Proteomics

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MSP22.8 is a protease inhibitor-like protein involved in shell mineralization in the edible mussel Mytilus galloprovincialis


ABSTRACT: MSP22.8 is a shell matrix protein described in Mytilus galloprovincialis. During the characterization of the monoclonal antibody M22.8, we have demostrated that MSP22.8 is secreted into the extrapallial space by cells of the mantle edge epithelium. The protein is detected in the extrapallial fluid and extrapallial hemocytes and finally becomes part of the shell matrix framework. In order to isolate the protein from the extrapallial fluid, a multi-step purification strategy was designed, involving ammonium sulfate precipitation followed by affinity or size-exclusion chromatography. Eluted fractions were further processed by SDS-PAGE or 2D-PAGE. Positivity of fractions, bands and spots were checked by Western or Dot blot. Positive bands and spots were manually excised and sent for mass spectrometry experiments for protein identification.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mytilus Galloprovincialis (mediterranean Mussel)

SUBMITTER: JUAN CALVO  

LAB HEAD: África González-Fernández

PROVIDER: PXD004706 | Pride | 2017-08-15

REPOSITORIES: Pride

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MSP22.8 is a protease inhibitor-like protein involved in shell mineralization in the edible mussel <i>Mytilus galloprovincialis</i>.

Calvo-Iglesias Juan J   Pérez-Estévez Daniel D   González-Fernández África Á  

FEBS open bio 20170917 10


The mussel shell protein 22.8 (MSP22.8) is recognized by a monoclonal antibody (M22.8) directed against larvae of the mussel <i>Mytilus galloprovincialis</i>. After being secreted by cells of the mantle-edge epithelium into the extrapallial (EP) space (the gap between the mantle and the shell), the protein is detected in the extrapallial fluid (EPF) and EP hemocytes and finally becomes part of the shell matrix framework in adult specimens of <i>M. galloprovincialis</i>. In the work described her  ...[more]

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