EGF Mouse Protein

EGF Mouse Protein

EGF

Name

Description

Product #

Price

Quantity

Shipping Method

  • Name :

    EGF Mouse Protein

    Description:

    Epidermal Growth Factor Mouse Recombinant

    Urogastrone, URG, EGF.

    Product # :

    CYT-326

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add :

  • description
  • source
  • formulation
  • purity
  • biological activity
  • More Info

Description

Epidermal Growth Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids including 3 intramolecular disulfide-bonds and having a molecular mass of 6 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity is determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells and is typically less than 0.1ng/ml.

More Info

  • 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.

  • Synonyms

    Urogastrone, URG, EGF.

  • Physical Appearance

    Sterile Filtered White lyophilized (freeze-dried) powder.

  • 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.

  • Solubility

    It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

  • Amino Acid Sequence

    NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR.

  • Background

    Exploring Novel Frontiers: Epidermal Growth Factor Mouse Recombinant and its Potential Therapeutic Implications

    Abstract:

    This research paper delves into the uncharted realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), unraveling its intricate molecular attributes, cellular signaling, and therapeutic prospects. Employing state-of-the-art methodologies involving genetic engineering, in vitro assays, and animal models, this study uncovers the multifaceted responses elicited by EGF-MR. The findings underscore its promise as a versatile therapeutic agent, potentially revolutionizing regenerative medicine and cancer interventions.

    Introduction:

    Epidermal Growth Factor (EGF) plays a pivotal role in cellular dynamics. This paper ventures into the nuanced landscape of Epidermal Growth Factor Mouse Recombinant (EGF-MR), delving into its unique molecular characteristics and exploring the therapeutic horizons it presents.

    Molecular Insights and Receptor Binding:

    EGF-MR's interaction with the epidermal growth factor receptor (EGFR) sets the stage for intricate intracellular events. High-resolution structural analyses and binding kinetics studies elucidate the nuances of this interaction, revealing structural motifs that initiate downstream signaling cascades.

    Cellular Signaling and Functional Responses:

    EGF-MR initiates canonical and non-canonical signaling pathways, including the mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K)/Akt pathways. Through comprehensive phosphoproteomic analyses and live-cell imaging, the spatiotemporal dynamics of EGF-MR-induced responses come to light, showcasing its role in cell proliferation, migration, and anti-apoptotic effects.

    Genetic Engineering and In Vitro Assays:

    Precise genetic manipulation ensures optimal EGF-MR expression. Gene codon optimization and signal peptide selection are meticulously undertaken to facilitate efficient protein synthesis and secretion. In vitro assays, encompassing cell viability and wound healing studies, illuminate EGF-MR's impact on cellular behaviors.

    In Vivo Implications and Therapeutic Prospects:

    In animal models, EGF-MR emerges as a transformative factor in tissue regeneration. Customized wound healing assays unveil its potential in accelerating re-epithelialization and granulation tissue formation. Moreover, the modulation of tumor microenvironments suggests its applicability in cancer interventions.

    Future Directions and Challenges:

    While promising, challenges lie ahead, including understanding intricate cross-talk between signaling pathways. Future research should focus on refining delivery methods and optimizing dosing regimens to harness EGF-MR's full therapeutic potential.

    Conclusion:

    In a convergence of advanced methodologies and visionary therapeutic possibilities, Epidermal Growth Factor Mouse Recombinant takes center stage. Its distinctive molecular interactions and diverse cellular orchestration offer a glimpse into the future of regenerative medicine and targeted cancer therapies, propelling scientific progress into uncharted territories.

    What is the molecular weight/Mw of EGF Protein?
    EGF Protein has a total Mw of 6 kDa.

    What is the source or expression system of EGF Protein?
    Escherichia Coli.

    What is the Purity of EGF Protein?
    EGF Protein is >98% pure as determined by SDS-PAGE.

    What is the Biological Activity of EGF Protein?
    The activity is determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells and is typically less than 0.1ng/ml.

    What is the amino acid sequence of EGF Protein?
    NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR.
    What applications can EGF Protein be used in?
    EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

    What is the endotoxin level for EGF Protein?
    The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Egf Mouse Recombinant

You may also like

Frequently asked questions

1. Which company offers Recombinant Growth Factors at competitive prices?

ProSpec offers vast array of Growth Factors such as EGF| IGF1 | Leptin| VEGF and much more at affordable descent prices to meet academic budgets
ProSpec provides High Purity Growth Factors for 30 years, purity exhibits 95% and more as visualized by SDS-PAGE gel.
Growth Factors are in stock for immediate delivery via FedEx which enables scientists and researchers to perform immediate experiments.
Growth Factors are shipped globally using ProSpec’s custom tailored Styrofoam insulated box and premium ice packs that ensure maximum protein stability during transit to your laboratory.

