VEGFA
(Vascular Endothelial Growth Factor A (VEGFA))
Type de proteíne
Recombinant
Activité biologique
Active
Attributs du protein
Transcript Variant 2
Origine
Humain
Source
HEK-293 Cells
Application
Functional Studies (Func), Antibody Production (AbP), Standard (STD), Protein Interaction (PI)
Specificité
Optimal preservation of protein structure, post-translational modifications and functions.
Attributs du produit
Recombinant human VEGF-A (transcript variant 2) protein expressed in HEK293.
Produced with end-sequenced ORF clone
Tested for bioactivity.
Pureté
> 98 % , as determined by Coomassie stained SDS-PAGE.
niveau d'endotoxine
Less than 0.01 ng per μg protein as determined by the LAL method.
Biological Activity Comment
The ED50 is 1 - 6 ng/ml, corresponding to a specific activity of 0.16 - 1.0 x 10^6 units/mg, determined by the dose dependent stimulation of HUVEC cells proliferation.
VEGFA
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
VEGFA
Origine: Souris
Hôte: Yeast (Pichia pastoris)
Recombinant
> 95 % as determined by SDS-PAGE
Indications d'application
Recombinant human proteins can be used for: Native antigens for optimized antibody production Positive controls in ELISA and other antibody assays Protein-protein interaction In vitro biochemical assays and cell-based functional assays
Restrictions
For Research Use only
Concentration
> 50 μg/mL
Buffer
5 mM citric acid, 5 mM NaHPO4, 0.15 M NaCl pH 4.0
Stock
-80 °C
Stockage commentaire
Store at -80°C. Thaw on ice, aliquot to individual single-use tubes, and then re-freeze immediately. Only 2-3 freeze thaw cycles are recommended.
Antigène
VEGFA
(Vascular Endothelial Growth Factor A (VEGFA))
This gene is a member of the PDGF/VEGF growth factor family. It encodes a heparin-binding protein, which exists as a disulfide-linked homodimer. This growth factor induces proliferation and migration of vascular endothelial cells, and is essential for both physiological and pathological angiogenesis. Disruption of this gene in mice resulted in abnormal embryonic blood vessel formation. This gene is upregulated in many known tumors and its expression is correlated with tumor stage and progression. Elevated levels of this protein are found in patients with POEMS syndrome, also known as Crow-Fukase syndrome. Allelic variants of this gene have been associated with microvascular complications of diabetes 1 (MVCD1) and atherosclerosis. Alternatively spliced transcript variants encoding different isoforms have been described. There is also evidence for alternative translation initiation from upstream non-AUG (CUG) codons resulting in additional isoforms. A recent study showed that a C-terminally extended isoform is produced by use of an alternative in-frame translation termination codon via a stop codon readthrough mechanism, and that this isoform is antiangiogenic. Expression of some isoforms derived from the AUG start codon is regulated by a small upstream open reading frame, which is located within an internal ribosome entry site.