Abcam, ab150375, Anti-EG-VEGF antibody [EPR9699]

Size: 100µL / 1mL
Rabbit Recombinant Monoclonal EG-VEGF antibody. Suitable for WB, Flow Cyt (Intra) and reacts with Human, Mouse samples. Cited in 14 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR9699,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Human,
Applications:Flow Cyt (Intra), WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies
Species reactivity
Rat: We have preliminary internal testing data to indicate this antibody may not react with this species.
Please
contact us
for more information.

Properties and Storage Information:
Form-Liquid, Purity-Tissue culture supernatant, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
EG-VEGF also known as endocrine gland-derived vascular endothelial growth factor or prokineticin 1 is a potent angiogenic mitogen. It typically has a molecular mass of around 9 kDa. EG-VEGF is expressed mainly in steroidogenic tissues such as the ovaries testes adrenal glands and placenta. It targets endothelial cells selectively within these glands inducing various responses like proliferation migration and fenestration. This selectivity makes it distinct from vascular endothelial growth factor A (VEGF-A) which has a broader expression pattern.
Biological function summary
EG-VEGF plays a critical role in the formation and remodeling of blood vessels specific to endocrine glands. It is not part of a larger protein complex but operates through interaction with its receptor prokineticin receptor 1 (PROKR1). This unique interaction means that it has a specific ligand-receptor activity contributing to the regulation of vascular development especially in tissues undergoing hormonal changes. This makes EG-VEGF significant in contexts where localized and specific angiogenesis is essential.
Pathways
EG-VEGF is important in the regulation of angiogenesis and endothelial function. It fits into pathways that influence cell signaling associated with vascular development. One such pathway is the hypoxia-inducible factor (HIF) pathway which enhances the expression of EG-VEGF under low oxygen conditions. Another related protein is vascular endothelial growth factor (VEGF) whereby VEGF and EG-VEGF demonstrate distinctive yet occasionally overlapping functions in angiogenesis optimizing vascular growth within specific environments.
EG-VEGF shows associations with conditions like preeclampsia and polycystic ovary syndrome (PCOS). Preeclampsia involves improper vascularization in the placenta where EG-VEGF's role in angiogenesis becomes critical as it may help or disrupt proper vascular development. Polycystic ovary syndrome a hormonal disorder impacting ovaries also links with EG-VEGF through its effect on ovarian blood vessels. These disorders highlight potential therapeutic targets considering EG-VEGF’s integration with other proteins like PROKR1 which could modulate its angiogenic functions.