Recombinant Pig VEGFA Protein

Beta LifeScience SKU/CAT #: BLA-2238P

Recombinant Pig VEGFA Protein

Beta LifeScience SKU/CAT #: BLA-2238P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Host Species Pig
Accession P49151
Synonym Folliculostellate cell-derived growth factor Glioma-derived endothelial cell mitogen MGC70609 MVCD1 vascular endothelial growth factor Vascular endothelial growth factor A vascular endothelial growth factor A121 vascular endothelial growth factor A165 Vascular permeability factor Vegf VEGF A VEGF-A VEGF120 Vegfa VEGFA_HUMAN VPF
Description Recombinant Pig VEGFA Protein was expressed in Yeast. It is a Full length protein
Source Yeast
AA Sequence APMAEGDQKP HEVVKFMDVY QRSYCRPIET LVDIFQEYPD EIEYIFKPSC VPLMRCGGCC NDEGLECVPT EEFNITMQIM RIKPHQGQHI GEMSFLQHNK CECRPKKDRA RQENPCGPCS ERRKHLFVQD PQTCKCSCKN TDSRCKARQL ELNERTCRCD KPRR
Molecular Weight 19 kDa
Purity Greater than 95% SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at -20°C. Avoid freeze / thaw cycle.

Target Details

Target Function Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development.
Subcellular Location Secreted.
Protein Families PDGF/VEGF growth factor family
Database References

Gene Functions References

  1. It regulates endometrial remodeling in the porcine endometrial tissues during follicular and luteal phase. PMID: 28139071
  2. It was concluded that VEGF and factor VIII are important growth factors associated with fetal development in pigs and are identified in all uterine segments. PMID: 28237345
  3. results are consistent with a participation of (VEFG) in the regulation of the dynamics of oviductal fluid secretion and the oviduct contractibility PMID: 28257866
  4. Here we demonstrate that VEGF-165 mediates MSC differentiation into ECs via VEGFR-2-dependent induction of Sox18, which ultimately coordinates the transcriptional upregulation of specific markers of the EC phenotype. PMID: 25913202
  5. VEGF was significantly downregulated 7 days after cryotherapy of the sclera and stayed at that level until day 14. It returned to baseline by day 21. PMID: 25510786
  6. VEGF production, blood vessel network and follicle remodeling are impaired by the antiprogesterone RU486. PMID: 24756033
  7. findings suggest that the augmented neovascular response seen with VEGF administration was through the VEGF-induced upregulation of Notch signaling. PMID: 24366099
  8. interleukin-1beta-induced vascular endothelial growth factor in airway smooth muscle cells PMID: 24142467
  9. Upregulation of VEGF during hypoxia in chondrocyte is mediated partially through HIF-1alpha. PMID: 22970342
  10. data shows that members of the VEGF-VEGFR system are temporally and spatially well localized for playing key roles during umbilical cord formation and its intensive growth observed after day 75 of pregnancy PMID: 20825582
  11. cardiac-specific and hypoxia-induced coexpression of VEGF and Ang1 improves the perfusion and function of porcine MI heart through the induction of angiogenesis and cardiomyocyte proliferation PMID: 21245320
  12. The mRNA for VEGFA was expressed in early developing and in maturing glomeruli. PMID: 20713984
  13. Data show that subventricular zone neural stem cells express VEGF and all VEGF splice variants, VEGFR1, VEGFR2 and Neuropilin-1 and -2 mRNAs. PMID: 20552272
  14. The earlier increase in VEGF protein and mRNA expression in the Meishan versus the Yorkshire conceptus may explain the previously reported increased vascularity and increased placental efficiency of this breed compared the Yorkshire breed. PMID: 14998908
  15. Contrast media did not affect bone marrow cell viability/VEGF secretion. PMID: 15274157
  16. VEGF upregulation in the proliferative zone after ischemic damage may play a role in stimulating vascular invasion and granulation tissue formation in the necrotic hypertrophic zone of the epiphyseal cartilage PMID: 15537448
  17. Data demonstrate that lipopolysaccharides evoke a heat shock response, with an increase heat shock proteins 70 and Hsp32) and of VEGF, a specific endothelial cell growth factor. PMID: 16333987
  18. Vascular endothelial growth factor (VEGF) plays an important role in the thecal angiogenesis during follicular development. PMID: 16372043
  19. number of preovulatory follicles and the capillary density in the theca interna increased significantly in the ovaries injected with VEGF gene PMID: 16538032
  20. our study revealed the presence of VEGF in endothelial and smooth muscle cells of vascular subovarian plexus arteries PMID: 16584087
  21. Differential regulation of VEGF isoforms may suggest specific physiological roles for some of them, particularly in angioregression occurring during the apoptotic structural luteolysis. PMID: 16967516
  22. VEGF ligand-receptor system may play an important role in the development and maintenance of the corpus luteum in pigs. PMID: 17120307
  23. Sanguinarine inhibited both VEGF production and VEGF-induced Akt activation in swine granulosa cells. PMID: 17310078
  24. VEGF/Flk-1/Flt-1 system is activated during myocardial ischemia reperfusion injury. PMID: 17868880
  25. VEGF-A family members are probably involved in appropriate preparation of endometrium for implantation and in vascular events during implantation in pigs. PMID: 17874446
  26. Hemodialysis graft placement leads to early increases in wall shear stress, VEGF-A, pro-MMP-9, MMP-2, VEGFR-1, VEGFR-2, and TIMP-1, which may contribute to the development of venous stenosis. PMID: 18326810
  27. Interaction of soluble factors in plasma possibly generated during PICSO are not responsible for upregulation of HO-1 and VEGF mRNA. PMID: 19618599

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

Recently viewed