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Render Timestamp: 2024-11-21T13:46:30.787Z
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XML generation date: 2024-10-15 15:01:07.288
Product last modified at: 2024-11-06T13:30:51.487Z
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PDP - Template Name: Growth Factors and Cytokines
PDP - Template ID: *******9ad1159

Human EGF Recombinant Protein #72528

    Product Information

    Storage

    Human EGF Recombinant Protein is supplied as lyophilized material that is very stable at -20°C. It is recommended to reconstitute with sterile water at a concentration of 0.1 mg/mL which can be further diluted in aqueous solutions as needed. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage.

    Once in solution, store at 4°C and use within 1 month, or store at -20ºC to -80ºC and use within 3 months to prevent loss of potency. Aliquot to avoid multiple freeze/thaw cycles if storing reconstituted material at -20ºC to -80ºC.

    Product Description

    MW (kDa) 6.2
    Purity A greater than or equal to 95% purity was determined by SDS-PAGE.
    Endotoxin Endotoxin levels are less than or equal to 1 EU / 1 μg hEGF.
    Activity The bioactivity of recombinant hEGF was determined in a BALB/c 3T3 cell proliferation assay. The ED50 of each lot is less than or equal to 100 pg/mL.

    Source / Purification

    Recombinant human EGF was expressed in E. coli and is supplied in a lyophilized form.

    Background

    Epidermal growth factor (EGF) is a small polypeptide hormone that has mitogenic properties in vivo and in vitro and affects the growth and/or differentiation of many cell types. EGF elicits biological responses by binding to its cell surface receptor, which is a transmembrane glycoprotein containing a cytoplasmic protein tyrosine kinase (PTK) (1,2). The binding of EGF to EGF receptor induces dimerization of the receptor, autophosphorylation, and activation of downstream signaling components (3). The integrated biological responses to EGF signaling are pleiotropic, including mitogenesis or apoptosis, enhanced cell motility, protein secretion, and differentiation or dedifferentiation. In addition to being implicated in organ morphogenesis, maintenance, and repair, research studies have correlated upregulated EGF receptor signaling with progression to invasion and metastasis in a wide variety of tumors (4-6). Thus, investigators have identified EGF receptor and its downstream signaling molecules as targets for therapeutic interventions in wound repair and cancer (4-6). EGF is derived from a 160 kDa precursor protein with an N-terminal extracellular domain, an EGF growth factor sequence, a transmembrane domain, and an extracellular tail (7). Once synthesized, the precursor can be stored or processed into EGF growth factor depending on different tissue/organ conditions.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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