EGF stands for epidermal growth factor. Human EGF is a recombinant protein optimized for use in cell culture, differentiation studies, and functional assays.

Data and images for Human EGF

Figures

Figure 1

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In vitro generation of primary mouse neurospheres.
A single-cell suspension was prepared from mouse brain using the Neural Tissue Dissociation Kit (P) and the gentleMACS™ Dissociator. Isolated Prominin-1
+
cells were cultivated for 7 days in MACS NeuroMedium containing MACS NeuroBrew, Human FGF-2 (20 ng/mL), and Human EGF (20 ng/mL).

Figure 1

In vitro generation of primary mouse neurospheres.
A single-cell suspension was prepared from mouse brain using the Neural Tissue Dissociation Kit (P) and the gentleMACS™ Dissociator. Isolated Prominin-1
+
cells were cultivated for 7 days in MACS NeuroMedium containing MACS NeuroBrew, Human FGF-2 (20 ng/mL), and Human EGF (20 ng/mL).

Figure 2

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Human EGF activity assay.
The biological activity of Human EGF is determined by proliferation assay using 3T3 cells. Activity of Human EGF, premium grade, (red line) was compared to another commercially available product (black line).

Figure 2

Human EGF activity assay.
The biological activity of Human EGF is determined by proliferation assay using 3T3 cells. Activity of Human EGF, premium grade, (red line) was compared to another commercially available product (black line).

Figure 3

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SDS-PAGE of Human EGF, premium grade
under reduced (R) and non-reduced (NR) conditions.

Figure 3

SDS-PAGE of Human EGF, premium grade
under reduced (R) and non-reduced (NR) conditions.

Figure 4

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Human EGF biological activity.
Activity of Human EGF, premium grade, (red bar) was compared to another commercially available product (black bar).

Figure 4

Human EGF biological activity.
Activity of Human EGF, premium grade, (red bar) was compared to another commercially available product (black bar).

Figure 5

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Mass spectrometry analysis (ESI-MS) of Human EGF, premium grade. The peak corresponds to the calculated molecular mass of 6347 Da.

Figure 5

Mass spectrometry analysis (ESI-MS) of Human EGF, premium grade. The peak corresponds to the calculated molecular mass of 6347 Da.

Specifications for Human EGF

Overview

EGF stands for epidermal growth factor. Human EGF is a recombinant protein optimized for use in cell culture, differentiation studies, and functional assays.

Applications

Human EGF can be used for a variety of applications, including:
  • Proliferation and differentiation of a wide variety of cell types deriving from ectoderm and mesoderm.

Detailed product information

Background information

Epidermal growth factor (EGF) is the prototype of the large family of EGF-like proteins with a common structural motif comprising three intramolecular disulfide bonds. EGF is produced by various cell types like mammary gland cells, gut epithelial cells, and cells in the nervous system and the kidney. Production of EGF is induced by testosterone and inhibited by estrogens. EGF stimulates the proliferation and differentiation of mesenchymal cells, acts as a mitogen for fibroblasts, epithelial and endothelial cells, and promotes colony formation of epidermal cells.

Biological activity

  • Proliferation of 3T3 cells
  • research grade: ≥ 0.5×
    10
    6
    IU/mg
  • premium grade: ≥ 0.8×
    10
    6
    IU/mg
    (Typical specific activity: ≥ 2×
    10
    6
    IU/mg
    )
  • We measure the biological activity of each batch of MACS Premium-Grade Cytokines and state the results in the Certificate of Analysis (CoA). Based on the lot-specific activity, exact doses of active cytokine can be applied to cell culture experiments. This allows for reproducible cell culture conditions without the need for time-consuming lot-to-lot testing.

