Thermo Fisher Scientific Human Amphiregulin Recombinant Protein, PeproTech

Applications

Tested Dilution

Publications

Western Blot (WB)

Assay-dependent

-

ELISA (ELISA)

Assay-dependent

-

Functional Assay (Functional)

Assay-dependent

View 2 publications 2 publications

In vitro Assay (IV)

-

View 9 publications 9 publications

Miscellaneous PubMed (Misc)

-

View 5 publications 5 publications

Product Specifications

Species

Human

Published species

Human, Mouse, Rat

Expression System

E. coli

Amino acid sequence

SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK

Molecular weight

11.3 kDa

Class

Recombinant

Type

Protein

Purity

≥ 95% by SDS-PAGE gel and HPLC analyses.

Endotoxin concentration

<1 EU/µg

Activity

Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml.

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Purification

purified

Contains

no preservative

Storage conditions

-20°C

Shipping conditions

Ambient

Product Specific Information

Recombinant Human Amphiregulin is an 11.3 kDa glycoprotein consisting of 98 amino acid residues.

This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

Target Information

Amphiregulin (AR) binds to EGF-Receptor (EGFR) with lower affinity than EGF. The mature secreted form AR is an 84-amino acid residue glycosylated polypeptide growth regulator, which is generated by proteolytic processing of a 252-amino acid transmembrane precursor. Seven different polypeptide ligands, which derive from distinct genes, are capable of binding to the extracellular domain of EGFR. These ligands include EGF, TGFalpha, AR, HB-EGF, cripto-1, epiregulin, and betacellulin. All of these growth factors contain a characteristic EGF-like domain which is defined by 6 evenly spaced cysteine residues that generate 3 loops through the formation of disulfide bonds. AR protein has been localized by immunohistochemistry to the epithelium of the colon, stomach, pancreas, breast, and placenta. AR is reportedly overexpressed in human cancers of breast, colon, stomach, and pancreas.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.