Recombinant Human Vascular Endothelial Growth Factor C (VEGFC) Protein (GST)

Name: Recombinant Human Vascular Endothelial Growth Factor C (VEGFC) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03589P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Vascular Endothelial Growth Factor C (VEGFC) 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	P49767
Target Symbol	VEGFC
Synonyms	Flt 4L; Flt4 ligand; FLT4 ligand DHM; Flt4-L; Flt4L; Vascular endothelial growth factor C; Vascular endothelial growth factor related protein; Vascular endothelial growth factor-related protein; VEGF C; VEGF-C; Vegfc; VEGFC_HUMAN; VRP
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	AHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGVATNTFFKPPCVSVYRCGGCCNSEGLQCMNTSTSYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRR
Expression Range	112-227aa
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, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates KDR/VEGFR2 and FLT4/VEGFR3 receptors.
Subcellular Location	Secreted.
Protein Families	PDGF/VEGF growth factor family
Database References	HGNC: 12682 OMIM: 601528 KEGG: hsa:7424 STRING: 9606.ENSP00000280193 UniGene: PMID: 30142879 The mutation induced skipping of exon 2 of VEGFC resulting in a frameshift and the introduction of a premature stop codon (p.Ala50ValfsTer18). The mutation leads to a loss of the entire VEGF-homology domain and the C-terminus. PMID: 30071673 VEGFR-3 and CAV3 expression demonstrated immunohistochemically in SMCs of the tunica media of SV grafts predicted their early restenosis in triple-vessel CAD patients. CAV2 protein expression in SMCs of ITA grafts indicated the risk of early graft failure both in double-vessel and triple-vessel CAD subjects. PMID: 29557990 VEGF-C expression and secretion in gastric cancer is downregulated by kallistatin. PMID: 29243194 Concomitant high expression of survivin and VEGF-C is closely associated with LNM status of PTC patients, which suggests their cooperation in the metastatic process. PMID: 29578160 TNFSF15, a cytokine mainly produced by blood endothelial cells, facilitates tumor lymphangiogenesis by upregulating VEGFC expression in A549 cells. PMID: 29890027 serum levels not elevated in patients with erythrodermic mycosis fungoides/Sezary syndrome PMID: 28925057 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 VEGF-A/VEGF-C analysis showed higher positivity in metastatic nodes and higher positivity in the surrounding negative nodes from positive cases in comparison with nonmetastatic patients. PMID: 28984690 this study shows that decidual NK cells facilitate the interaction between trophoblastic and endothelial cells via VEGF-C and HGF PMID: 28653669 Lymphangiogenesis during tubulointerstitial fibrosis to be associated with increased expression of CTGF and VEGF-C in human obstructed nephropathy as well as in diabetic kidney disease. vitro, CTGF induced VEGF-C production in HK-2 cells, while CTGF siRNA suppressed transforming growth factor beta1-induced VEGF-C upregulation. PMID: 28545716 study is the first to describe the mechanism of leptin-promoted lymphangiogenesis by upregulating VEGF-C expression in chondrosarcomas. PMID: 27345723 Retroperitoneal tumour progression in EOC patients is associated with high VEGF-C expression. PMID: 28591727 Mechanistic investigations indicated that BDNF facilitated VEGF-C-dependent lymphangiogenesis through the MEK/ERK/mTOR signaling pathway. PMID: 28771226 Results has shown that VEGF-C was highly expressed in non-small cell lung cancer (NSCLC) tissues and metastatic lymph nodes. VEGF-C expression levels was significantly correlated with lymph node metastasis in NSCLC. Along with CXCR4, VEGF-C might synergically promote lymphatic metastasis in lung cancer and might be a clinical predictor of lymph node metastasis in NSCLC patients. PMID: 28925100 CXCR4, CCR7, VEGF-C and VEGF-D expression might have synergistic effects on the lymph node metastasis in patients with cervical cancer. PMID: 28535405 prolactin induction of VEGF-C and Runx2 was inhibited partly by Carboxypeptidase-D inhibitors, implicating nitric oxide , produced by PRL-regulated Carboxypeptidase-D, in breast cancer progression PMID: 28364216 Study is the first to describe the mechanism of bFGF-promoted lymphangiogenesis by upregulating VEGF-C expression in chondrosarcomas. PMID: 27229532 eIF4E promoted cholangiocarcinoma cell metastasis by up-regulating the expression of VEGF-C, MMP-2 and suppressing E-cadherin expression. PMID: 27907907 High expression of VEGF-C in the primary tumour may be a good determinant for detection of occult tumour cells in the lymph nodes of OSCC cases. PMID: 27417330 document for the first time that CCL5 induces tumor lymphangiogenesis by the induction of VEGF-C in human cancer cells. PMID: 27166194 Data suggest that the BRG1/STAT3/VEGFC in tumor-associated lymphangiogenesis might lead to the discovery of novel therapeutic targets in the treatment of cancers with BRG1 loss of function. PMID: 27145366 Studied the effect of recombinant human vascular endothelial growth factor (VEGF)-C on lymphangiogenesis, inflammation, and fibrosis in the mouse kidney using the unilateral ureteral obstruction (UUO); lymphangiogenesis was significantly induced in the UUO+VEGF-C group. In lymphatic endothelial cells, VEGF-C increased the activity and proliferation of such cells and expression of VCAM-1. PMID: 29083411 