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Application of HisDetector Ni‐Hrp conjugate to the detection of various Histidine tagged proteins.
Author(s) -
Jerome Lawrence Francis,
Russell Danielle,
Levin Josh,
Webster Helen,
Federman Mike,
Sreeram Renjina
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a634-b
Subject(s) - nitrilotriacetic acid , conjugate , histidine , horseradish peroxidase , chemistry , biochemistry , alkaline phosphatase , recombinant dna , protein tag , peroxidase , nickel , enzyme , microbiology and biotechnology , biology , fusion protein , chelation , organic chemistry , mathematical analysis , mathematics , gene
The expression and purification of polyhistidine‐tagged recombinant proteins can be monitored on Western blots using anti‐His antibodies or with nickel‐enzyme conjugates. KPL, Inc. supplies nickel‐nitrilotriacetic acid conjugates of horseradish peroxidase (HisDetector™ Nickel‐HRP) and alkaline phosphatase (HisDetector™ Nickel‐AP) for this purpose. HisDetector conjugates provide highly specific detection of histidine‐tagged proteins in a variety of cell extracts. In this poster, we show that HisDetector conjugates can be used for the detection of a wide variety of proteins containing C‐terminal and N‐terminal histidine tags.