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Vol. 27, Issue 2, 274-280, February 1999
National Center For Toxicological Research, Jefferson, Arkansas
(Y.M.T., G.-F.C., P.A.T., F.F.K.);
Arkansas Cancer Research Center,
Little Rock, Arkansas (N.P.L.); and
Cancer Institute, Chinese Academy
of Medical Sciences/Beijing Union Medical College, Beijing,
China (D.-X.L.)
An antipeptide antibody was raised against a 14-mer synthetic
peptide (CDFRANPNEPA KMN) corresponding to the amino acid sequence from
491 to 504 of human cytochrome P-450 (CYP)1B1. Rabbit-derived antisera
demonstrated the ability to induce moderately high antibody titers
(>1:105) as judged by enzyme-linked immunosorbent assay.
In Western blot analysis, the purified antibody recognized a single
protein band (estimated as 56 kDa) in microsomes prepared from human
and rodent tissues. No significant cross-reactivity to either human
CYP1A1 or human CYP1A2 protein was detected. Titration studies using recombinant human CYP1B1 and an enhanced chemiluminescence-based detection method demonstrated a minimal detection sensitivity for this
antiserum at about 0.34 ng/band in 8 × 7-cm minigels. The
immunoprecipitation and immunoinhibition results indicate that this
antisera recognizes the nondenatured human CYP1B1 protein but does not
inhibit its enzyme activity. Using this antibody, CYP1B1 protein was
detected in nine different human tissues and in cultured cells induced
by various chemicals. This highly specific, highly sensitive antibody
provides an important tool to study tissue distribution and cellular
expression levels of CYP1B1, with negligible cross-reactivity from the
other members of the CYP1 family.
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