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Recombinant Human Amphiregulin protein (rFc Tag)

Species

Human

Purity

>85 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg4569

Validation Data Gallery

  • Purity of Recombinant Human Amphiregulin was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

    Purity of Recombinant Human Amphiregulin was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

Product Information

Purity >85 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Human Amphiregulin protein Ser101-Lys187 (Accession# P15514) with a rabbit IgG Fc tag at the N-terminus.
GeneID 374
Accession P15514
PredictedSize 37.3 kDa
SDS-PAGE 10-16 kDa and 37-48 kDa, reducing (R) conditions
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Amphiregulin (AREG) is one of the ligands of the epidermal growth factor receptor (EGFR). AREG plays a central role in mammary gland development and branching morphogenesis in organs and is expressed both in physiological and in cancerous tissues. The AREG protein is synthesized as a 252-amino acid transmembrane precursor, pro-AREG. At the plasma membrane, pro-AREG is subjected to sequential proteolytic cleavages within its ectodomain and is then released as the soluble AREG protein. Depending on the cell type and microenvironment, AREG can be produced in multiple cellular and mature forms using alternative pro-AREG cleavage sites and glycosylation motifs.

References:

1. Brown C.L., et al. (1998). J Biol Chem. Jul 3;273(27):17258-17268.
2. Busser B, et al. (2011). Biochim Biophys Acta. Dec;1816(2):119-131. 
3. McBryan J, et al. (2008). J Mammary Gland Biol Neoplasia. Jun;13(2):159-69.