Research Interests:I direct the University of Maryland, Baltimore Biopolymer Core Facility. This laboratory provides molecular biology support services for University research investigators on a fee-for-service basis. Support services include DNA and RNA synthesis, automated DNA sequencing, peptide synthesis and HPLC purification of synthetic polymers and mass spectrometry. The services are provided using state of the art instrumentation and up to date chemistries and technologies. The Facility is staffed by experienced individuals who can provide technical support and assistance with experimental design. Standard DNA synthesis services are enhanced by the availability of a variety of modified bases to allow fluorescent labeling, incorporation of halogenated bases, mutagenic bases and many other modified bases. Synthetic oligonucleotides can be purified, by request, by reversed phase HPLC methods. All oligonucleotides are evaluated for purity by capillary gel electrophoresis. Our automated DNA sequencing service offers rapid sequence determination with an average resolution of 800 bases per sequencing reaction. Support is available for construction of large sequence contigs by primer walking methods. Synthetic peptides can be produced and purified in scales ranging from milligram amounts to gram scale quantities. Modified amino acids, such as phosphorylated residues, are available for incorporation into synthetic peptides. All synthetic peptides are evaluated for purity by mass spectrometry. Customized services are also available to incorporate a variety of labels such as fluorescent or biotinylated tags into peptides, to synthesize conformationally constrained analogs such as cyclic peptides, or provide peptide libraries derived from combinatorial techniques.
Bramucci, M.G., B.D. Green, N.P. Ambulos, Jr., and P. Youngman. 1995. Identification of a Bacillus subtilis spoOH allele that is necessary for suppression of the sporulation-defective pheotype of a spoOA mutation. J. Bacteriol., 177:1630-1633.
Sax, C.M., A. Cvekl, M. Kantorow, R. Gopal-Srivastava, J. Ilagan, N.P. Ambulos, Jr., and J. Piatigorsky. 1995. Lens-specific activity of the mouse aA-crystallin promoter in the absence of a TATA box: Functional and protein binding analysis of the mouse aA-crystallin PE1 region. Nucl. Acids Res., 23:442-451.
Hawkinson, D. C., R. M. Pollack, and N. P. Ambulos, Jr. 1994. Evaluation of the internal equilibrium constant for 3-oxo-¿-steroid isomerase using the D38E and D38N mutants. Biochemistry, 33:12172-12183.
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