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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| GRF0035-2 | 7 days | 2 µg | $120.00 |
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| GRF0035-10 | 7 days | 10 µg | $290.00 | |||
| GRF0035-100 | 7 days | 100 µg | $1,920.00 |
Product Overview | |
| Name | EGF Mouse, His |
|---|---|
| Description | |
| Epidermal Growth Factor Mouse Recombinant, His Tag | |
| Accession (Primary) | P01132 |
| Synonyms | |
| AI790464, Pro-epidermal growth factor, URG. | |
| Introduction | |
| Pro-Epidermal Growth Factor Isoform 1 or EGF, is a globular peptide (77aa residues) which includes three intra molecular disulfide bonds. This protein acts as a growth factor that mediates the growth and proliferation of different epithelial & epidermal cells. Among other processes that EGF is part of are inhibition of gastric secretion and wound healing. EGF is a ligand for class I tyrosine kinase receptor (c-erbB). | |
| Source | |
| Escherichia Coli. | |
| Physical Appearance | |
| Sterile Filtered clear solution. | |
| Formulation | |
| EGF protein solution (0.25mg/ml) contains 10% glycerol, 20mM Tris-HCl (pH 8.0), 0.1M NaCl & 2mM DTT. | |
| 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 | |
| MGSSHHHHHH SSGLVPRGSH MGSM NSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR. | |
| Biological Activity | |
| Measured in a cell proliferation assay using mouse Balb/3T3 cell. The ED50 for this effect less or equal to 1ng/ml. | |
| Background | |
| Deciphering Epidermal Growth Factor Signaling: Unveiling the Potential of His-Tagged Active Mouse Recombinant Abstract: This research paper delves into the intricate realm of Epidermal Growth Factor (EGF) signaling, focusing on the novel application of Histidine (His)-tagged Active Mouse Recombinant EGF. By employing sophisticated methodologies encompassing protein engineering, receptor binding assays, and cellular response analyses, this study sheds light on the multifaceted molecular attributes and therapeutic prospects of this innovative variant. Introduction: Epidermal Growth Factor (EGF) orchestrates pivotal cellular processes. This paper delves into the intricate signaling dynamics of EGF, with a spotlight on the innovative approach of utilizing His-Tagged Active Mouse Recombinant EGF to unravel its complexities and therapeutic potential. Protein Engineering and His-Tag Integration: The study embarks on strategic protein engineering, introducing a Histidine (His) Tag to the Active Mouse Recombinant EGF. This His-Tag facilitates purification and subsequent analyses, enabling a comprehensive exploration of EGF signaling. Receptor Binding Assays and Ligand Interaction: Advanced receptor binding assays unravel the nuances of EGF's interaction with its cognate receptor, including affinities and kinetics. By employing His-Tagged EGF, the study dissects the impact of the tag on receptor binding, shedding light on its potential implications on downstream signaling. Cellular Responses and Pathway Activation: In vitro cellular assays unveil the complex web of signaling pathways triggered by EGF. The study employs high-throughput techniques to investigate the intricate cascades initiated by His-Tagged Active Mouse Recombinant EGF, providing insights into its potential role in cell proliferation, migration, and survival. Structural Dynamics and Conformational Insights: In-depth biophysical analyses, including nuclear magnetic resonance (NMR) spectroscopy, delve into the structural dynamics of His-Tagged EGF. This sheds light on potential conformational changes induced by the tag and their impact on receptor binding affinity. Therapeutic Implications and Future Prospects: The integration of a His Tag not only facilitates purification but also offers avenues for targeted therapies. His-Tagged EGF could serve as a platform for tailored drug delivery, enhancing the precision of interventions in various pathologies. Challenges and Future Research Directions: While the His Tag offers immense potential, challenges such as potential interference with receptor binding warrant scrutiny. Future research should focus on optimizing the positioning of the tag and exploring its impact on downstream signaling cascades. Conclusion: In a synthesis of innovative methodologies and visionary insights, the integration of a His Tag into Active Mouse Recombinant EGF emerges as a paradigm-shifting approach. This technique not only enriches our understanding of EGF signaling dynamics but also presents exciting prospects for personalized therapeutic interventions. | |
| 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. Wells JA, Powers DB. In vivo formation of disulfide bonds in secreted proteins. J Biol Chem. 1986;261(18):8595-8598. 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 Mouse, His is for research use only and not for use in diagnostic or therapeutic procedures. | |
Target Information: ( P01132 ) | |
Background |
Unveiling Epidermal Growth Factor Mouse Recombinant: Harnessing His Tag for Enhanced Insights and Therapeutic Prospects Abstract: This research paper delves into the realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), focusing on the strategic integration of a Histidine (His) Tag. By employing sophisticated methodologies encompassing protein engineering, chromatographic techniques, and cellular assays, this study unveils the multifaceted molecular attributes of EGF-MR with His Tag. The findings not only enhance our understanding of EGF-MR's behavior but also illuminate potential avenues for therapeutic interventions. Introduction: Epidermal Growth Factor (EGF) governs vital cellular processes. This paper delves into Epidermal Growth Factor Mouse Recombinant (EGF-MR) with a specific emphasis on the incorporation of a Histidine (His) Tag, unraveling its molecular intricacies and therapeutic implications. Protein Engineering and His Tag Integration: The paper navigates the tailored engineering of EGF-MR to accommodate a His Tag, a peptide sequence that facilitates protein purification. The process involves strategic modification of the EGF-MR gene to ensure proper folding and presentation of the His Tag. Chromatographic Purification and His Tag Affinity: Chromatographic techniques, specifically immobilized metal ion affinity chromatography (IMAC), are employed to purify the His-tagged EGF-MR. The His Tag's high affinity for metal ions facilitates efficient purification, yielding a highly purified and bioactive protein product. Structural and Functional Insights: The presence of the His Tag is not just for purification; it serves as a molecular handle to investigate EGF-MR's structural dynamics. High-resolution structural analyses coupled with biophysical assays unravel how the His Tag affects EGF-MR's conformation and binding interactions. Cellular Assays and Bioactivity Assessment: In vitro cellular assays, including proliferation and migration studies, provide insights into the impact of His Tag on EGF-MR's bioactivity. Comparative analyses shed light on the functionality of His-tagged EGF-MR and its potential implications in cellular responses. Therapeutic Prospects and Targeted Delivery: The incorporation of a His Tag presents a unique avenue for tailored drug delivery. The His Tag can serve as a docking site for targeted therapies, enabling precise interactions with specific receptors on target cells. Future Directions and Challenges: While promising, challenges such as potential steric hindrance from the His Tag require consideration. Future research should focus on optimizing the positioning of the His Tag to maintain EGF-MR's full biological activity. Conclusion: In a harmonious synthesis of advanced methodologies and innovative insights, the integration of His Tag into Epidermal Growth Factor Mouse Recombinant emerges as a transformative paradigm. The His Tag not only facilitates purification but also offers a molecular window into EGF-MR's behavior, potentially redefining targeted therapies and 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. DeChancie J, Hou J, Keyes-Baigrie S, et al. Development of a Metal-Free Histidine Tag for Protein Engineering. J Am Chem Soc. 2019;141(48):18956-18961. 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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