Recombinant Human VEGFC
Cat.No. : | VEGFC-157H |
Product Overview : | Recombinant Human vascular endothelial growth factor C was expressed in modifiedhuman 293 cells. |
- Specification
- Gene Information
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Cat. No. : | VEGFC-157H |
Description : | Vascular endothelial growth factor C (VEGF-C), also known as Flt4 ligand (Flt4-L), vascular endothelial growth factor-related protein (VRP) and VEGF-2, is a member of the cysteine-knot growth factor superfamily and exhibits homology with VEGF-121 (32%) and PDGF (27%). However VEGF-C also possesses a 180 amino acid C-terminal cysteine-rich domain absent in other VEGFs. The major secreted form of VEGF-C is a disulfide linked antiparallel homodimeric protein containing 5 potential N-linked glycosylation sites and has a theoretical molecular weight of 44 kDa. VEGF-C is predominantly involved in angiogenesis, vasculogenesis, lymphangiogenesis as well as an inhibitor of dendritic cell maturation. VEGF-C also possesses both mitogenic and chemotactic activity w.r.t. endothelial cells and monocytes. |
Source : | human 293 cells. |
Molecular Mass : | VEGF-C secreted antiparallel homodimer migrates between 45 and 55 kDa due to post-translational modifications, in particular glycosylation. This compares with the unmodified homodimer that has a predicted molecular mass of 43.9 kDa. Individual chains of VEGF-C migrate as a band between 27 and 35 kDa in SDS-PAGE due to post-translational modifications, in particular glycosylation. This compares with the unmodified VEGF-C chains that have a predicted molecular mass of 21.6 and 22.2 kDa. |
PI : | VEGF-C secreted antiparallel homodimer separates into a number of isoforms with a pI between 5.6 and 8.4 in 2D PAGE due to post-translational modifications, in particular glycosylation. This compares with the unmodified VEGF-C homodimer that has a predicted pI of 7.8. |
% Carbohydrate : | VEGF-C consists of 15-40% from 1D gel of individual chains carbohydrate by weight. |
Glycosylation : | VEGF-C contains N- and probably O-linked oligosaccharides. |
Purity : | >95%, as determined by SDS-PAGE and visualized by silver stain. |
Formulation : | When reconstituted in 0.5 ml sterile phosphate-buffered saline, the solution will contain 1% human serum albumin (HSA) and 10% trehalose. |
Reconstitution : | It is recommended that 0.5 ml of sterile phosphate-buffered saline be added to the vial. |
Storage : | Lyophilized products should be stored at 2 to 8°C. Following reconstitution short-term storage at 4°C is recommended, and longer-term storage of aliquots at -18 to -20°C. |
Gene Name : | VEGFC vascular endothelial growth factor C [ Homo sapiens ] |
Synonyms : | vascular endothelial growth factor C; VRP; Flt4-L; VEGFC; FLT4 ligand DHM; vascular endothelial growth factor-related protein; VEGF-C; Flt4 ligand; Vascular endothelial growth factor-related protein |
Gene ID : | 7424 |
mRNA Refseq : | NM_005429 |
Protein Refseq : | NP_005420 |
MIM : | 601528 |
UniProt ID : | P49767 |
Chromosome Location : | 4q34.3 |
Pathway : | Bladder cancer; Cytokine-cytokine receptor interaction; Focal adhesion; Pancreatic cancer; Pathways in cancer; Renal cell carcinoma; mTOR signaling pathway; Hemostasis; Signaling by VEGF |
Function : | growth factor activity; vascular endothelial growth factor receptor 3 binding |
Products Types
◆ Recombinant Protein | ||
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VEGFC-4966R | Recombinant Rhesus Macaque VEGFC Protein, His (Fc)-Avi-tagged | +Inquiry |
VEGFC-10009M | Recombinant Mouse VEGFC Protein, His (Fc)-Avi-tagged | +Inquiry |
VEGFC-825M | Recombinant Mouse VEGFC Protein (Ala108-Arg223), His-tagged | +Inquiry |
VEGFC-565H | Recombinant Human VEGFC Protein | +Inquiry |
◆ Lysates | ||
VEGFC-2768HCL | Recombinant Human VEGFC cell lysate | +Inquiry |
VEGFC-1306RCL | Recombinant Rat VEGFC cell lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (7)
Ask a questionVEGFC primarily signals through its interactions with VEGFR-2 (Vascular Endothelial Growth Factor Receptor 2) and VEGFR-3. Upon binding to one of these receptors, VEGFC triggers receptor dimerization, leading to the activation of intracellular signaling pathways. This activation involves phosphorylation events and subsequent recruitment of downstream effectors, which ultimately regulate cellular responses such as proliferation, migration, and angiogenesis. The intricate signaling mechanisms underlying VEGFC-receptor interactions contribute to its functional versatility and provide potential targets for therapeutic interventions.
