Recombinant Rat VEGFC cell lysate
Cat.No. : | VEGFC-1306RCL |
Product Overview : | Rat VEGFC / VEGF-C (aa 108-223) derived in Human Cells. The whole cell lysate is provided in 1X Sample Buffer.Browse all transfected cell lysate positive controls |
- Specification
- Gene Information
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Source : | Human cells |
Species : | Rat |
Preparation method : | Transfected cells were cultured for 48hrs before collection. The cells were lysed in modified RIPA buffer with cocktail of protease inhibitors. Cell debris was removed by centrifugation and then centrifuged to clarify the lysate. The cell lysate was boiled for 5 minutes in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 5% b-mercaptoethanol, and lyophilized. |
Lysis buffer : | Modified RIPA Lysis Buffer: 50 mM Tris-HCl pH 7.4, 150 mM NaCl, 1mM EDTA, 1% Triton X-100, 0.1% SDS, 1% Sodium deoxycholate, 1mM PMSF |
Quality control Testing : | 12.5% SDS-PAGE Stained with Coomassie Blue |
Recommended Usage : | 1. Centrifuge the tube for a few seconds and ensure the pellet at the bottom of the tube.2. Re-dissolve the pellet using 200μL pure water and boiled for 2-5 min.3. Store it at -80°C. Recommend to aliquot the cell lysate into smaller quantities for optimal storage. Avoid repeated freeze-thaw cycles.Notes:The lysate is ready to load on SDS-PAGE for Western blot application. If dissociating conditions are required, add reducing agent prior to heating. |
Stability : | Samples are stable for up to twelve months from date of receipt at -80°C |
Storage Buffer : | 50 mM Tris-HCl pH 7.4, 150 mM NaCl, 1mM EDTA, 1% Triton X-100, 0.1% SDS, 1% Sodium deoxycholate, 1mM PMSF |
Storage Instruction : | Lysate samples are stable for 12 months from date of receipt when stored at -80°C. Avoid repeated freeze-thaw cycles. Prior to SDS-PAGE fractionation, boil the lysate for 5 minutes. |
Gene Name : | Vegfc vascular endothelial growth factor C [ Rattus norvegicus ] |
Official Symbol : | VEGFC |
Synonyms : | VEGFC; vascular endothelial growth factor C; VRP; VEGF-C; flt4-L; flt4 ligand; vascular endothelial growth factor-related protein; |
Gene ID : | 114111 |
mRNA Refseq : | NM_053653 |
Protein Refseq : | NP_446105 |
Pathway : | Bladder cancer, organism-specific biosystem; Bladder cancer, conserved biosystem; Cytokine-cytokine receptor interaction, organism-specific biosystem; Cytokine-cytokine receptor interaction, conserved biosystem; Focal adhesion, organism-specific biosystem; Focal adhesion, conserved biosystem; Hemostasis, organism-specific biosystem; |
Function : | chemoattractant activity; growth factor activity; vascular endothelial growth factor receptor 3 binding; vascular endothelial growth factor receptor 3 binding; |
Products Types
◆ Recombinant Protein | ||
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VEGFC-4506H | Recombinant Human VEGFC Protein, His (Fc)-Avi-tagged | +Inquiry |
VEGFC-5839H | Recombinant Human VEGFC Protein(112-227aa), GST-tagged | +Inquiry |
VEGFC-108H | Active Recombinant Human VEGFC Protein | +Inquiry |
VEGFC-1148M | Recombinant Mouse/Rat VEGFC protein(Ala108-Arg223), His-tagged | +Inquiry |
◆ Lysates | ||
VEGFC-2768HCL | Recombinant Human 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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