EMRK2, HUMAN Chemical Properties

storage temp. 

-70°C

form 

buffered aqueous glycerol solution

biological source

human

Specific Activity

30-40nmol/min·mg

Safety Information

Hazard Codes 

T

Risk Statements 

61

Safety Statements 

53-45

WGK Germany 

1

HS Code 

3504009000

EMRK2, HUMAN Usage And Synthesis

Uses

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Biological Activity

FLT1 (fms-related tyrosine kinase 1) or VEGFR (vascular endothelial growth factor receptor) is implicated in angiogenesis in tumors, which plays a key role in tumorigenesis, invasion and metastasis of tumors, especially the malignant ones. In human circulation, angiogenesis is balanced by soluble FLT1 (sFLT1) and VEGF. An imbalance leads to multiple conditions such as pre-eclampsia. sFLT1 plays an essential role in the angiogenesis of placenta. An overexpression of this protein in placenta is associated with prenatal arsenic exposure and thus, reduced birth weight.

Description

Soluble FLT1 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 687 amino acids and having a molecular mass of 96 kDa. The soluble receptor protein contains only the first 6 extracellular domains, which contain all the information necessary for binding of VEGF.
The FLT1 is purified by proprietary chromatographic techniques.

Source

Insect Cells

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.

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