Proteomics

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Detect the shared protein components between spider dragline silk and silkworm cocoon by Label free quantitative proteomics


ABSTRACT: The spider major ampullate gland and silkworm silk gland have similar morphological structure and function, so we explored whether there are some common protein components on silks, with three biological replicates for each sample. Dragline silk samples from mature female Trichonephila clavata spider and cocoon samples are from silkworm Bombyx mori chain. The dragline silk of the spider T. clavata and cocoon silk of the silkworm B. mori were cut with scissors. First, silk samples (20 mg of each sample) were dissolved in 500 μL of 9 M LiSCN, and the supernatant was collected after centrifugation (10,000 × g, 10 min). Protein concentrations were measured via the Bradford protein assay (Beyotime, China). Then, the samples were diluted 10-fold in an 8 M urea solution, mixed with 5 × SDS–PAGE buffer, and separated using a NuPAGE 4–12% Bis-Tris protein gel (Thermo Fisher Scientific, USA). The samples were subsequently digested using trypsin, and peptides were measured via LC–MS/MS on a Q Exactive HF-X column.

ORGANISM(S): Bombyx Mori Trichonephila

SUBMITTER: Yi Wang  

PROVIDER: PXD038734 | iProX | Fri Dec 09 00:00:00 GMT 2022

REPOSITORIES: iProX

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Publications


The process of natural silk production in the spider major ampullate (Ma) gland endows dragline silk with extraordinary mechanical properties and the potential for biomimetic applications. However, the precise genetic roles of the Ma gland during this process remain unknown. Here, we performed a systematic molecular atlas of dragline silk production through a high-quality genome assembly for the golden orb-weaving spider Trichonephila clavata and a multiomics approach to defining the Ma gland tr  ...[more]

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