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Recombinant Rat Vascular Endothelial Growth Factor C, His-tagged

Cat.No. : Vegfc-5345R
Product Overview : Recombinantrat Vegfc contains129 amino acids and is fused to a His-tag (6x His) at theC-terminal end. As a result of glycosylation, Vegfc migratesas an 18-24 kDa protein in SDS-PAGE under reducingconditions.
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  • Gene Information
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Cat. No. : Vegfc-5345R
Description : Theprotein encoded by this gene is a member of the platelet-derived growthfactor/vascular endothelial growth factor family, is active in angiogenesis, lymphangiogenesisand endothelial cell growth and survival, and can also affect thepermeability of blood vessels. This secreted protein undergoes a complexproteolytic maturation, generating multiple processed forms that bind andactivate VEGFR-3 receptors. Only the fully processed form can bind andactivate VEGFR-2 receptors. The structure and function of this protein issimilar to those of vascular endothelial growth factor D.
Source : Insect cells
Species : Human
Molecular Weight : 18-24 kDa
Endotoxin Level : < 0.1 ng/μgof the protein.
Form : Lyophilized from asterile filtered solution containing BSA.
Purity : > 90% bySDS-PAGE and visualized by silver stain.
Biological Activity : Measuredby its ability to stimulate phosphorylation of the VEGFR-3/FLT-4 receptor in pigaortic endothelial cells. The ED50 for this effect is typically 200-300ng/ml.
Reconstitution : Centrifugevial prior to opening. The lyophilized Vegfc issoluble in water and most aqueous buffers. The lyophilized Vegfc shouldbe reconstituted in PBS or medium to a concentrationnot lower than 50 μg/ml.
Storage : Lyophilizedsamples are stable for greater than six months at -20°C to -80°C. ReconstitutedVegfc shouldbe stored in working aliquots at -20°C. Avoid repeated freeze-thawcycles.
OfficialSymbol : Vegfc
Gene Name : Vegfc vascular endothelialgrowth factor C [ Rattus norvegicus ]
Synonyms : Vegfc; vascularendothelial growth factor C; vascular endothelial growth factor C; VRP;VEGF-C; flt4-L; flt4 ligand; vascular endothelial growth factor-relatedprotein
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; Hemostasis;Pancreatic cancer; Pathways in cancer; Platelet activation; Plateletdegranulation; Renal cell carcinoma; Response to elevated platelet cytosolicCa2+; Signal Transduction; Signaling by VEGF; VEGF binds to VEGFR leading toreceptor dimerization; VEGF ligand-receptor interactions; VEGFR-3 signaling;mTOR signaling pathway
Function : chemoattractantactivity; growth factor activity; vascular endothelial growth factor receptor3 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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Q&As (7)

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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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Reviews
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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