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EGF Protein (Monomer)

EGF Origin: Human Host: Escherichia coli (E. coli) Recombinant > 95 % by SDS-PAGE. Visualized by silver stain Active
Catalog No. ABIN1589620
  • Target See all EGF Proteins
    EGF (Epidermal Growth Factor (EGF))
    Protein Type
    Recombinant
    Biological Activity
    Active
    Protein Characteristics
    Monomer
    Origin
    • 31
    • 19
    • 10
    • 4
    • 3
    • 1
    Human
    Source
    • 36
    • 9
    • 8
    • 4
    • 3
    • 2
    • 1
    • 1
    • 1
    • 1
    Escherichia coli (E. coli)
    Sequence
    MNSDSECPLS HDGYCLHDGV CMYIEALDKY ACNCVVGYIG ERCQYRDLKW WELR
    Cross-Reactivity
    Mouse (Murine)
    Characteristics
    Length (AA): 54
    Chromosomal location: 4q25
    The biological activity was determined by the ability to induce EGF receptor phosphorylation in the A431 tumor cell line [Soler et al, J Chromatography B, 788, 2003] and the induction of proliferation in NHDF cells (Normal Human Dermal Fibroblasts).
    Purity
    > 95 % by SDS-PAGE. Visualized by silver stain
    Top Product
    Discover our top product EGF Protein
  • Comment

    Cytokines & Growth Factors

    Restrictions
    For Research Use only
  • Format
    Lyophilized
    Reconstitution
    Reconstitution in water to a concentration of 0.1-1.0 mg/mL.
    Buffer
    PBS
    Handling Advice
    Centrifuge vial prior to opening.
    Storage
    -20 °C
    Storage Comment
    The lyophilized protein is stable for a few weeks at room temperature, but best stored at -20 °C. Reconstituted EGF should be stored in working aliquots at -20 °C.
  • Target
    EGF (Epidermal Growth Factor (EGF))
    Alternative Name
    EGF (EGF Products)
    Synonyms
    HOMG4 Protein, URG Protein, AI790464 Protein, CEGF Protein, epidermal growth factor Protein, pro-epidermal growth factor Protein, EGF Protein, egf Protein, CpipJ_CPIJ020278 Protein, Egf Protein
    Background
    Epidermal growth factor (EGF) is the founding member of the EGF family that also includes TGFα, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth factor (HBEGF), epigen, and the neuregulins (NRG) 1 through 6. Members of the EGF family share a structural motif, the EGF-like domain, which is characterized by three intra-molecular disulfide bonds that are formed by six similarly spaced conserved cysteine residues. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The 1207 amino acid (aa) human EGF precursor contains nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is generated by proteolytic excision of the EGF domain proximal to the transmembrane region. Mature human EGF shares 70 % aa sequence identity with mature mouse and rat EGF. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2. Biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture.
    Synonyms: EGF, URG, HOMG4, Urogastrone, Epidermal growth factor
    Molecular Weight
    6.35 kDa
    NCBI Accession
    NP_001954, NM_001178131
    UniProt
    P01133
    Pathways
    NF-kappaB Signaling, RTK Signaling, Fc-epsilon Receptor Signaling Pathway, EGFR Signaling Pathway, Neurotrophin Signaling Pathway, Regulation of Carbohydrate Metabolic Process, Hepatitis C, Protein targeting to Nucleus, Interaction of EGFR with phospholipase C-gamma, Thromboxane A2 Receptor Signaling, EGFR Downregulation
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