The EGF Long is purified by proprietary chromatographic techniques.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Amino acid sequence
Safety Data Sheet
Expanding Therapeutic Frontiers: Epidermal Growth Factor Long Human Recombinant Production using Pichia Expression System
This research paper delves into an innovative realm of Epidermal Growth Factor Long Human Recombinant (EGF-L) production, employing Pichia as an expression host. By amalgamating sophisticated methodologies involving genetic engineering, fermentation optimization, and bioinformatics analyses, this study elucidates the potential of Pichia-based platforms for augmenting EGF-L yield and functionality. The implications of this approach span therapeutic applications and hold the promise of revolutionizing medical interventions.
Epidermal Growth Factor Long (EGF-L) emerges as a pivotal regulator in cellular processes. This paper navigates the uncharted territory of EGF-L Human Recombinant production, harnessing the prowess of Pichia expression systems, and accentuating both technological intricacies and therapeutic implications.
Pichia as an Expression Host:
Pichia emerges as an ideal candidate due to its eukaryotic machinery, ensuring proper folding and post-translational modifications. This paper delves into the strategic integration of EGF-L gene into Pichia, employing tailored promoters and vectors for optimal protein synthesis.
Precision Genetic Engineering:
The success of this endeavor hinges on precision genetic manipulation. Through gene codon optimization and signal peptide selection, the study ensures efficient translation and secretion of EGF-L in Pichia. The resultant production not only maximizes yield but also maintains biological activity.
Fermentation and Purification Strategy:
Post expression, the study elucidates the intricacies of fermentation optimization, a critical step in EGF-L accumulation. This is coupled with meticulous purification techniques, encompassing chromatography, that guarantee EGF-L purity. The biologically active nature of purified EGF-L is verified through intricate bioassays.
Bioinformatics Unveiling EGF-L Pichia Interaction:
Bioinformatics strides enrich the narrative by illuminating the intricate cross-talk between EGF-L and Pichia host. Molecular dynamics simulations and structural modeling shed light on potential glycosylation patterns and protein-protein interactions, enhancing our comprehension of EGF-L behavior in the host.
Beyond production optimization, the paper underscores the profound therapeutic implications of EGF-L production via Pichia. The efficient production regime can drive down costs, ensuring broader access to therapeutic EGF-L. This transformative approach holds promise for wound healing therapies and targeted cancer treatments.
Overcoming Challenges and Future Prospects:
Challenges loom, including glycosylation patterns that demand further scrutiny. The paper calls for future research to focus on optimizing glycosylation profiles for consistent biological activity and scaling up production using innovative bioreactor designs.
In a synergy of sophisticated methodologies and therapeutic foresight, Pichia-based Epidermal Growth Factor Long Human Recombinant production marks a watershed moment. The harmonious interplay between Pichia and EGF-L synthesis unveils a new era of therapeutic possibilities, potentially reshaping the landscape of medical interventions.
- Gasser B, Saloheimo M, Rinas U, et al. Pichia pastoris: Protein production host and model organism for biomedical research. Future Microbiol. 2010;5(5):727-764.
- 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, 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.
- Prabhu A, Michalak M. ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partnering properties. Cell Stress Chaperones. 2009;14(3):253-266.
- Li S, Li Y, Wang J, et al. In silico analysis of microRNA target genes and their regulation in tomato during gold nanoparticles stress. PLoS One. 2012;7(6):e38960.