Recombinant Human Vascular Endothelial Growth Factor D (VEGFD) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08393P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Vascular Endothelial Growth Factor D (VEGFD) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08393P
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Product Overview

Description Recombinant Human Vascular Endothelial Growth Factor D (VEGFD) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb O43915
Target Symbol VEGFD
Synonyms c-fos induced growth factor; c-fos induced growth factor (vascular endothelial growth factor D); c-fos induced growth factor; c-fos-induced growth factor; FIGF; Vascular endothelial growth factor D; Vascular endothelial growth factor D precursor; Vascular endothelial growth factor D precursor; VEGF D; VEGF-D; VEGFD; VEGFD_HUMAN
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence FAATFYDIETLKVIDEEWQRTQCSPRETCVEVASELGKSTNTFFKPPCVNVFRCGGCCNEESLICMNTSTSYISKQLFEISVPLTSVPELVPVKVANHTGCKCLPTAPRHPYSIIRR
Expression Range 89-205aa
Protein Length Full Length of Mature Protein
Mol. Weight 40.1kDa
Research Area Cancer
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in the formation of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors.
Subcellular Location Secreted.
Protein Families PDGF/VEGF growth factor family
Database References
Tissue Specificity Highly expressed in lung, heart, small intestine and fetal lung, and at lower levels in skeletal muscle, colon, and pancreas.

