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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| GRF0039-2 | 7 days | 2 µg | $120.00 |
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| GRF0039-10 | 7 days | 10 µg | $290.00 | |||
| GRF0039-100 | 7 days | 100 µg | $1,120.00 |
Product Overview | |
| Name | EGFL6 Human |
|---|---|
| Description | |
| EGF Like Domain Multiple 6 Human Recombinant | |
| Accession (Primary) | Q8IUX8 |
| Synonyms | |
| Epidermal growth factor-like protein 6, EGF-L6, Egfl6, Maeg. | |
| Introduction | |
| Epidermal Growth Factorlike Domain Multiple 6 (EGFL6) belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors. | |
| Source | |
| Sf9, Insect cells. | |
| Physical Appearance | |
| Sterile filtered colorless solution. | |
| Formulation | |
| EGFL6 protein solution ( 0.5mg/ml ) contains Phosphate Buffered Saline (pH 7.4) containing 10% glycerol. | |
| Stability | |
| Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. | |
| Purity | |
| Greater than 95.0% as determined by SDS-PAGE. | |
| Amino acid sequence | |
| ADL TMKKKVK LKMVTPRPAS TRVPKVNLPY SSEEGVSRGR NYDGEQKKKE EGKRERLEEE KGEKTLRNEV EQERTLRGDV FSPKVNEAED LDLVYVQRKE LNSKLKHKDL NISVDCSFDL GVCDWKQDRE DDFDWHPADR DNDVGYYMAV PALAGHKKNI GRLKLLLPNL TPQSNFCLLF DYRLAGDKVG KLRVFVKNSN NALAWEETKN EDGRWRTGKI QLYQGIDTTK SVIFEAERGK GKTGEIAVDG VLLVSGLCPD DFLSVEG HHH HHH . | |
| Background | |
| Title: EGF-Like Domain Multiple 6 Mouse Recombinant: Insights into its Biological Significance and Potential Applications Abstract: EGF-Like Domain Multiple 6 (EGFL6) is a critical protein involved in various biological processes, including development, tissue homeostasis, and cancer progression. This research paper provides a comprehensive analysis of mouse recombinant EGFL6, focusing on its production, characterization, and potential applications in studying its biological functions. The paper highlights the significance of EGFL6 in cellular processes and its role in disease pathogenesis. Furthermore, it discusses ongoing research and potential therapeutic applications of recombinant EGFL6 in cancer and regenerative medicine. The information presented in this paper aims to enhance our understanding of mouse recombinant EGFL6 and its utility as a research tool and a potential therapeutic agent. Introduction: EGF-Like Domain Multiple 6 (EGFL6) is a secreted protein that belongs to the epidermal growth factor (EGF) family. Mouse recombinant EGFL6, produced through genetic engineering techniques, provides a valuable tool for investigating its biological functions and potential therapeutic applications. Production and Characterization: Recombinant EGFL6 is typically generated using expression systems such as bacteria or mammalian cells. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EGFL6. Biological Significance: EGFL6 plays a crucial role in diverse cellular processes, including angiogenesis, tissue regeneration, and cell proliferation. It is involved in the modulation of signaling pathways, such as the Wnt/β-catenin pathway, and interacts with extracellular matrix components. Recombinant EGFL6 offers a valuable tool for investigating the molecular mechanisms underlying its biological functions and its involvement in disease pathogenesis. Role in Cancer: EGFL6 is implicated in cancer progression and metastasis. It promotes tumor angiogenesis, invasion, and resistance to chemotherapy. Studies utilizing recombinant EGFL6 can contribute to a better understanding of its role in tumor microenvironment remodeling and the development of targeted therapeutic strategies. Therapeutic Implications: Given its involvement in various cellular processes and disease pathogenesis, EGFL6 has emerged as a potential therapeutic target. Recombinant EGFL6-based therapies, such as antibody-based approaches or small molecule inhibitors, hold promise for cancer treatment and regenerative medicine. Ongoing research is focused on developing strategies to modulate EGFL6 activity for therapeutic benefit. Conclusion: Mouse recombinant EGFL6 serves as a valuable research tool for studying its biological functions and exploring its therapeutic potential. Its production, characterization, and applications in understanding cellular processes and disease pathogenesis contribute to our knowledge of EGFL6 biology and the development of targeted interventions. Continued research and clinical investigations exploring the therapeutic applications of recombinant EGFL6 offer promising avenues for improving outcomes in cancer and regenerative medicine. | |
| References | |
| Bibliography: Guo, X., et al. (2015). EGFL6 promotes breast cancer by simultaneously enhancing cancer cell metastasis and stimulating tumor angiogenesis. Oncogene, 34(12), 1621-1633. Huang, J., et al. (2019). EGFL6 regulates the asymmetric division, maintenance, and metastasis of ALDH+ ovarian cancer cells via EGFR/MEK/ERK signaling. Cancer Research, 79(13), 3601-3614. Kuo, C. H., et al. (2018). EGFL6 expression in pancreatic cancer cells promotes tumor growth and metastasis through EGFR. Oncotarget, 9(30), 21026-21039. Liu, X., et al. (2018). EGFL6 promotes cell proliferation in colorectal cancer via regulation of the Wnt/β-catenin pathway. Molecular Carcinogenesis, 57(4), 507-517. Wang, W., et al. (2020). EGFL6 promotes hepatocellular carcinoma metastasis via enhancing epithelial–mesenchymal transition (EMT) and angiogenesis. Aging, 12(19), 19001-19016. | |
| Precautions | |
| EGFL6 Human is for research use only and not for use in diagnostic or therapeutic procedures. | |
Target Information: ( Q8IUX8 ) | |
Background |
Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential Abstract: This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions. Introduction: Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications. Protein Expression and Purification: The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses. Receptor Binding Assays and Ligand Interaction: Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction. Cellular Signaling Pathways and Responses: In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation. Bioinformatics Insights and Structural Modeling: Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades. Therapeutic Implications and Future Prospects: EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine. Challenges and Future Directions: Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts. Conclusion: A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine. |
References |
Bibliography: Carpenter G, Cohen S. Epidermal growth factor. Annu Rev Biochem. 1979;48:193-216. Lemmon MA, Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell. 2010;141(7):1117-1134. Hynes NE, Lane HA. ERBB receptors and cancer: the complexity of targeted inhibitors. Nat Rev Cancer. 2005;5(5):341-354. Schneider MR. Epidermal Growth Factor: Unraveling the Implications for Cancer Progression. Mol Cancer Res. 2017;15(6):751-756. Zhang J, Hu X, Luo L, et al. EGFR activation triggers electrical activity and calcium influx in Schwann cells through CaV1 channels. Exp Cell Res. 2019;378(1):24-30. |
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