cdna encoding human c-src wt puseamp cmv-based vector (Upstate Biotechnology Inc)
90
Structured Review
Upstate Biotechnology Inc
cdna encoding human c-src wt puseamp cmv-based vector
Cdna Encoding Human C Src Wt Puseamp Cmv Based Vector, supplied by Upstate Biotechnology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cdna+encoding+human+c-src+wt+puseamp+cmv-based+vector/cdna+encoding+human+c+src+wt+puseamp+cmv+based+vector/pm11724572-66-8-14
Average 90 stars, based on 1 article reviews
Cdna Encoding Human C Src Wt Puseamp Cmv Based Vector, supplied by Upstate Biotechnology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cdna+encoding+human+c-src+wt+puseamp+cmv-based+vector/cdna+encoding+human+c+src+wt+puseamp+cmv+based+vector/pm11724572-66-8-14
Average 90 stars, based on 1 article reviews
cdna encoding human c-src wt puseamp cmv-based vector - by Bioz Stars,
2026-10
90/100 stars
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Plasmid Preparation:Article Title: Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins. Article Snippet: â-Dystroglycan is a ubiquitously expressed integral membrane protein that undergoes tyrosine phosphorylation in an adhesion-dependent manner.. However, it remains unknown whether tyrosinephosphorylated â-dystroglycan interacts with SH2 domain containing proteins.. Here, we show that the tyrosine phosphorylation of â-dystroglycan is constitutively elevated in v-Src transformed cells. Expressing:Article Title: Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins. Article Snippet: â-Dystroglycan is a ubiquitously expressed integral membrane protein that undergoes tyrosine phosphorylation in an adhesion-dependent manner.. However, it remains unknown whether tyrosinephosphorylated â-dystroglycan interacts with SH2 domain containing proteins.. Here, we show that the tyrosine phosphorylation of â-dystroglycan is constitutively elevated in v-Src transformed cells. |