Gene Functions References

  1. SPARC expression was inversely associated with the degree of malignancy and it had a negative correlation with VEGF-C and VEGF-D expression. Results suggest SPARC might function as a tumor suppressor inhibiting angiogenesis and lymphangiogenesis in ovarian cancer by reducing the expression of VEGF-C and VEGF-D. PMID: 29075785
  2. Serum VEGF-D levels were significantly increased in definite lymphangioleiomyomatosis (LAM) patients compared with healthy controls. Serum VEGF-D levels were significantly increased in definite LAM patients who had chylothorax compared with those without chylothorax. PMID: 29906075
  3. no difference in the levels of VEGF-A, VEGF-C, and VEGF-D in pre-eclampsia compared to normotensive pregnant women stratified by HIV status PMID: 28524736
  4. CXCR4, CCR7, VEGF-C and VEGF-D expression might have synergistic effects on the lymph node metastasis in patients with cervical cancer. PMID: 28535405
  5. VEGF-D-induced changes in serine/threonine kinase mTOR shuttling between the cytosol and nucleus and its increased phosphorylation at Ser-2448, lead us to the conclusion that the observed shift in redox balance is regulated via mTOR kinase signalling. PMID: 27957793
  6. High VEGFD expression is associated with lymphangioleiomyomatosis. PMID: 28202529
  7. Data show that VEGF-C, VEGF-D, and VEGFR-3 were expressed in a substantial percentage of breast carcinomas. PMID: 28791841
  8. High VEGFD expression is associated with angiogenesis and lymphangiogenesis. PMID: 27852824
  9. VEGF-D and its receptors were co-localized on blood vessels in clinical samples of human lungs exposed to hyperoxia; hence, VEGF-D may act directly on blood vessels to promote fluid leak. PMID: 26924464
  10. VEGF-D-enhanced metastasis was evidently reversed by MP. MP significantly reduced the invasion of VEGFD-SK cells, tumor volume, lymphatic metastasis rates and lymphatic vessel density compared with control groups PMID: 27211072
  11. Sulf2 facilitated lymphangiogenesis in breast cancer cells by regulating VEGF-D and that the AKT1related signaling pathway was involved. PMID: 27748846
  12. Data indicate that vascular endothelial growth factor D (VEGF-D) was the best indicator of metastasis and vascular endothelial growth factors and receptor-3 (VEGFR-3) may help to determine the prognosis and management of colorectal cancer (CRC). PMID: 26476536
  13. Taken together, our data suggest that TNF-alpha can promote lymphangiogenesis and lymphatic metastasis of GBC through the ERK1/2/AP-1/VEGF-D pathway. PMID: 26992854
  14. VEGF-D may play an important role in the process of lymphatic metastasis of epithelial ovarian cancer PMID: 23915006
  15. CCL21/CCR7 induce VEGF-D up-regulation and promote lymphangiogenesis via ERK/Akt pathway in lung cancer. PMID: 26884842
  16. The most extensively accepted signaling pathways promoting lymphangiogenesis in tumors include the secreted lymphangiogenic proteins: VEGF-C and VEGF-D, and their cognate receptor on lymphatic endothelium VEGF receptor-3 (VEGFR-3). PMID: 26706909
  17. Study demonstrated that VEGF-D upregulates myofibroblast proliferation, migration, and collagen synthesis through activation of VEGF pathway. PMID: 26724950
  18. MTA1 is up-regulated in CRC; its expression is inversely associated with lymphatic metastases and the expression of VEGFC, VEGFD and VEGFR3 PMID: 26543080
  19. VEGF-C/D score correlated neither with periphery Lymphatic vessel density (LVD) nor with LVD in the tumor center PMID: 26296919
  20. study suggests that both VEGF-C and VEGF-D in tumor cells promote lymph node metastasis PMID: 25911567
  21. A positive association for VEGF-D and an inverse association for MMP-2 were observed in patients with positive lymph node status at the time of radical cystectomy in urothelial carcinoma of the bladder. PMID: 26241709
  22. These findings suggest that IL-8 may be a potent inducer of LECs, although this effect does not appear to involve the VEGF-C/VEGF-D and VEGFR-3 signaling pathway. PMID: 25891418
  23. fluid shear stress induces the synthesis of Insulin growth factor-2 and vascular endothelial growth factor (VEGF) B and D, which in turn transactivate MMP-12. PMID: 25435370
  24. Among VEGF homologs, MMPE from various kinds of tumor origin, VEGF-D showed 92.6% rate of positive expression. ICC stain of VEGF-D is a useful marker in the aid of MMPE diagnosis. PMID: 25221955
  25. The preoperative sVEGF-C/D levels might be reliable biomarkers for the presence of disease and LNM in patients with GBC. The sVEGF-C/D levels may be prognosis factors that can predict a poor outcome for GBC patients PMID: 25801241
  26. VEGF-D is involved in the development of lymphangiogenesis in peritoneal dialysis patients. PMID: 26121315
  27. Both VEGF-C and VEGF-D are highly expressed in esophageal squamous cell cancer tissue, which may be related to the lymph node metastasis of cancer cells. PMID: 25640364
  28. predictive value of VEGF-D expression for bevacizumab may depend on the chemotherapy backbone used PMID: 26125443
  29. Transforming growth factor-beta1 downregulates vascular endothelial growth factor-D expression in human lung fibroblasts via the Jun NH2-terminal kinase signaling pathway PMID: 24515257
  30. Increase of VEGFD protein expression is associated with oral squamous cell carcinoma. PMID: 24085575
  31. overexpression of lymphangiogenic factors VEGF-C and VEGF-D in colon adenocarcinoma was associated with increased vessel density in tumor-surrounding stroma. PMID: 24173916
  32. Predictive marker analysis indicated that plasma levels of VEGF-D, Ang2, and SDF1 significantly predicted for benefit or lack of benefit from bevacizumab in this population. PMID: 24097873
  33. VEGF-D promotes lymph node metastasis by increasing tumor lymphangiogenesis, stimulating draining lymphatic vessel formation and enhancing tumor invasiveness. PMID: 24502459
  34. High VEGF-D is associated with gastric cancer. PMID: 23238856
  35. Dysregulated expression of VEGF-D likely contributes to altered angiogenesis, lymphangiogenesis, neurogenesis and immune function in endometriosis. PMID: 23585340
  36. The expression of VEGFR-3 and its ligands, VEGF-C and VEGF-D, significantly increased after activating ET(B)R by ET-1 in primary and metastatic melanoma cell lines PMID: 22965194
  37. Serum VEGF-D may be useful for monitoring response to treatment with sirolimus and kidney angiomyolipoma size in patients with tuberous sclerosis complex. PMID: 23437092
  38. Serum vascular endothelial growth factor (VEGF)-D is significantly elevated in patients with lymphangioleiomyomatosis and is a better diagnostic marker than matrix metalloproteinase (MMP)-2, MMP-9 and ACE. PMID: 22513045
  39. The propeptides profoundly influence molecular interactions of VEGF-D with VEGF receptors, co-receptors, and heparin, and its effects on tumor biology. PMID: 23404505
  40. Peritumoral lymphangiogenesis induced by vascular endothelial growth factor D promotes lymph node metastasis in breast cancer. PMID: 22906075
  41. Correlation between intensity of AT-1R expression and expression of lymph- and angiogenesis markers in IDC was examined. Expression intensity of AT-1R was found to correlate with expressions of VEGF-A (r = 0.26; p = 0.008)and VEGF-D (r = 0.24; p = 0.015). PMID: 22581182
  42. Lymphatic microvessel density, VEGF-C and VEGF-D could predict poor prognosis in patients with breast cancer. PMID: 23054001
  43. VEGFD added to the culture medium increased the number of cells expressing tyrosine hydroxylase (a marker for DA neurons) and betaIII-tubulin (a marker for DA neurons) and betaIII-tubulin (a marker for immature neurons) in both the NTera2 and I6 cell lines. PMID: 22535492
  44. results demonstrated that ET-1 and hypoxia act, at list in part, through VEGF to induce lymphangiogenic events and that these two stimuli may cooperate to induce VEGF-A/-C/-D expression and lymphatic differentiation. PMID: 22552325
  45. Differential capacity for VEGF-D production and integrin alpha 9 beta 1 expression by human breast cancer cell line MDA-MB-468LN jointly contributed to their lymphatic metastatic phenotype. PMID: 22545097
  46. VEGF-D has a role in progestin-induced break-through bleeding in thin-walled blood and lymphatic endometrial vessels PMID: 22383980
  47. These data demonstrate that the VEGF-D serum levels are reduced in patients with metastases of differentiated thyroid cancer, regardless of the degree of metastatic spread. PMID: 21781145
  48. A significant relationship was found in salivary gland tumors with myoepithelial differentiation regarding simultaneous positive staining for VEGF-C/VEGF-D and flt-4 PMID: 22326635
  49. Vascular endothelial growth factor D was expressed in 4 of 7 primary and 7 of 7 metastatic lesions. In culture, vascular endothelial growth factor D significantly increased the migration of sarcoma cells through lymphatic endothelial monolayers. PMID: 22326461
  50. VEGF-D is involved and plays an important role in gallbladder cancer (GBC), progression, suggesting that VEGF-D may be a potential molecular target in the treatment of GBC. PMID: 22071224

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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.

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