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  • 99
    Thermo Fisher superscript vilo cdna synthesis kit
    Superscript Vilo Cdna Synthesis Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 12677 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Thermo Fisher superscrip iii reverse transcription kit
    Superscrip Iii Reverse Transcription Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher superscritpt iii first strand synthesis kit
    Superscritpt Iii First Strand Synthesis Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher superscript kit
    Superscript Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1463 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher superscript preamplification kit
    Alternative splicing of sheep myostatin pre-mRNA and translation of MSV mRNA into protein. (A) A representative Northern blot identified canonical myostatin (Mstn) and MSV mRNAs in poly(A) + <t>RNA</t> isolated from sheep skeletal muscle using a radiolabeled probe complementary to exon 1 2 sequence of sheep myostatin (nt 1–621). (B) Schematic representation of alternative splicing of the myostatin gene. Genomic structure, splicing of canonical myostatin and MSV mRNAs are shown as determined by RT-PCR amplification and sequencing. The sheep myostatin gene has a cryptic third intron sequence (Int 3, 1011 bp) located 21 bp downstream of the intron 2/exon 3 boundary, thereby removing the coding sequence of the canonical mature myostatin protein. Alternate splicing creates a new ORF (966 bp) by appending a novel C-terminal coding sequence (exon 3b, 198 bp) to a truncated propeptide coding sequence of myostatin (exon 1 2 and 3a) in the MSV transcript. Open boxes show 5′ and 3′ untranslated regions, filled boxes represent translated sequences. Also shown are exons (Ex), introns (Int), translation start (ATG) and stop (TGA, TAA) sites, and the size of each transcript. Location of the 11 bp deletion in exon 3 identified in Belgian Blue cattle is also indicated. (C) Tissue-specific mRNA expression of MSV and myostatin was analyzed in biceps femoris (Biceps), quadriceps (Quad.) and semitendinosus (Semit.) muscles, and heart, liver, brain, kidney, testicle, ovary, gut, skin and aorta tissues of <t>three</t> months old sheep using RT-PCR. Actin was used as a positive control for each tissue sample. NTC is a no template PCR control. (D) Multiple polypeptide sequence alignment of the predicted C-terminus of MSV in sheep, cattle, pig and dolphin. A consensus proteolytic cleavage site [(K/R)-(X) n -(K/R)↓ where n = 0, 2, 4, 6 and X is any amino acid except cysteine at aa 271–274] has been identified for precursor convertases. A dotted line indicates the location of the putative cleavage site. The scale shows the positions of the amino acid residues in the MSV polypeptide sequence. The unshaded background highlights residues that are different from the consensus sequence. An in-silico predicted secondary structure of mature sheep MSV is also shown. (E) Schematic representation of the known and proposed proteolytic processing of canonical myostatin and MSV precursors, respectively. The location of the secretion signal peptide and the C-terminal cleavage sites are indicated. Grey filling shows the novel C-terminus of the MSV precursor. Black bars denote the location of polypeptide sequences used to raise MSV-specific polyclonal antibodies (MSVab and MSVab65). (F) Detection of MSV-immunoreactive proteins in semitendinosus muscles of sheep and cattle and its absence in gastrocnemius muscles of mouse and rat (20 µg of total protein per lane) using an anti-MSVab in Western immunoblotting. Recombinant peptide (Recomb.) corresponds to a polypeptide for the C-terminal 65 amino acids (11.9 kDa) of sheep MSV. Molecular weights of a protein marker are also indicated.
