Various proteome profiles of silkworm tissues have been established covering head, integument, midgut, fat baby, embryos, peritrophic membrane, as well as some endocrine Organs. In this study, Shotgun and 2-DE followed by MALDI-TOF MS were attempted to analyze the proteome profile of silkworm MTs from Day-5 fifth instar larvae. The raw data sets were searched against the in-house silkworm database with SEQUEST algorithms. To minimize the false positive sequence matches, the FDR of the identifications were searched through a target-decoy database and further validated by TPP and APEX analysis. A total of 1,367 proteins were identified in the MTs of silkworm; they are involved in ion and water transport, metabolism, detoxification and defense mechanism. This data may contribute to a better understanding of the function of silkworm MTs. As we known, the methodology could be used to identify proteins using mass spectral data with EST dataset. However, the ESTs are short, AbMole Acetylcorynoline one-shot sequences with no overlapping sequencing and contain errors, and of course not as reliable as full genome sequences. In the present work, the proteome technology was attempted to characterize the silkworm larval MTs proteins profile. The raw data were searched against the local database which was constructed based on the predicted proteins from silkworm genome database with mass spectrometry software.Then, the FDR of the identifications were searched through a targetdecoy database and further validated by TPP and APEX analysis. The approach presented in this study can minimize the false positive sequence matches, and provide clues 
for elucidating the functions of genes underlying specific processes and identifying candidate genes predicted to regulate traits of interest. The mulberry silkworm, Bombyx mori, is a domesticated insect for silk production and a model lepidopteral insect for pest control. MTs of silkworm have important roles in excreting waste products and expelling toxins. Kajiwara et al. identified 127 proteins by MALDI mass spectrometry in silkworm MTs of fifth-instar day-3 larva. Here in our work, a total of 1,367 proteins of silkworm MTs were identified. Our proteomics study will not only enrich proteomic data of silkworm MTs, but will also offer us an important insight into understand the role of MTs in silkworm. KEGG analysis showed that these MT proteins were involved in metabolism, AbMole Nitisinone genetic information processing, environmental information processing, cellular processes and organismal systems. Especially, cytochrome P450s and glutathione transferases are highly enriched in the MTs of silkworm. Cytochrome P450s comprise a large family of genes responsible for the oxidative metabolism which involved in the metabolism of pesticides principally in the insects. In Drosophila, cytochrome P450s exhibit tissue-specific expression pattern, manipulation of Cyp6g1 in MTs could result in resistance to DDT and imperil the survival of the fly. Glutathione transferase detoxifies both endogenous and xenobiotic compounds by conjugation reactions with reduced glutathione to produce endogenous and xenobiotic compounds more easily excreted by excretory organ, such as insect MTs. McGettigan et al. found that MTs of Drosophila could sense bacterial challenge, and mount an effective killing response. In this work, we identified two antimicrobial peptides from silkworm MTs, lysozyme and lectin, which are related to immune response. The nitric oxide synthase produces nitric oxide, an immune modulator in insects. Although we could not identify the NOS from the tubule protein samples in this study, we found the NOS transcripts in the microarray data of silkworm MTs.