This study reports that human dendritic cells produce VEGF-C, a cytokine with potent pro-lymphangiogenic activity when stimulated with IFN-gamma PMID: 26987844 Association of coexpressed high levels of VEGF-C and active MMP-9 with lymphatic spreading and local invasiveness of Papillary thyroid carcinoma (PTC) suggests their potential usefulness as predictive biomarkers of aggressive PTC behavior. PMID: 27806941 Data show that VEGF-C, VEGF-D, and VEGFR-3 were expressed in a substantial percentage of breast carcinomas. PMID: 28791841 By treating LECs with VEGF-C156S and analyzing subsequent changes in gene expression, we identified several 'immediate early' transcription factors that showed a rapid transient upregulation VEGFR-3 stimulation. these results reveal an important and unanticipated role of HOXD10 in the regulation of VEGFR-3 signaling in lymphatic endothelial cells, and in the control of lymphangiogenesis and permeability. PMID: 27199372 In colon cancer samples, there was a positive correlation between the expression of integrin alpha4 and VEGF-C. Integrin alpha4 and VEGF-C were significantly associated with the clinicopathological parameters (LMVD, Duke's stage, and lymph node metastasis). patients with high integrin alpha4 or VEGF-C expression had significantly shorter overall survival and tumor-free survival time. PMID: 26917449 High VEGFC expression is associated with angiogenesis and lymphangiogenesis. PMID: 27852824 Adiponectin promoted VEGF-C expression and secretion in human chondrosarcoma cells. PMID: 27252405 Study showed that VEGF-C levels are high in hypervolemic and low in euvolemic (and hypovolemic) chronic kidney disease patients; serum VEGF-C levels were significantly correlated with bioimpedance spectroscopy measurements PMID: 28471955 Taken together, we suggest that ELK3 is an upstream regulator of the NF-kappaB signaling pathway, the inhibition of which leads to the suppression of peritumoral lymphatic vessel development, possibly due to a low VEGFC expression. PMID: 28188790 These results indicate that VEGF-C-induced MSC osteogenesis is mediated through VEGFR2 and VEGFR3, and followed the activation of the ERK/RUNX2 signaling pathway. PMID: 28163024 Overexpression of vascular endothelial growth factor C (VEGF-C) in Kazakh esophageal squamous cell carcinoma (ESCC) was significantly associated with gender, depth of tumor invasion, lymph node metastasis and tumor clinical stage. PMID: 27939650 This paper quantifies the lymphatic microvessel density (LMD) in benign and malignant salivary gland tumors and analyzes the relationship between LMD and tumor expression of vascular endothelial growth factors C (VEGF-C) and the proliferative index. PMID: 27229879 KAI1-induced decreases in VEGFC expression are mediated via Src/STAT3 signaling pathways in pancreatic cancer cells. PMID: 27082851 The results of this study suggest that the more aggressive biological behavior of squamous cell carcinoma of the tongue in young patients may be related to a higher expression of VEGF-C. PMID: 27876236 This study suggests that NRP1 expression and LVD are independent factors that are likely to predict the risk of LN metastasis in squamous cell carcinoma (SCC)of the tongue, whereas the expression of VEGFC, VEGFR3, CCR7, and SEMA3E are nonindependent predictive factors PMID: 27666723 High expression of VEGFC is associated with peritoneal dissemination in gastric cancer. PMID: 26621525 TNF-alpha mediates VEGF-C expression, which plays a critical role in the pathogenesis of pterygia. PMID: 27314284 a potential link between the upregulation of Syk and VEGF-C expression and lung adenocarcinoma. PMID: 27461624 The summarizes the structure and function features of pathway-related molecules of VEGFC/D-VEGFR3/NRP2 axis, stages of various tumors and their molecular mechanisms and significances in tuthe expression changes of these molecules in different anatomic organs or histopathologic types or development lymphatic metastasis. PMID: 27527412 Data show that WNT1-inducible signaling pathway protein-1 (WISP)-1/CCN4 expression was correlated with vascular endothelial growth factor-C (VEGF-C) expression in Oral squamous cell carcinoma (OSCC) specimens. PMID: 26824419 VEGF-C overexpression shows an unfavorable prognosis for EC patients. PMID: 27540974 FIGO stage (P < 0.0001), tumor grade (P < 0.0001), lymph node metastasis (P < 0.0001), serum VEGF-C concentration (P = 0.0001), and ascites VEGF-C concentration (P < 0.0001) were significantly correlated with overall survival in ovarian cancer. PMID: 23473018 Our data suggested that IL-6 mediates the singnal pathway of JAK-STAT3-VEGF-C promoting the growth, invasion and lymphangiogenesis in gastric cancer PMID: 26750536 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 the concurrent high expression of VEGF-C and NRP2 is predictive of the unfavorable prognosis in glioblastoma. PMID: 26753562 a significant decrease in miR101 levels, accompanied with an increased expression of vascular endothelial growth factor (VEGF)C in cisplatinresistant SGC7901 gastric cancer cells. PMID: 26573417 MTA1 is up-regulated in CRC; its expression is inversely associated with lymphatic metastases and the expression of VEGFC, VEGFD and VEGFR3 PMID: 26543080

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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.

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