Amphiregulin Polyclonal Antibody, PeproTech®, Invitrogen™

Description

• AA Sequence of recombinant protein: SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK
• Preparation: Produced from sera of rabbits immunized with highly pure Recombinant Human Amphiregulin
• Anti-Human Amphiregulin-specific antibody was purified by affinity chromatography employing an immobilized Human Amphiregulin matrix
• Sandwich ELISA: To detect Human Amphiregulin by sandwich ELISA (using 100 μL/well), a concentration of 0.5-2.0 μg/mL of this antibody is required
• This antigen affinity purified antibody, in conjunction with PeproTech Biotinylated Anti-Human Amphiregulin (500-P322Bt) as a detection antibody, allows the detection of at least 2000-4000 pg/mL of Recombinant Human Amphiregulin
• Western Blot: To detect Human Amphiregulin by Western Blot analysis this antibody can be used at a concentration of 0.1-0.2 μg/mL
• When used in conjunction with compatible secondary reagents, the detection limit for Recombinant Human Amphiregulin is 1.5-3.0 ng/lane, under either reducing or non-reducing conditions
• 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.