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VEGF-A

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Recombinant Human VEGF-A thumbnail image 1 Recombinant Human VEGF-A thumbnail image 2
Recombinant Human VEGF-A gallery image 1
Human Anti-Ranibizumab Antibody antigen capture ELISA for pharmacokinetic (PK) assay development

A microtiter plate was coated overnight with recombinant human VEGF-A (PHP293) at a concentration of 5 µg/ml. After washing and blocking with PBST+5% BSA, 10% human serum was added spiked with increasing concentrations of ranibizumab. Detection was performed using Human Anti-Ranibizumab Antibody, clone AbD29928 (HCA304) at a concentration of 2 µg/ml and a rat anti-DYKDDDDK-tag antibody in HISPEC Assay Diluent (BUF049A) followed by QuantaBlu Fluorogenic Peroxidase Substrate. Data are shown as the mean of three measurements.
Recombinant Human VEGF-A gallery image 2
Human Anti-Ranibizumab Antibody antigen capture ELISA for pharmacokinetic (PK) assay development

A microtiter plate was coated overnight with recombinant human VEGF-A (PHP293) at a concentration of 5 µg/ml. After washing and blocking with PBST+5% BSA, 10% human serum was added spiked with increasing concentrations of bevacizumab. Detection was performed using Human Anti-Ranibizumab Antibody, clone AbD29865 (HCA307, cross-reactive with bevacizumab) at a concentration of 2 μg/ml and a rat anti-DYKDDDDK-tag antibody in HISPEC Assay Diluent (BUF049A) followed by QuantaBlu Fluorogenic Peroxidase Substrate. Data are shown as the mean of three measurements.

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Recombinant Human VEGF-A

Product Type
Recombinant Protein
Specificity
VEGF-A

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Product Code Applications Pack Size List Price Your Price Qty
PHP293
Datasheet Datasheet Datasheet
SDS Safety Datasheet SDS
E 0.2 mg loader
List Price Your Price
loader

Recombinant Human VEGF-A
Vascular endothelial growth factor alpha forms a homodimer and is a potent stimulator of angiogenesis of both normal and cancerous cells. It acts as a regulator of vasculogenesis, angiogenesis and endothelial cell growth. VEGF-A is secreted by many different cell types such as endothelial cells (Nissen et al. 1998), smooth muscle cells (Brogi et al. 1994), neutrophils (Gaudry et al. 1997), platelets (Banks et al. 1998), macrophages and 60% of all tumours (Berse et al. 1992).

The sequence of this recombinant protein product is amino acid (aa) 27 - aa 141 + CDKPRR but deficient from aa 142-226, and it is closest to isoform 121. Isoform 121 and 111 lack exons 6 and 7, and for this reason neither of these isoforms bind to the extracellular matrix (Krilleke et al. 2017). This product has been demonstrated for use, in a pharmacokinetic (PK) antigen capture ELISA with the monoclonal antibody drugs ranibizumab and bevacizumab using anti-ranibizumab antibodies for detection.

Target Species
Human
Product Form
Purified recombinant protein - lyophilized
Reconstitution
Centrifuge vial prior to reconstitution. Reconstitute to 0.5 mg/ml by adding 0.4 ml ddH2O.
Care should be taken during reconstitution as the protein may appear as a film at the bottom of the vial. Mix gently after reconstitution. Do not vortex.
Preparation
Recombinant protein expressed in E. coli and purified by affinity chromatography
Source
E.coli
Buffer Solution
20 mM Phosphate Buffer, 0.1 M Sodium Chloride
Preservative Stabilisers
1% Trehalose
Purity
≥90% determined by SDS-PAGE under reducing conditions and visualized by coomassie blue staining
Approx. Protein Concentrations
0.5 mg/ml after reconstitution
Protein Molecular Weight
Predicted 14 kDa. The apparent molecular mass of the human VEGF-A monomer is approximately 17 kDa determined by SDS-PAGE under reducing conditions, and 17 kDa (monomer) and 30 kDa (dimer) under non-reducing conditions.
Regulatory
For research purposes only
Guarantee
Guaranteed for 3 months from the date of reconstitution or until the date of expiry, whichever comes first. Please see label for expiry date.

Prior to reconstitution store at -70oC. Following reconstitution store at -20oC.

This product should be stored undiluted.

Storage in frost-free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the protein.

This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Application Name Verified Min Dilution Max Dilution
ELISA
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.

Description Product Code Applications Pack Size List Price Your Price Quantity
Human anti Ranibizumab (Drug/Target Complex) HCA304 E 0.1 mg loader
List Price Your Price
loader
Description Human anti Ranibizumab (Drug/Target Complex)
Human anti Ranibizumab HCA307 E 0.1 mg loader
List Price Your Price
loader
Description Human anti Ranibizumab

Further Reading

  1. Krilleke, D. et al. (2007) Molecular mapping and functional characterization of the VEGF164 heparin-binding domain.
    J Biol Chem. 282 (38): 28045-56.
  2. Berse, B. et al. (1992) Vascular permeability factor (vascular endothelial growth factor) gene is expressed differentially in normal tissues, macrophages, and tumors.
    Mol Biol Cell. 3 (2): 211-20.
  3. Gaudry, M. et al. (1997) Intracellular pool of vascular endothelial growth factor in human neutrophils.
    Blood. 90 (10): 4153-61.
  4. Banks, R.E. et al. (1998) Release of the angiogenic cytokine vascular endothelial growth factor (VEGF) from platelets: significance for VEGF measurements and cancer biology.
    Br J Cancer. 77 (6): 956-64.
  5. Brogi, E. et al. (1994) Indirect angiogenic cytokines upregulate VEGF and bFGF gene expression in vascular smooth muscle cells, whereas hypoxia upregulates VEGF expression only.
    Circulation. 90 (2): 649-52.
  6. Nissen, N.N. et al. (1998) Vascular endothelial growth factor mediates angiogenic activity during the proliferative phase of wound healing.
    Am J Pathol. 152 (6): 1445-52.

UniProt
P15692

PHP293

153177 157461 159087 164050

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