FLT1 D7 Human

Vascular Endothelial Growth Factor Receptor-1 D1-7 Human Recombinant
Cat. No.
BT21255
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.
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Description

Soluble FLT1 Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric, glycosylated, polypeptide containing 751 amino acids and having a molecular mass of 130 kDa. The soluble receptor protein contains only the first 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. The FLT1 fc/Chimera 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, known as 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. Each VEGF receptor shares structural similarities, including seven immunoglobulin-like extracellular domains, a single transmembrane region, and an intracellular split tyrosine kinase domain. While VEGFR-2 exhibits a lower affinity for VEGF compared to Flt-1, it demonstrates greater signaling activity. Notably, VEGFR-2 plays a crucial role in endothelial cell proliferation by mediating mitogenic activity. The flt-1 gene undergoes differential splicing, resulting in a soluble variant known as sVEGFR-1. However, no naturally occurring secreted forms of VEGFR-2 have been identified. Heparin plays a vital role in facilitating the binding of VEGF165 to VEGFR-2.
Description
Recombinant human soluble FLT1, fused with the Fc region of human IgG1, is produced in a baculovirus expression system. This disulfide-linked homodimeric glycoprotein consists of 751 amino acids, boasting a molecular weight of 130 kDa. The soluble receptor encompasses only the first seven extracellular domains (Met1-Thr751), which are sufficient for high-affinity ligand binding. The purification process of FLT1 Fc/Chimera involves proprietary chromatographic techniques.
Physical Appearance
White, lyophilized powder, sterile-filtered.
Formulation
FLT1 D1-7 undergoes lyophilization from a sterile solution at a concentration of 1 mg/ml in PBS buffer with a pH of 7.4.
Solubility
For reconstitution, it is recommended to dissolve the lyophilized FLT1 Fc/Chimera in PBS at a minimum concentration of 50 µg/ml. Further dilutions can be prepared in other aqueous solutions.
Stability
Lyophilized FLT-1 demonstrates stability at room temperature for a period of 3 weeks. However, for optimal storage, it is recommended to store the desiccated product at a temperature below -18°C. Upon reconstitution, FLT1 should be stored at 4°C for a period of 2-7 days. For long-term storage, it is advisable to aliquot and store the reconstituted protein below -18°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for enhanced stability during long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of the protein is determined to be greater than 95.0% by SDS-PAGE analysis.
Biological Activity
The biological activity of FLT1/Fc is assessed by its capacity to inhibit VEGF-dependent proliferation in human umbilical vein endothelial cells. The ED50 for this inhibitory effect typically falls within the range of 10-30 ng/ml, corresponding to a specific activity of 33,333.33-100,000 units/mg.
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
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK IQQEPGIILG PGSSTLFIER VTEEDEGVYH CKATNQKGSV ESSAYLTVQG TAASDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI S.

Product Science Overview

Introduction

Vascular Endothelial Growth Factor Receptor-1 (VEGFR-1), also known as Flt-1, is a high-affinity tyrosine kinase receptor that plays a crucial role in angiogenesis and vasculogenesis. It binds to several ligands, including VEGF-A, VEGF-B, and placental growth factor (PlGF) . The recombinant form of VEGFR-1 D1-7 (Human) is a truncated version that includes the first seven immunoglobulin-like domains of the extracellular region, which are essential for ligand binding.

Structure and Function

VEGFR-1 is composed of an extracellular domain with seven immunoglobulin-like loops, a single transmembrane helix, and an intracellular tyrosine kinase domain. The D1-7 fragment specifically refers to the extracellular portion, which is responsible for binding VEGF ligands. This binding initiates a cascade of downstream signaling pathways that regulate endothelial cell proliferation, migration, and survival .

Role in Angiogenesis

VEGFR-1 is primarily involved in the regulation of angiogenesis, the process by which new blood vessels form from pre-existing vessels. This receptor modulates the activity of VEGF-A, a potent angiogenic factor, by acting as a decoy receptor that sequesters VEGF-A, thereby preventing it from binding to VEGFR-2, which has a higher signaling activity . This regulatory mechanism is crucial for maintaining the balance between angiogenesis and vascular stability.

Clinical Significance

The expression of VEGFR-1 is upregulated in various pathological conditions, including cancer, where it contributes to tumor angiogenesis and metastasis. Inhibiting VEGFR-1 signaling has been explored as a therapeutic strategy to suppress tumor growth and progression . Additionally, VEGFR-1 is implicated in inflammatory diseases, where it mediates the recruitment of monocytes and macrophages to sites of inflammation .

Recombinant VEGFR-1 D1-7

The recombinant form of VEGFR-1 D1-7 is produced using recombinant DNA technology, which involves the insertion of the VEGFR-1 gene into an expression vector, followed by the expression of the protein in a suitable host system, such as insect cells . This recombinant protein is used in various research applications, including the study of VEGF signaling pathways, the development of anti-angiogenic therapies, and the screening of potential drug candidates.

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