- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
CYT-217
Synonyms
Introduction
Description
Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.
Source
Physical Appearance
Formulation
EGF was lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.
Solubility
Stability
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 98.0% as determined by SDS-PAGE.
Amino acid sequence
Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.
References
1.Title:Activation of the Hedgehog pathway in pilocytic astrocytomas.
Publication:Neuro Oncol (2010) 12 (8): 790-798. doi: 10.1093/neuonc/noq026 First published online: March 11, 2010
Link:EGF prospec publication
2.Title:Evaluation of bioactivity and effect of polymeric stabilizers during heat treatment for the unfolded fraction of human epidermal growth factor.
Publication:SEN'I GAKKAISHI vol.67,nov.8(2011)
Link:EGF Human prospec publication
3.Title:GPR56 is essential for testis development and male fertility in mice.
Publication:Article first published online: 27 OCT 2010 DOI: 10.1002/dvdy.22468
Link:Epidermal Growth Factor prospec publication
4.Title:Changing the Receptor Specificity of Anthrax Toxin.
Publication:doi: 10.1128/?mBio.00088-12 1 May 2012 mBio vol. 3 no. 3 e00088-12
Link:Epidermal Growth Factor Human prospec publication
5.Title:Characterization of Non-Specific Cytotoxic Cell Receptor Protein 1: A New Member of the Lectin-Type Subfamily of F-Box Proteins.
Publication:Kallio H, Tolvanen M, J?nis J, Pan P-w, Laurila E, et al. (2011) Characterization of Non-Specific Cytotoxic Cell Receptor Protein 1: A New Member of the Lectin-Type Subfamily of F-Box Proteins. PLoS ONE 6(11): e27152. doi:10.1371/journal.pone.0027152
Link:EGF Protein prospec publication
Publication: Blood 116.5 (2010): 759-766.
Link: Epidermal Growth Factor Protein prospec publication
Safety Data Sheet
Usage
Background
Unveiling the Therapeutic Potential of Epidermal Growth Factor Human Recombinant: A Comprehensive Analysis
Abstract:
This research paper delves into the intricate realm of Epidermal Growth Factor (EGF) Human Recombinant, deciphering its multifaceted molecular attributes, signaling mechanisms, and emerging therapeutic prospects. Employing a combination of state-of-the-art methodologies, encompassing structural elucidation, cellular assays, and preclinical models, this study provides a nuanced understanding of the diverse cellular responses orchestrated by EGF. The findings underscore its promise as a therapeutic agent across various medical domains.
Introduction:
Epidermal Growth Factor (EGF) emerges as a pivotal cytokine governing essential cellular functions. This paper explores the distinct facets of EGF Human Recombinant, focusing on its molecular intricacies and therapeutic implications.
Molecular Insights and Cellular Signaling:
At the heart of its functionality lies the interaction between EGF and its cognate receptor. High-resolution structural analyses unravel the intricate binding interfaces, setting the stage for downstream signaling cascades. The canonical mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K)/Akt pathways emerge as pivotal mediators of cellular responses, encompassing cell proliferation, survival, and motility.
Experimental Approaches and Cellular Responses:
To dissect the cellular ramifications of EGF, a spectrum of in vitro assays has been harnessed. These encompass proliferation assays, wound healing studies, and advanced live-cell imaging techniques. Through these, the dynamic orchestration of EGF-induced responses is unveiled, elucidating its role in fostering cellular migration, division, and tissue repair.
Preclinical Insights and Therapeutic Prospects:
Translating these in vitro insights to tangible clinical benefits, preclinical investigations offer compelling narratives. In animal models, EGF emerges as a pivotal factor in cutaneous wound healing, accelerating tissue regeneration. Additionally, its potential extends to oncology, where it modulates tumor microenvironments and exhibits anti-apoptotic effects, thus offering novel avenues for targeted cancer interventions.
Challenges and Future Horizons:
Despite these promising strides, challenges persist. The intricate cross-talk between signaling pathways necessitates meticulous examination to decipher potential synergies or conflicts. Moreover, optimizing delivery methods and dosing regimens for clinical translation remains imperative.
Conclusion:
In a synthesis of intricate molecular insights and transformative therapeutic potential, Epidermal Growth Factor Human Recombinant emerges as a remarkable entity. Its pivotal role in cellular orchestration underscores its promise as a therapeutic intervention. As research evolves, harnessing the therapeutic benefits of EGF holds the key to innovative medical 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.
- Oda K, Matsuoka Y, Funahashi A, Kitano H. A comprehensive pathway map of epidermal growth factor receptor signaling. Mol Syst Biol. 2005;1(1):2005.0010.
- Schneider MR. Epidermal Growth Factor: Unraveling the Implications for Cancer Progression. Mol Cancer Res. 2017;15(6):751-756.
- Sen CK, Gordillo GM, Roy S, et al. Human skin wounds: a major and snowballing threat to public health and the economy. Wound Repair Regen. 2009;17(6):763-771.