Quality description

Research-grade
cytokines are suitable for a wide variety of cell culture applications. They are sterile-filtered prior to lyophilization. Generally, endotoxin levels are <0.1 ng/μg (<1 EU/μg), and purities are >95%. The biological activity is tested in appropriate bioassays.
Premium-grade
cytokines offer the convenience of high and well-defined biological activities and allow exact unit dosing for demanding applications. The biological activity is determined after lyophilization and reconstitution, and normalized to WHO/NIBSC standards whenever available. In general, endotoxin levels are <0.01 ng/μg (<0.1 EU/μg), and purities are >97%. Lot-specific activities are stated in the Certificate of Analysis (www. miltenyibiotec.com/certificates).

Resources for Human EGF

Documents and Protocols

Certificates

Please follow this
link
to search for Certificates of Analysis (CoA) by lot number.

References for Human EGF

Publications

  1. Robinson, C. J. and Gaines-Das, R. (1996)
    The international standard for epidermal growth factor (EGF): comparison of candidate preparations by
    in vitro
    bioassays and immunoassays. National Institute for Biological Standards and Control.
    Growth Factors 13: 163-170
  2. Ac Kar, L. et al. (2021) Blood-based detection of lung cancer using cysteine-rich angiogenic inducer 61 (CYR61) as a circulating protein biomarker: a pilot study. Mol Oncol. 15(11): 2877-2890
  3. Giambra, M. et al. (2021) Characterizing the Genomic Profile in High-Grade Gliomas: From Tumor Core to Peritumoral Brain Zone, Passing through Glioma-Derived Tumorspheres. Biology (Basel) 10(11): 1157
  4. Tyciakova, S. et al. (2021) Overexpression of TNFα induces senescence, autophagy and mitochondrial dysfunctions in melanoma cells. BMC Cancer 21(1): 507
  5. Roswag, S. et al. (2021) Functional Characterization of Circulating Tumor Cells (CTCs) from Metastatic ER+/HER2- Breast Cancer Reveals Dependence on HER2 and FOXM1 for Endocrine Therapy Resistance and Tumor Cell Survival: Implications for Treatment of ER+/HER2- Breast Cancer. Cancers (Basel) 13(8): 1810
  6. Witte, K. E. et al. (2021) Nanopore Sequencing Reveals Global Transcriptome Signatures of Mitochondrial and Ribosomal Gene Expressions in Various Human Cancer Stem-like Cell Populations. Cancers (Basel) 13(5): 1136
  7. Smit, D. J. et al. (2020) High Sensitivity of Circulating Tumor Cells Derived from a Colorectal Cancer Patient for Dual Inhibition with AKT and mTOR Inhibitors. Cells 9(9): 2129
  8. Noonan, J. J. et al. (2019) Implementing Patient-Derived Xenografts to Assess the Effectiveness of Cyclin-Dependent Kinase Inhibitors in Glioblastoma. Cancers (Basel) 11(12): 2005
  9. Goikuria, H. et al. (2018) Characterization of Carotid Smooth Muscle Cells during Phenotypic Transition. Cells 7(3): 23
  10. Brawanski, K. et al. (2018) Efficacy of D,L-methadone in the treatment of glioblastoma in vitro. CNS Oncol 7(3): CNS18
  11. Gray, K. M. et al. (2018)
    Self-oligomerization regulates stability of survival motor neuron protein isoforms by sequestering an SCF
    Slmb
    degron.
    Mol. Biol. Cell 29(2): 96-110
  12. Cilibrasi, C. et al. (2016) Pioglitazone Effect on Glioma Stem Cell Lines: Really a Promising Drug Therapy for Glioblastoma? PPAR Res 2016: 7175067
  13. Hagmann, S. et al. (2013) Different culture media affect growth characteristics, surface marker distribution and chondrogenic differentiation of human bone marrow-derived mesenchymal stromal cells. BMC Musculoskelet Disord 14: 223
  14. Kucerova, L. et al. (2013) Altered features and increased chemosensitivity of human breast cancer cells mediated by adipose tissue-derived mesenchymal stromal cells. BMC Cancer 13: 535
  15. Diaz-Guerra, E. et al. (2012) Intrinsic cues and hormones control mouse mammary epithelial tree size. FASEB J. 26(9): 3844-3853

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