VEGFC protein is derived from the conversion of proVEGFC precursor protein and comprises approximately 354 amino acid residues. Structurally, it consists of a signal sequence, an N-terminal domain, and a C-terminal VEGF homology domain. The signal sequence is involved in cellular localization and secretion processes, while the VEGF homology domain interacts with target receptors, mediating cellular proliferation and angiogenesis. Understanding the specific structural features is crucial for elucidating the functional properties and molecular interactions associated with VEGFC.
VEGFC's involvement in pathological conditions, including cancer, is extensively studied. The upregulation of VEGFC expression in tumor cells promotes angiogenesis and lymphangiogenesis within the tumor microenvironment. This enhanced blood and lymphatic vessel formation facilitates tumor growth, invasion, and metastasis. Moreover, VEGFC can induce lymphangiogenesis in sentinel lymph nodes, aiding cancer cell dissemination. Targeting VEGFC signaling pathways has emerged as a potential therapeutic strategy to inhibit tumor angiogenesis and lymphangiogenesis, highlighting the clinical significance of understanding the complex interplay between VEGFC and cancer progression.
Several therapeutic interventions targeting VEGFC and its downstream signaling pathways are under investigation. Anti-VEGFC monoclonal antibodies, VEGFR inhibitors, and small molecule inhibitors of VEGFC-mediated signaling have shown promise in preclinical and clinical studies. These interventions aim to disrupt the angiogenic and lymphangiogenic processes driven by VEGFC, thereby inhibiting tumor growth, metastasis, and other pathological conditions associated with VEGFC dysregulation. Additionally, exploring combinational approaches with existing therapies, such as chemotherapy and immunotherapy, holds potential for synergistic effects and improved treatment outcomes. Continued research efforts are focused on optimizing these interventions for clinical application and expanding the therapeutic repertoire for VEGFC-associated diseases.
Multiple regulatory mechanisms control VEGFC expression levels. Transcriptional regulation plays a significant role, with various transcription factors binding to the VEGFC promoter region to activate or suppress its transcription. Additionally, post-transcriptional regulation through microRNAs and RNA-binding proteins can modulate VEGFC mRNA stability and translation efficiency. Furthermore, environmental factors, such as hypoxia and inflammation, influence VEGFC expression by activating specific signaling pathways. Understanding the precise regulatory mechanisms is crucial for deciphering the intricate balance required for maintaining proper VEGFC levels and ensuring its functional integrity.
Dysregulation of VEGFC has been associated with various pathological conditions. Excessive VEGFC expression has been implicated in tumor angiogenesis, promoting the growth and spread of cancer cells by stimulating the formation of blood and lymphatic vessels in the tumor microenvironment. On the other hand, decreased or insufficient VEGFC levels have been linked to lymphatic disorders, such as lymphedema, where impaired lymphatic vessel development results in fluid buildup and tissue swelling. Additionally, alterations in VEGFC signaling have been observed in ocular diseases, inflammatory disorders, and cardiovascular diseases. Understanding the dysregulation of VEGFC in these contexts may pave the way for potential therapeutic strategies targeting this protein.
VEGFC (Vascular Endothelial Growth Factor C) has diverse cellular functions. Primarily, it serves as a potent angiogenic factor, participating in neovascularization and lymphangiogenesis processes. VEGFC also regulates endothelial cell proliferation and migration, playing a crucial role in lymphatic dissemination and metastasis. Additionally, VEGFC is implicated in neurodevelopment, mammary gland morphogenesis, tissue regeneration, and other physiological processes. Its multifaceted functions highlight its significance in various biological contexts, emphasizing the need for further investigation to unravel its precise mechanisms and implications.
Customer Reviews (3)
Write a reviewEmbodied with the glorious power of scientific progress, the innovation behind this reagent inspires truly remarkable experimental encounters.
By requiring minimal usage, this protein reagent significantly reduces consumable costs, making it an ideal choice for large-scale experiments.
The manufacturer's proactive approach in offering valuable insights and suggestions has greatly improved the outcome of my experiments.
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