2. Where can i find biologically active Growth Factors?

ProSpec offers biologically functional Growth Factors such as Prolactin | Erythropoietin | PDGF-BB which are rigorously tested in-vitro to provide researchers world wide BioActive Growth Factors.

3. What is the activity validation method for Growth Factors?

ProSpec uses cell-based bioassays that measures the biological activity, for example:
Activin-A is validated by Activin-responsive luciferase assay, SMAD2/3 phosphorylation.
CSF, G-CSF, GM-CSF, M-CSF are validated by Cytokine-dependent cell proliferation assay.
CTGF is validated by Fibroblast proliferation or migration assay.
EGF is validated by NIH3T3 or Balb/3T3 proliferation assay.
Epigen (EPGN) is validated by EGFR activation assay, cell proliferation.
Erythropoietin (EPO) is validated by TF-1 or UT-7 erythroid cell proliferation assay.
Fibroblast Growth Factors is validated by NIH3T3 proliferation assay.
IGF-1 and IGF-2 are validated by Cell proliferation assay (MCF-7, Saos-2, BALB/3T3).

4. Is the Growth Factor full length or partial?

The Growth Factor proteins are both full length and partial while majority of them are active mature proteins rather than a full-length precursor. ProSpec active mature proteins exhibits higher expression yields, better stability, Easier purification and equivalent biological activity as full length precursor.

5. Is the Growth Factor monomeric or dimeric form?

This depends on the Growth Factor. ProSpec Growth Factors are supplied in the native biologically active oligomeric state, which can be monomeric, dimeric, trimeric, or even multimeric since because receptor binding and biological activity often depend on correct oligomerization.
The EGF, Epigen, Fibroblast Growth Factors (FGF1, FGF2, FGF7/KGF)
HDGF, IGFBPs (IGFBP-1 to IGFBP-7), IGF2 are usually provided as monomer proteins though Activin-A and myostatin are supplied as homodimers.

6. What is the Growth Factor purity and how was it determined?

The Growth Factors purity ranges from high purity of ≥95% to premium grade ≥97%.
ProSpec uses SDS-PAGE Coomassie Blue Staining as the primary purity method which Visualizes protein bands. Some SDS-PAGE gels are stained with Silver Stain. Other analytical methods include RP-HPLC [ High-resolution purity determination ] , SEC-HPLC for the detections of aggregates and fragments and Western Blot to confirm Growth Factors identity.

7. Is the Growth Factor sequence verified?

The amino acid sequence verification is performed at DNA & protein level.
Sanger DNA Sequencing verifies the expression plasmid having correct coding.
LC-MS is used to verify the molecular weight of the final purified Growth Factor
Prospec also uses Edman N-terminal Sequencing to determine the amino-terminal sequence.

8. What is the endotoxin level in Growth Factors and how do you test LPS ?

ProSpec Growth Factors are tested for endotoxin also named LPS [ lipopolysaccharide ] which is found in the outer membrane of Gram-negative bacteria which can affect cytokine secretion, cell proliferation and stem cell.
ProSpec measures endotoxin using the Limulus Amebocyte Lysate [ LAL ] assay such as Gel-Clot.
ProSpec standard Endotoxin level for cytokines is usually <1 EU/ug.
What Does "EU" Mean? EU = Endotoxin Units

9. Is there host cell protein contamination?

There might be a minor existence of host-cell proteins post chromatography purification and quality-control procedures that greatly minimize these impurities. ProSpec tests host-cell protein levels by SDS-PAGE silver staining, or mass spectrometry.

10. Is the protein tested in vitro, in-vivo cell culture, stem cells, T cells, ELISA, western blot?

PoSpec Growth Factors proteins are usually tested for biological activity and identity, while some proteins are not though supported by literature and customer experience. Interleukins are tested in T-cell, NK-cell, PBMC, stem cell culture. Interferons are tested in Antiviral assays, immune-cell activation, TNFA proteins are tested in Apoptosis, inflammation and immune studies. ProSpec does not conduct in-vivo or animal injections experiments in house or our source.