Phone:
+1 877 302 8632
Fax:
+1 888 205 9894 (Toll-free)
E-Mail:
orders@antibodies-online.com

EGF Protein (AA 971-1023) (His tag)

EGF Origin: Human Host: HEK-293 Cells Recombinant >95 % (SDS-PAGE) Active
Catalog No. ABIN6253313
  • Target See all EGF Proteins
    EGF (Epidermal Growth Factor (EGF))
    Protein Type
    Recombinant
    Biological Activity
    Active
    Protein Characteristics
    AA 971-1023
    Origin
    • 26
    • 16
    • 9
    • 4
    • 3
    • 1
    Human
    Source
    • 39
    • 9
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    HEK-293 Cells
    Purification tag / Conjugate
    This EGF protein is labelled with His tag.
    Purpose
    EGF (human) (rec.) (His)
    Specificity
    Human EGF (aa 971-1023) is fused at the C-terminus to a His-tag.
    Characteristics
    Protein. Human EGF (aa 971-1023) is fused at the C-terminus to a His-tag. Source: HEK 293 cells. Endotoxin content: <0.01EU/μg protein (LAL test, Lonza). Lyophilized from 0.2μm-filtered solution in PBS. Purity: >95 % (SDS-PAGE). Epidermal growth factor (EGF) is a growth factor and the founding member of the EGF family. 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. 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. These receptors undergo a complex pattern of ligand induced homo or heterodimerization to transduce EGF family signals. EGF binds to the receptor EGFR stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity initiates a signal transduction cascade that results in a variety of biochemical changes within the cell, including a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR, which lead to DNA synthesis, cell growth, proliferation and differentiation. Other biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture. Defects in EGF are the cause of hypomagnesemia type 4 (HOMG4), also known as renal hypomagnesemia normocalciuric. HOMG4 is a disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to mederate psychomotor retardation, and brisk tendon reflexes.
    Purity
    >95 % (SDS-PAGE)
    Endotoxin Level
    <0.01EU/μg protein (LAL test, Lonza).
    Biological Activity Comment
    Measured by its ability to stimulate the proliferation of balb/c3T3 cells. The ED50 for this effect is typically 0.1ng/ml, corresponding to a specific activity of 1x 107 units/mg.
    Top Product
    Discover our top product EGF Protein
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Concentration
    Lot specific
    Buffer
    Lyophilized from 0.2μm-filtered solution in PBS.
    Handling Advice
    Avoid freeze/thaw cycles. PBS containing at least 0.1 % BSA should be used for further dilutions.
    Storage
    4 °C,-20 °C
    Storage Comment

    Short Term Storage: +4°C

    Long Term Storage: -20°C

    Use & Stability: Stable for at least 1 year after receipt when stored at -20°C. Working aliquots are stable for up to 3 months when stored at -20°C.

  • Target
    EGF (Epidermal Growth Factor (EGF))
    Alternative Name
    EGF (EGF Products)
    Background

    Alternate Names/Synonyms: Pro-Epidermal Growth Factor, HOMG4, URG

    Product Description: Epidermal growth factor (EGF) is a growth factor and the founding member of the EGF family. 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. 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. These receptors undergo a complex pattern of ligand induced homo or heterodimerization to transduce EGF family signals. EGF binds to the receptor EGFR stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity initiates a signal transduction cascade that results in a variety of biochemical changes within the cell, including a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR, which lead to DNA synthesis, cell growth, proliferation and differentiation. Other biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture. Defects in EGF are the cause of hypomagnesemia type 4 (HOMG4), also known as renal hypomagnesemia normocalciuric. HOMG4 is a disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to mederate psychomotor retardation, and brisk tendon reflexes.

    Molecular Weight
    ~10kDa (SDS-PAGE)
    NCBI Accession
    NP_001954
    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
You are here:
Support