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dc.contributor.authorSalah Eldein E.
dc.contributor.authorAbdalla M.
dc.contributor.authorEltayb W.A.
dc.contributor.authorEl-Arabey A.A.
dc.contributor.authorGanash M.
dc.contributor.authorAlshammari F.D.
dc.contributor.authorBarreto G.
dc.contributor.authorAshraf G.M.
dc.date.accessioned2020-09-02T22:27:37Z
dc.date.available2020-09-02T22:27:37Z
dc.date.issued2019
dc.identifier10.1002/jcb.28826
dc.identifier.citation120, 9, 15594-15603
dc.identifier.issn07302312
dc.identifier.urihttps://hdl.handle.net/20.500.12728/6140
dc.descriptionSerine protease (SPs) is one of the immune enzyme's molecules that play a main role in the variation of a physiological process by controlling protease actions in vertebrates. For example, signaling cells, protector and improvement, which are included in melanization, are utilized to cascade with the meddling pathogens and defense the harmed tissue in insects. In this study, we explore the biochemical process of (SP-22) from Bombyx mori. Reverse-transcription polymerase chain reaction (RT-PCR) discloses that BmSP-22 is expressed in all tissues including the fat body. The formative expression profile of BmSP-22 reveal that BmSP-22 messenger RNA is expressed constitutively in larvae. Injection of recombinant BmSP-22 into B. mori larvae reduces significantly the transcript levels of antimicrobial peptides in the fat body. Our results suggest that BmSP-22 plays an important role in the innate immunity of B. mori and possibly in other insects. © 2019 Wiley Periodicals, Inc.
dc.language.isoen
dc.publisherWiley-Liss Inc.
dc.subjectanalysis
dc.subjectBombyx mori
dc.subjectcloning
dc.subjectexpression
dc.subjectserine protease
dc.subjectserine proteinase
dc.subjectserine proteinase 22
dc.subjectunclassified drug
dc.subjectamino acid sequence
dc.subjectanimal tissue
dc.subjectArticle
dc.subjectbiochemistry
dc.subjectBombyx mori
dc.subjectcontrolled study
dc.subjectfat pad
dc.subjectgene expression
dc.subjectgene function
dc.subjectgenetic code
dc.subjectgenetic transcription
dc.subjecthemolymph
dc.subjectlarva
dc.subjectMalpighian tubule
dc.subjectmolecular cloning
dc.subjectnonhuman
dc.subjectopen reading frame
dc.subjectphylogeny
dc.subjectpriority journal
dc.subjectprotein purification
dc.subjectreverse transcription polymerase chain reaction
dc.subjectsequence alignment
dc.subjectstart codon
dc.subjecttissue distribution
dc.subjectWestern blotting
dc.titleMolecular cloning, expression, purification, and functional characterization of SP-22 gene from Bombyx mori
dc.typeArticle


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