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Epiregulin Protein (EREG) (AA 63-108)

This Recombinant Epiregulin protein is produced in Escherichia coli (E. coli).
Catalog No. ABIN2666804

Quick Overview for Epiregulin Protein (EREG) (AA 63-108) (ABIN2666804)

Target

See all Epiregulin (EREG) Proteins
Epiregulin (EREG)

Protein Type

Recombinant

Biological Activity

Active

Origin

  • 9
  • 5
  • 1
Human

Source

  • 10
  • 3
  • 1
Escherichia coli (E. coli)

Application

Flow Cytometry (FACS)

Purity

> 95 % , as determined by Coomassie stained SDS-PAGE.
  • Protein Characteristics

    AA 63-108

    Sterility

    0.22 μm filtered

    Endotoxin Level

    Less than 0.01 ng per μg cytokine as determined by the LAL method.

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  • Application Notes

    Optimal working dilution should be determined by the investigator.

    Comment

    Biological activity: ED50 = 0.5 - 3.0 ng/ml, corresponding to a specific activity of 0.33 - 2.0 x 106 units/mg, as determined by induction of BALB/3T3 cell proliferation.

    Restrictions

    For Research Use only
  • Format

    Liquid

    Reconstitution

    For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 μg/mL in sterile buffer (PBS, HPBS, DPBS, and EBSS) containing carrier protein such as 1 % BSA or HSA. After dilution, the cytokine can be stored between 2 °C and 8 °C for one month or from -20 °C to -70 °C for up to 3 months.

    Buffer

    0.22 μm filtered protein solution is in PBS, pH 7.2.

    Handling Advice

    Avoid repeated freeze/thaw cycles.

    Storage

    -20 °C

    Storage Comment

    Unopened vial can be stored between 2°C and 8°C for three months, at -20°C for six months, or at -70°C for one year.
  • Target

    Epiregulin (EREG)

    Alternative Name

    Epiregulin

    Background

    Epiregulin was initially identified as a growth-inhibitory factor from the conditioned medium of the murine tumor cell line NIH3T3/clone T7. It belongs to the EGF family of proteins that includes EGF, TGF-α, heparin-binding EGF like-growth factor (HB-EGF), epigen, epiregulin, betacellulin, neuroregulin, and tomoregulin. It posesses 24-50 % amino acid sequence identity with sequences of other EGF-related growth factors. All the EGF family members are synthesized as type I membrane protein precursors, which can undergo proteolytic cleavage at the plasma membrane to release a mature soluble ectodomain. Epiregulin acts as an autocrine growth factor in human epidermal keratinocytes and it can be induced by HB-EGF, amphiregulin, and TGF-α. Epiregulin is expressed by, and plays a key role in, immune-related responses of keratinocytes and tissue resident macrophages. It has been shown that epiregulin-deficient (EP-/-) mice develop chronic dermatitis. Also, epiregulin is involved in proinflammatory cytokine production in bone marrow-derived macrophages. In addition, epiregulin induces proliferation of human corneal epithelial cells and its expression can be induced in these cells by TGF-α, HB-EGF, AR, and EGF. Epiregulin plays a role in the development of hyperkeratosis during the pathogenesis of middle ear cholesteatoma, and it is overexpressed in psoriatic epidermis. Epiregulin polymorphisms seem to be associated with susceptibility to different clinical phenotypes of TB, and epiregulin modulates the innate immune responses of TB.

    Molecular Weight

    The 47 amino acid recombinant protein has a predicted molecular mass of approximately 5.4 kDa. The DTT-reduced and non-reduced protein migrate at approximately 6 kDa and 8 kDa, respectively, by SDS-PAGE. The predicted N-terminal amino acid is Met.

    Pathways

    RTK Signaling, Fc-epsilon Receptor Signaling Pathway, EGFR Signaling Pathway, Neurotrophin Signaling Pathway, Regulation of Muscle Cell Differentiation
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