Abbreviation
Recombinant Human AREG protein, partial (Active)
Purity
>95% as determined by SDS-PAGE.
Endotoxin
Less than 1.0 EU/μg as determined by LAL method.
Activity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is between 5-10 ng/ml.
Alternative Names
AREG; AREGB; SDGF; Amphiregulin; AR; Colorectum cell-derived growth factor; CRDGF
Species
Homo sapiens (Human)
Expression Region
101-198aa
Target Protein Sequence
SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK
Note: The complete
sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is
translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application,
please explicitly request the full and complete sequence of this protein before ordering.
Tag Info
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Buffer
Lyophilized from a 0.2 µm filtered PBS, pH 7.4
Lead Time
5-10 business days
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Datasheet & COA
Please contact us to get it.
Description
Amphiregulin is a key EGF receptor ligand that drives autocrine and paracrine signaling in tumor proliferation, making it a critical target in cancer biology research. This tag-free recombinant human AREG (residues 101–198) encompasses the mature EGF-like domain responsible for EGFR binding, and its confirmed ED50 of 5–10 ng/mL in Balb/c 3T3 proliferation assays demonstrates robust receptor-binding potency suitable for cell proliferation and survival studies, EGFR-ligand competition assays by ELISA or SPR, and in vivo tumor biology models. The E. coli expression system yields a non-glycosylated protein that provides a defined, homogeneous preparation — an advantage when glycosylation variability could confound receptor-binding quantitation or use as an ELISA standard for antibody characterization. Purity exceeding 95% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the criteria typically required for sensitive cell-based assays and wound healing migration studies.
