Human TBPL1 (TATA box-binding protein-like protein 1) ELISA Kit

TBPL2 is the most recently discovered and less characterized member of the TATA box binding protein (TBP) family that also comprises TBP, TATA box binding protein-like 1 (TBPL1), and Drosophila melanogaster TBP related factor (TRF). In this paper we report our in silico and in vitro data on (i) the genomics of the TBPL2 gene in Homo sapiens, Pan troglodytes, Mus musculus, Rattus norvegicus, Gallus gallus, Xenopus tropicalis, and Takifugu rubripes; (ii) its evolution and phylogenetic relationship with TBP, TBPL1, and TRF; (iii) the structure of the TBPL2 proteins that belong to the recently identified group of the intrinsically unstructured proteins (IUPs); and (iv) TBPL2 expression in different organs and cell types of Homo sapiens and Rattus norvegicus. Similar to TBP, both the TBPL2 gene and protein are bimodular. The 30 region of the gene encoding the DNA binding domain (DBD) was well conserved during evolution. Its high homology to vertebrate TBP suggests that TBPL2 also should bind to the TATA box and interact with the proteins binding to TBP carboxy-terminal domain, such as the TBP associated factors (TAFs). As already demonstrated for TBP, TBPL2 amino-terminal segment is intrinsically unstructured and, even though variable among vertebrates, comprises a highly conserved motif not found in any other known protein. Absence of TBPL2 from the genome of invertebrates and plants demonstrates its specific origin within the subphylum of vertebrates. Our RT-PCR analysis of human and rat RNA shows that, similar to TBP, TBPL2 is ubiquitously synthesized even though at variable levels that are at least two orders of magnitude lower. Higher expression of TBPL2 in the gonads than in other organs suggests that it could perform important functions in gametogenesis. Our genomic and expression data should contribute to clarify why TBP has a general master role within the transcription apparatus (TA), whereas both TBPL1 and TBPL2 perform tissue-specific functions.

Recent advances in the understanding of microRNA have rendered microRNAs (miRNAs) a compelling novel class of biomarker in cancer biology. However, the specific function of miRNA-18a (miR-18a) in colorectal cancer (CRC) remains unclear. In the present study, the role of miR-18a in the carcinogenesis of CRC was investigated. miR-18a expression was assessed in CRC specimens and cell lines using reverse transcription-quantitative polymerase chain reaction (RT-qPCR). The targets of miR-18a were predicted using bioinformatics tools. Luciferase reporter assays were used to confirm the functional association between miR-18a and its target genes. The effect of miR-18a on cell proliferation, invasion and migration was confirmed in vitro by a methylthiazol tetrazolium assay, cell invasion assay, and wound healing assay. Gene and protein expression was examined using RT-qPCR and western blotting, respectively. It was demonstrated that the expression of miR-18a in CRC tissues and cell lines was markedly lower than in normal control tissues and cells, respectively. In addition, miR-18a inhibited cell proliferation, invasion and migration in CRC cells. Moreover, TATA box-binding protein-like protein 1 (TBPL1) was identified as a potential target gene of miR-18a in the bioinformatics analysis and luciferase reporter assays, and miR-18a directly inhibited TBPL1 expression by targeting its 3'-untranslated region. Furthermore, TBPL1 was downregulated and inversely correlated with miR-18a expression in tissues. These findings demonstrate that miR-18a exhibits a protective role in CRC via inhibiting proliferation, invasion and migration of CRC cells by directly targeting the TBPL1 gene.