| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1. |
| Biological Activity | |
| Cellular Localization | |
| Concentration | |
| Expression System | |
| Form | Sterile Filtered White lyophilized (freeze-dried) powder. |
| Formulation | |
| Product Type | |
| Protein Length | |
| Protein Size | |
| Purity | |
| Solubility | It is recommended to reconstitute the lyophilized FLT1 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions. |
| Source | Insect Cells. |
| Species | |
| Storage | |
| Target |
Recombinant Human Vascular Endothelial Growth Factor receptor-1 is supplied as a recombinant protein for in vitro research use.
Background
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in
1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
Product format
Provided as a recombinant protein suitable for in vitro workflows such as binding studies, screening, and assay development. Refer to the specifications table for expression format and molecular properties.
What is the purity of Recombinant Human Vascular Endothelial Growth Factor receptor-1 (Human)?
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE. BioHippo includes a Certificate of Analysis (CoA) confirming purity per lot with every order.
What buffer / formulation is this protein supplied in?
How should Recombinant Human Vascular Endothelial Growth Factor receptor-1 (Human) be stored?
What expression system was used to produce this protein?
Is this protein biologically active?
Is this protein approved for clinical or in vitro diagnostic use?
Can I request a custom size, tag variant, or formulation?
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
