Select country change
Shopping cart (0 , 0,00 ) Menu Search
Manufactured by BioVendor

VEGF-R2/KDR Human ELISA Kit

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:FLK1, Kinase insert domain receptor, CD309, VEGFR2
  • Species:Human
Please select your region to see available products and prices.
Cat. No. Size Price


RAF140R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Plasma-EDTA, Plasma-Heparin, Plasma-Citrate, Cell culture supernatant

Sample Requirements

50 µl/ well

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the complete kit at 2–8°C. Under these conditions, the kit is stable until the expiration date (see label on the box).

Calibration Curve

Calibration Range

78–5000 pg/ml

Limit of Detection

7.0 pg/ml

Intra-assay (Within-Run)

CV = 5.3%

Inter-assay (Run-to-Run)

CV = 9.8%

Summary

Research topic

Cytokines and chemokines and related molecules

Summary

Angiogenesis is a fundamental physiological process, both during the development of the organism and in adult life, requiring the well coordinated action of a variety of growth factors and adhesion molecules in endothelial cells. So far, VEGF-A (also called VEGF) and its receptors represent the best characterized signalling pathway in developmental and tumour angiogenesis. VEGF-A binds to two receptor-tyrosine kinases: VEGFR-1/Flt-1 and VEGFR-2/KDR. VEGFR-2 is the major mediator of the mitogenic, angiogenic and permeability-enhancing effects of VEGF-A.
The VEGFR’s possess an approximately 750 amino acid residue extracellular domain, which is organized into seven immunoglobulin (Ig)-like folds. This extracellular domain (also called ectodomain) is followed by a single transmembrane region, a juxtamembrane domain, a split tyrosine-kinase domain interrupted by a 70-amino acid kinase insert and a C-terminal tail. Alternative splicing or proteolytic processing of VEGFR’s give rise to secreted variants of VEGFR-2, also called soluble VEGFR-2 (sVEGFR-2). Although the VEGFR’s are primarily expressed in the vascular system, sensitive methods like sandwich ELISA’s have allowed the detection of VEGFR expression in non-endothelial cells like hematopoietic stem cells.
The important role of VEGFR-2 signalling during development and in neo-vascularization in physiological or pathological conditions in vivo has allowed the design of clinically beneficial therapies. A soluble form of VEGFR-2 protein can be detected in human and murine plasma. Studies confirmed that the detected soluble fragment was a truncated form of VEGFR-2, shed from mouse and human endothelial cells.
Since the activation of VEGFR-2 plays an important role in tumour angiogenesis, there is broad clinical interest in monitoring plasma soluble VEGFR-2 levels in cancer patients with a focus on its potential as a surrogate biomarker for disease progression as well as monitoring marker of the efficiency of anti-angiogenesis drugs. Using mouse models with human tumours a reverse relationship could be shown between the levels of sVEGFR-2 and tumour size.
Besides its putative role as a surrogate marker for tumour angiogenesis, naturally occurring sVEGFR-2 is a molecular regulator for VEGF and VEGFR signalling. Further investigations will reveal if sVEGFR-2 can arrest solid tumour angiogenesis and modulate metastasis.
The sandwich ELISA to detect, measure and quantify soluble and solubilized VEGFR-2 levels will help to explain recent clinical results for anti-angiogenic therapy and will allow further understanding of VEGFR-2 as biomarker for monitoring cancer progression and its possible role in modulation of vessel growth.

Related Products Docs