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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| GRF0029-100 | 7 days | 100 µg | $120.00 |
Select product before adding to cart
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| GRF0029-500 | 7 days | 500 µg | $290.00 | |||
| GRF0029-1 | 7 days | 1 mg | $360.00 |
Product Overview | |
| Name | EGF Human |
|---|---|
| Description | |
| Epidermal Growth Factor Human Recombinant | |
| Accession (Primary) | P01133 |
| 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 | |
| Pichia Pastoris. | |
| Physical Appearance | |
| Sterile Filtered White lyophilized (freeze-dried) powder. | |
| Formulation | |
| Lyophilized from a filtered concentrated solution in PBS, pH 7.4. | |
| 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 98.0% as determined by(a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. | |
| Amino acid sequence | |
| NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E. | |
| Biological Activity | |
| The ED₅₀, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3 H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 10 7 Units/mg. | |
| 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 | |
| Harnessing Pichia for Epidermal Growth Factor Human Recombinant Production: Novel Approaches and Therapeutic Implications Abstract: This research paper delves into a cutting-edge avenue of Epidermal Growth Factor (EGF) Human Recombinant production by leveraging Pichia as an expression host. Through a synthesis of advanced methodologies encompassing genetic engineering, fermentation, and bioinformatics, this study explores the potential of Pichia-based platforms for enhanced EGF yield and biological activity. The findings not only offer insights into efficient EGF production but also underscore the therapeutic prospects of this approach. Introduction: Epidermal Growth Factor (EGF) holds a crucial place in cellular processes. This paper explores a novel dimension of EGF Human Recombinant production utilizing Pichia expression systems, emphasizing both technical aspects and the potential impact on therapeutic applications. Pichia as an Expression Host: Pichia stands as a promising alternative to conventional expression platforms due to its robustness and eukaryotic machinery. This paper investigates the strategic integration of EGF gene into Pichia, utilizing tailored vectors and promoters for optimal protein production. Genetic Engineering Strategies: Precise genetic manipulation is pivotal for enhanced EGF yield. Gene codon optimization and signal peptide selection are meticulously undertaken to ensure proper protein folding and secretion in Pichia. Through these approaches, EGF expression and secretion are finely tuned, resulting in biologically active EGF. Fermentation and Protein Purification: Expression is followed by fermentation in controlled conditions, leading to EGF accumulation. This step is supplemented by purification processes like chromatography, ensuring high EGF purity. Biochemical assays validate the biological activity of the purified EGF, affirming its therapeutic potential. Bioinformatics in EGF-Pichia Interaction: Advanced bioinformatics analyses shed light on the intricate interactions between EGF and Pichia host. Structural modeling and molecular dynamics simulations provide insights into potential post-translational modifications and protein-protein interactions, enriching our understanding of EGF behavior in Pichia. Therapeutic Implications: Beyond production, the paper emphasizes the therapeutic significance of EGF produced in Pichia. Enhanced production efficiency directly impacts cost-effectiveness, broadening its accessibility for therapeutic use. The EGF-Pichia approach presents exciting avenues for wound healing therapies and targeted cancer interventions. Challenges and Future Directions: Despite the progress, challenges such as glycosylation patterns and scaling-up strategies remain. Future efforts should focus on refining glycosylation profiles to ensure consistent bioactivity and optimizing bioreactor designs to scale up production for clinical applications. Conclusion: In a synergy of advanced methodologies and therapeutic implications, the Pichia-based Epidermal Growth Factor Human Recombinant production presents an innovative paradigm. The intricate harmony between Pichia host and EGF production holds promise for novel therapies, underscoring the potential impact of this pioneering approach. | |
| References | |
| Bibliography: Cereghino JL, Cregg JM. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol Rev. 2000;24(1):45-66. Hohenblum H, Gasser B, Maurer M, Borth N, Mattanovich D. Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris. Biotechnol Bioeng. 2004;85(4):367-375. Ahmad B, Gromiha MM, Sarai A. Analysis and prediction of DNA-binding proteins and their binding residues based on composition, sequence and structural information. Bioinformatics. 2004;20(4):477-486. Sen CK, Roy S. Redox signals in wound healing. Biochim Biophys Acta. 2008;1780(11):1348-1361. 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 Human is for research use only and not for use in diagnostic or therapeutic procedures. | |
Target Information: ( P01133 ) | |
Background |
About EGF: In the sphere of biomedical studies, epidermal boom factor (EGF) is a cornerstone that gives precious insights into the mechanisms underlying tissue healing, differentiation, and mobile proliferation. In this article we will explore the characteristics and uses of epidermal growth factor (EGF). Description: Epidermal growth factor (EGF) is a 6-kDa protein consisting of 53 amino acid residues and 3 intramolecular disulfide linkages. Human tissues, such as platelets, the parotid gland, and the submandibular gland, are rich in EGF. EGF, which was first discovered in human urine and the submaxillary glands of mice, functions as a major modulator of cell proliferation by attaching to its receptor, EGFR, which is found on the cell membrane. EGF triggers autophosphorylation of transmembrane protein tyrosine kinase EGFR upon binding, hence initiating downstream signaling cascades through pathways such as phosphatidylinositol and ras. Beyond the cell membrane, EGF has a variety of roles as it also initiates cytoplasmic processes such actin depolymerization and membrane ruffle formation. Studies indicate that EGF and its receptor might possibly be important components of the nucleus, highlighting the complexity of EGF-mediated cellular responses. Function: By attaching to the epidermal growth factor receptor (EGFR), EGF promotes the survival, differentiation, and multiplication of cells. This connection is essential for boosting many physiological processes and stimulating cell proliferation. The preservation of oro-esophageal and stomach tissue integrity is greatly supported by salivary EGF, which is regulated by dietary inorganic iodine. Its actions include the healing of gastric and oral ulcers, the inhibition of gastric acid secretion, the stimulation of DNA synthesis, and the protection of mucosal surfaces against harmful substances such as bile acids, gastric acid, and bacteria. Salivary EGF's role extends to repairing gastric tissue and addressing oro-esophagal issues, showcasing its healing ability in resolving oral and gastrointestinal ailments, including ulcers. Mechanism: EGF functions by forming a strong bond with the cell surface's epidermal growth factor receptor (EGFR), which triggers ligand- induced dimerization. This incident sets off the intrinsic protein-tyrosine kinase activity of EGFR, which in turn initiates a signal transduction cascade inside the cell. Numerous biochemical changes are brought about by this cascade, such as increased intracellular calcium levels, increased glycolysis and protein synthesis, and increased expression of particular genes, most notably the EGFR gene. These carefully planned alterations eventually promote DNA synthesis and cell division, illuminating the complex process by which EGF directs basic biological functions and modulates cellular responses. |
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 6. Title: Cancer-Associated Carbonic Anhydrases IX and XII: Effect of Growth Factors on Gene Expression in Human Cancer Cell Lines. Publication: Journal of Cancer Molecules 5(3): 73-78, 2010. Link: http://mupnet.com/JOCM%205(3)%2073-78.pdf 7. Title: EGR-1 activation by EGF inhibits MMP-9 expression and lymphoma growth Publication: Blood 116.5 (2010): 759-766. Link: Epidermal Growth Factor Protein prospec publication |
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