The National Institute of Standards and Technology (NIST) has compiled and maintained a Short Tandem Repeat DNA Internet Database (http://www.cstl.nist.gov/biotech/++ +strbase/) since 1997 commonly referred to as STRBase. This database is an information resource for the forensic DNA typing community with details on commonly used short tandem repeat (STR) DNA markers. STRBase consolidates and organizes the abundant literature on this subject to facilitate on-going efforts in DNA typing. Observed alleles and annotated sequence for each STR locus are described along with a review of STR analysis technologies. Additionally, commercially available STR multiplex kits are described, published polymerase chain reaction (PCR) primer sequences are reported, and validation studies conducted by a number of forensic laboratories are listed. To supplement the technical information, addresses for scientists and hyperlinks to organizations working in this area are available, along with the comprehensive reference list of over 1300 publications on STRs used for DNA typing purposes.

Analysis of length polymorphism at short tandem repeat (STR) loci utilizing the polymerase chain reaction (PCR) process has proven to be an ideal assay for human identification purposes. The short length of STR loci coupled with the amplification of target sequence through PCR allows for a robust, sensitive, and specific assay for highly polymorphic markers. A multiplex containing fifteen STR loci plus the gender-determining locus Amelogenin was developed to provide a single amplification/detection of all CODIS (Combined DNA Index System) STR loci (CSF1PO, D3S1358, D5S818, D7S820, D8S1179, D13S317, D16S539, D18S51, D21S11, FGA, THO1, TPOX, and vWA) as well as two internationally-accepted STRs (D2S1338 and D19S433). By incorporating five-dye fragment analysis technology and non-nucleotide linkers, previously optimized AmpFℓSTR® kit primer sequences have been maintained. This kit has been developed in accordance with the standards of the forensic community as defined by the DNA Advisory Board. Validation studies were performed to include developmental validation, and the results support the use of the AmpFℓSTR® Identifiler® PCR Amplification Kit for human identity and parentage testing.

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of inhibitors from cytosolic fractions demonstrated a precursor-product relationship. Within the cytosolic Recently, we reported the identification and partial fraction, 26-, 29-, and 30-kDa inhibitors were detected characterization of three serine protease inhibitors in the early chases (0 and 15 min) but they form precur-(M r 33,000, 31,000, and 27,000) from the extracellular sors to the synthesis of the 33-kDa inhibitor which acmatrix (ECM) of human umbilical vein endothelial cumulated in the later chases (30 min to 1 h). When cells and skin cells. Here, we report that a full-length pulse-chase experiments were performed in the prescDNA clone for the 33-kDa inhibitor from SV-40 transence of tunicamycin, synthesis as well as sequestration formed human skin fibroblasts (t12FB) is identical to of the three inhibitors into ECM was completely inhiba recombinant trypsin/tissue factor pathway inhibitor ited. In the presence of tunicamycin, the cells synthecalled TFPI-2 from placenta. By immunoblotting, the three inhibitors from ECM and cell lysates demon-sized and sequestered a single 25.5-kDa inhibitor into strated cross-reactivity with an antiTFPI-2 IgG. To fur-ECM. Peak quantities of the 25.5-kDa inhibitor apther elucidate how these inhibitors are related, pulse-peared in the ECM after 6 h chase while they were chase labeling of t12FB with [ 35 S]methionine followed 1 h for the 27-and 31-kDa inhibitors and 3 h for the by immunoprecipitation with antiTFPI-2 IgG was per-33-kDa inhibitor. To further support that the three informed on ECM and cytosolic proteins. A precursor-hibitors are related but only differ in the extent of product relationship did not exist between the three glycosylation, the 33-kDa inhibitor from the t12FB inhibitors from ECM. In contrast, the various species ECM was deglycosylated with N-glycosidase F and the products were identified by immunoblotting with anti-TFPI-2 IgG. The enzyme released the 31-, 27-, and 25.5-Certain commercial equipment, instruments, and materials are kDa inhibitors from the 33-kDa inhibitor. Collectively, identified in this paper in order to specify the experimental procedure these results demonstrate that the ECM-associated 33-, ECM. Quantitation of the inhibitors with cell-condi-2 To whom correspondence should be addressed. Fax: (312) 908-1984. tioned medium and ECM fractions reveals that 70-75% 82

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