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Amphiregulin, Human recombinant protein
AR, AREG, Colorectum cell-derived growth factor (CRDGF)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P15514 |
|---|---|
| Calculated MW | 11.3 kDa |
| Gene ID | 374 |
|---|---|
| Gene Symbol | AREG |
| Other Names | AR, AREG, Colorectum cell-derived growth factor (CRDGF) |
| Gene Source | Human |
| Source | E.coli |
| Assay&Purity | SDS-PAGE; ≥95% |
| Assay2&Purity2 | HPLC; |
| Recombinant | Yes |
| Sequence | SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK |
| Target/Specificity | Amphiregulin |
| Application Notes | Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C. |
| Format | Lyophilized powder |
| Storage | -20°C; Sterile filtered through a 0.2 micron filter. Lyophilized from 5 mM Sodium phosphate, pH 7.0. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Amphiregulin is an EGF related growth factor that signals through the EGF/TGF-a receptor, and stimulates growth of keratinocytes, epithelial cells and some fibroblasts. Amphiregulin also inhibits the growth of certain carcinoma cell lines. Synthesized as a transmembrane protein, amphiregulin’s extracellular domain is proteolytically processed to release the mature protein. There are 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds essential for biological activity. Recombinant human Amphiregulin is a 11.3 kDa glycoprotein consisting of 98 amino acid residues.
References
Plowman G.D.,et al.Mol. Cell. Biol. 10:1969-1981(1990).
Kalnine N.,et al.Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Shoyab M.,et al.Science 243:1074-1076(1989).
Shoyab M.,et al.Proc. Natl. Acad. Sci. U.S.A. 85:6528-6532(1988).
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