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Recombinant Rat Vascular Endothelial Growth Factor C, His-tagged

Cat.No. : Vegfc-46R
Product Overview : Recombinant Rat Vascular Endothelial Growth Factor –C 152 contains 152 amino acids residues and was fused to a His-tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 18-24kDa protein in SDS-PAGE under reducing conditions.
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Cat. No. : Vegfc-46R
Description : VEGF-C152S is a point mutant generated by the replacement of the second conserved Cys residue of the recombinant processed VEGF-C by a Ser residue. VEGF-C 152S is analog to the human VEGF-C 156S mutant and only active toward VEGFR-3/FLT-4 but, unlike wild type VEGF-C, is unable to bind to and to activate signaling through VEGFR-2/KDR. VEGF-C152S was inactive in the vascular permeability assay and did not increase migration of the capillary endothelial cells, indicating that these VEGF-like effects of VEGF-C require VEGFR-2 binding. VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. The rat VEGF-C cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant rat VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT -4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant rat VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.
Source : Sf9, Insect Cells
Physical Appearance : Sterile Filtered White lyophilized (freeze-dried) powder.
Purity : Greater than 90.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Formulation : The protein was lyophilized from a concentrated (1mg/ml) solution with BSA.
Solubility : It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor C 152 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Biological Activity : Measured by its ability to stimulate phosphorylation of the VEGFR-3/FLT-4 receptor in porcine aortic endothelial cells (PAE/FLT -4 cells). The ED50for this effect is typically 150-300ng/ml, corresponding to a specific activity of 5 x 103 Units/mg.
Storage : Lyophilized Vascular Endothelial Growth Factor-C152 although stable at room temperature for 3 weeks, should be stored desiccated below -18℃. Upon reconstitution VEGF-C 152 should be stored at 4℃ between 2-7 days and for future use below -18℃. Please prevent freeze-thaw cycles.
Gene Name : Vegfc vascular endothelial growth factor C [ Rattus norvegicus ]
Synonyms : VEGF-C; Vascular endothelial growth factor C; Flt4 ligand; FLT4 ligand DHM; AW228853; Flt4-L; VRP; AW228853; Vegfc; vascular endothelial growth factor C
Gene ID : 114111
mRNA Refseq : NM_053653
Protein Refseq : NP_446105
UniProt ID : O35757
Chromosome Location : 16p11
Pathway : Bladder cancer; Cytokine-cytokine receptor interaction; Focal adhesion; Pancreatic cancer; Pathways in cancer; Renal cell carcinoma; mTOR signaling pathway
Function : growth factor activity; vascular endothelial growth factor receptor 3 binding

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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What signaling mechanisms are involved in VEGFC and its receptor interactions? 05/21/2022

VEGFC 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.

What is known about the structural characteristics of VEGFC and its precursor? 03/29/2022

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.

How does VEGFC contribute to pathological conditions, particularly in cancer? 12/06/2021

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.

What are the current therapeutic interventions targeting VEGFC and its downstream signaling pathways? 04/22/2021

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.

Are there any known regulatory mechanisms that modulate VEGFC expression levels? 08/20/2020

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.

What are the clinical implications of VEGFC dysregulation? 05/08/2020

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.

What are the cellular functions of VEGFC and its involvement in physiological processes? 05/30/2017

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)

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02/12/2021

    Embodied with the glorious power of scientific progress, the innovation behind this reagent inspires truly remarkable experimental encounters.

    02/21/2018

      By requiring minimal usage, this protein reagent significantly reduces consumable costs, making it an ideal choice for large-scale experiments.

      03/26/2016

        The manufacturer's proactive approach in offering valuable insights and suggestions has greatly improved the outcome of my experiments.

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