHKI QQEPGIILGP GNSTLFIERV TEEDEGVYRC RATNQKGAVE SAAYLTVQGT SDKSNAASDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSREEMTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPMLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGK

Product Science Overview

Introduction

Vascular Endothelial Growth Factor Receptor-1 (VEGFR-1), also known as Flt-1, is a receptor tyrosine kinase that plays a crucial role in the regulation of angiogenesis and vasculogenesis. It is one of the key receptors for vascular endothelial growth factors (VEGFs), which are essential for the development and maintenance of blood and lymphatic vessels .

Structure and Domains

VEGFR-1 is composed of several domains, including seven immunoglobulin-like domains (D1-D7) in its extracellular region, a single transmembrane domain, and an intracellular tyrosine kinase domain . The D1-D7 domains are critical for ligand binding and receptor activation. The recombinant form of VEGFR-1 D1-7 (Mouse) is a truncated version that includes only the extracellular ligand-binding domains, making it useful for studying ligand-receptor interactions and signaling pathways .

Ligands and Binding Specificity

VEGFR-1 binds to multiple ligands, including VEGF-A, VEGF-B, and Placenta Growth Factor (PlGF). Among these, VEGF-A and PlGF are particularly important for angiogenesis. VEGF-A binds to both VEGFR-1 and VEGFR-2, while VEGF-B and PlGF bind exclusively to VEGFR-1 . The binding of these ligands to VEGFR-1 triggers a cascade of downstream signaling events that promote endothelial cell proliferation, migration, and survival .

Biological Functions

VEGFR-1 has distinct biological functions compared to other VEGF receptors. While VEGFR-2 is primarily responsible for mediating angiogenic signals, VEGFR-1 acts as a decoy receptor that modulates the availability of VEGF ligands for VEGFR-2. This regulatory mechanism ensures a balanced angiogenic response . Additionally, VEGFR-1 is involved in the recruitment of monocytes and macrophages to sites of inflammation and tissue repair .

Therapeutic Implications

The recombinant form of VEGFR-1 D1-7 (Mouse) has significant therapeutic potential. It can be used to develop VEGFR-1 inhibitors that block ligand binding and receptor activation, thereby inhibiting pathological angiogenesis in diseases such as cancer and age-related macular degeneration . Furthermore, understanding the structural and functional aspects of VEGFR-1 can aid in the design of targeted therapies for various vascular disorders .

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