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EGF Protein (Monomer)

Recombinant EGF-Protein exprimiert in Escherichia coli (E. coli).
Produktnummer ABIN1589620

Kurzübersicht für EGF Protein (Monomer) (ABIN1589620)

Target

Alle EGF Proteine anzeigen
EGF (Epidermal Growth Factor (EGF))

Protein-Typ

Recombinant

Biologische Aktivität

Active

Spezies

  • 27
  • 17
  • 9
  • 4
  • 3
  • 1
Human

Quelle

  • 40
  • 10
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
Escherichia coli (E. coli)

Reinheit

> 95 % by SDS-PAGE
  • Proteineigenschaft

    Monomer

    Verwendungszweck

    EGF

    Sequenz

    MNSDSECPLS HDGYCLHDGV CMYIEALDKY ACNCVVGYIG ERCQYRDLKW WELR

    Spezifität

    Chromosomal location:4q25

    Kreuzreaktivität

    Maus

    Produktmerkmale

    Length (aa):54

    Endotoxin-Niveau

    < 0.1 ng/μg of protein (<1EU/μg)
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  • Applikationshinweise

    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).

    Kommentare

    Cytokines & Growth Factors

    Beschränkungen

    Nur für Forschungszwecke einsetzbar
  • Format

    Lyophilized

    Rekonstitution

    We recommend a quick spin followed by reconstitution in water to a concentration of 0.1-1.0 mg/mL.

    Buffer

    PBS

    Handhabung

    Centrifuge vial prior to opening.

    Lagerung

    RT,-20 °C

    Informationen zur Lagerung

    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))

    Andere Bezeichnung

    EGF

    Hintergrund

    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

    Molekulargewicht

    6.35 kDa

    Gen-ID

    1950

    NCBI Accession

    NM_1963, NP_001954

    UniProt

    P01133

    Pathways

    NF-kappaB Signalweg, RTK Signalweg, Fc-epsilon Rezeptor Signalübertragung, EGFR Signaling Pathway, Neurotrophin Signalübertragung, 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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