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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| GRF0037-20 | 7 days | 20 µg | $120.00 |
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| GRF0037-100 | 7 days | 100 µg | $290.00 | |||
| GRF0037-1 | 7 days | 1 mg | $1,584.00 |
Product Overview | |
| Name | EGF Rat |
|---|---|
| Description | |
| Epidermal Growth Factor Rat Recombinant | |
| Accession (Primary) | P07522 |
| Synonyms | |
| Urogastrone, URG, EGF. | |
| Introduction | |
| Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. | |
| Source | |
| Adult Male Rat Submandibular Glands. | |
| Physical Appearance | |
| Sterile Filtered White lyophilized (freeze-dried) powder. | |
| Formulation | |
| The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer. | |
| Stability | |
| Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. | |
| Purity | |
| Greater than 99.0% as determined by(a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. | |
| Solubility | |
| It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. | |
| 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. | |
| Precautions | |
| EGF Rat is for research use only and not for use in diagnostic or therapeutic procedures. | |
Target Information: ( P07522 ) | |
Background |
Pioneering Insights into Epidermal Growth Factor Rat Recombinant: Unraveling Signaling Dynamics and Therapeutic Implications Abstract: This research paper delves into the unexplored landscape of Epidermal Growth Factor Rat Recombinant (EGF-RR), delving into its intricate molecular attributes, signaling pathways, and potential therapeutic applications. By employing advanced methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the complex interplay between EGF-RR and cellular responses, offering a new perspective for therapeutic interventions. Introduction: Epidermal Growth Factor (EGF) holds a key role in cellular regulation. This paper navigates the intricacies of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and its potential therapeutic implications. Protein Expression and Purification: The paper delves into the meticulous engineering of EGF-RR, involving gene optimization for enhanced expression. Protein purification strategies, such as affinity chromatography, are employed to obtain highly purified EGF-RR for subsequent analyses. Receptor Binding Assays and Ligand Interaction: Advanced receptor binding assays elucidate the interaction of EGF-RR with its cognate receptor. By quantifying binding affinities and kinetic rates, the study unveils the nuances of EGF-RR's engagement with its receptor, shedding light on potential structural determinants. Cellular Signaling Pathways and Functional Responses: Through in vitro cellular assays, the study unravels the intricate signaling pathways initiated by EGF-RR. Quantitative phosphoproteomic analyses expose the dynamic phosphorylation events triggered by EGF-RR, providing insights into its role in cellular proliferation, migration, and differentiation. Bioinformatics Insights and Molecular Modeling: Utilizing advanced bioinformatics tools, molecular dynamics simulations provide a deeper understanding of EGF-RR's interactions with its receptor and potential downstream effectors. Structural modeling unveils the conformational changes driving signaling cascades. Therapeutic Prospects and Novel Avenues: The molecular insights into EGF-RR's signaling dynamics open avenues for therapeutic exploration. Targeted interventions harnessing EGF-RR's potential in wound healing and tissue regeneration, as well as its role in modulating cancer microenvironments, emerge as promising prospects. Challenges and Future Directions: Despite progress, challenges such as deciphering context-dependent signaling responses remain. Future research should focus on unraveling the intricate cross-talk between different signaling pathways and exploring EGF-RR's role in specific disease contexts. Conclusion: In a convergence of advanced methodologies and visionary insights, Epidermal Growth Factor Rat Recombinant emerges as a captivating subject. Its distinctive molecular attributes and complex cellular interplay offer potential avenues for therapeutic interventions, 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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