- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
CYT-798
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. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.
Description
Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa.
The EGF Long is purified by proprietary chromatographic techniques.
The EGF Long is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.
Solubility
It is recommended to reconstitute the lyophilized EGF Long in sterile 100mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized EGF Long although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF Long 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.
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 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Amino acid sequence
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.
Safety Data Sheet
Usage
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Background
Expanding Therapeutic Frontiers: Epidermal Growth Factor Long Human Recombinant Production using Pichia Expression System
Abstract:
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.
Introduction:
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.
Therapeutic Vistas:
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.
Conclusion:
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.
References
Bibliography:
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