    Superscript Preamplification Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 239 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher iii kit
    Alternative splicing of sheep myostatin pre-mRNA and translation of MSV mRNA into protein. (A) A representative Northern blot identified canonical myostatin (Mstn) and MSV mRNAs in poly(A) + <t>RNA</t> isolated from sheep skeletal muscle using a radiolabeled probe complementary to exon 1 2 sequence of sheep myostatin (nt 1–621). (B) Schematic representation of alternative splicing of the myostatin gene. Genomic structure, splicing of canonical myostatin and MSV mRNAs are shown as determined by RT-PCR amplification and sequencing. The sheep myostatin gene has a cryptic third intron sequence (Int 3, 1011 bp) located 21 bp downstream of the intron 2/exon 3 boundary, thereby removing the coding sequence of the canonical mature myostatin protein. Alternate splicing creates a new ORF (966 bp) by appending a novel C-terminal coding sequence (exon 3b, 198 bp) to a truncated propeptide coding sequence of myostatin (exon 1 2 and 3a) in the MSV transcript. Open boxes show 5′ and 3′ untranslated regions, filled boxes represent translated sequences. Also shown are exons (Ex), introns (Int), translation start (ATG) and stop (TGA, TAA) sites, and the size of each transcript. Location of the 11 bp deletion in exon 3 identified in Belgian Blue cattle is also indicated. (C) Tissue-specific mRNA expression of MSV and myostatin was analyzed in biceps femoris (Biceps), quadriceps (Quad.) and semitendinosus (Semit.) muscles, and heart, liver, brain, kidney, testicle, ovary, gut, skin and aorta tissues of <t>three</t> months old sheep using RT-PCR. Actin was used as a positive control for each tissue sample. NTC is a no template PCR control. (D) Multiple polypeptide sequence alignment of the predicted C-terminus of MSV in sheep, cattle, pig and dolphin. A consensus proteolytic cleavage site [(K/R)-(X) n -(K/R)↓ where n = 0, 2, 4, 6 and X is any amino acid except cysteine at aa 271–274] has been identified for precursor convertases. A dotted line indicates the location of the putative cleavage site. The scale shows the positions of the amino acid residues in the MSV polypeptide sequence. The unshaded background highlights residues that are different from the consensus sequence. An in-silico predicted secondary structure of mature sheep MSV is also shown. (E) Schematic representation of the known and proposed proteolytic processing of canonical myostatin and MSV precursors, respectively. The location of the secretion signal peptide and the C-terminal cleavage sites are indicated. Grey filling shows the novel C-terminus of the MSV precursor. Black bars denote the location of polypeptide sequences used to raise MSV-specific polyclonal antibodies (MSVab and MSVab65). (F) Detection of MSV-immunoreactive proteins in semitendinosus muscles of sheep and cattle and its absence in gastrocnemius muscles of mouse and rat (20 µg of total protein per lane) using an anti-MSVab in Western immunoblotting. Recombinant peptide (Recomb.) corresponds to a polypeptide for the C-terminal 65 amino acids (11.9 kDa) of sheep MSV. Molecular weights of a protein marker are also indicated.
    Iii Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 194 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher custom superscript kit
    Alternative splicing of sheep myostatin pre-mRNA and translation of MSV mRNA into protein. (A) A representative Northern blot identified canonical myostatin (Mstn) and MSV mRNAs in poly(A) + <t>RNA</t> isolated from sheep skeletal muscle using a radiolabeled probe complementary to exon 1 2 sequence of sheep myostatin (nt 1–621). (B) Schematic representation of alternative splicing of the myostatin gene. Genomic structure, splicing of canonical myostatin and MSV mRNAs are shown as determined by RT-PCR amplification and sequencing. The sheep myostatin gene has a cryptic third intron sequence (Int 3, 1011 bp) located 21 bp downstream of the intron 2/exon 3 boundary, thereby removing the coding sequence of the canonical mature myostatin protein. Alternate splicing creates a new ORF (966 bp) by appending a novel C-terminal coding sequence (exon 3b, 198 bp) to a truncated propeptide coding sequence of myostatin (exon 1 2 and 3a) in the MSV transcript. Open boxes show 5′ and 3′ untranslated regions, filled boxes represent translated sequences. Also shown are exons (Ex), introns (Int), translation start (ATG) and stop (TGA, TAA) sites, and the size of each transcript. Location of the 11 bp deletion in exon 3 identified in Belgian Blue cattle is also indicated. (C) Tissue-specific mRNA expression of MSV and myostatin was analyzed in biceps femoris (Biceps), quadriceps (Quad.) and semitendinosus (Semit.) muscles, and heart, liver, brain, kidney, testicle, ovary, gut, skin and aorta tissues of <t>three</t> months old sheep using RT-PCR. Actin was used as a positive control for each tissue sample. NTC is a no template PCR control. (D) Multiple polypeptide sequence alignment of the predicted C-terminus of MSV in sheep, cattle, pig and dolphin. A consensus proteolytic cleavage site [(K/R)-(X) n -(K/R)↓ where n = 0, 2, 4, 6 and X is any amino acid except cysteine at aa 271–274] has been identified for precursor convertases. A dotted line indicates the location of the putative cleavage site. The scale shows the positions of the amino acid residues in the MSV polypeptide sequence. The unshaded background highlights residues that are different from the consensus sequence. An in-silico predicted secondary structure of mature sheep MSV is also shown. (E) Schematic representation of the known and proposed proteolytic processing of canonical myostatin and MSV precursors, respectively. The location of the secretion signal peptide and the C-terminal cleavage sites are indicated. Grey filling shows the novel C-terminus of the MSV precursor. Black bars denote the location of polypeptide sequences used to raise MSV-specific polyclonal antibodies (MSVab and MSVab65). (F) Detection of MSV-immunoreactive proteins in semitendinosus muscles of sheep and cattle and its absence in gastrocnemius muscles of mouse and rat (20 µg of total protein per lane) using an anti-MSVab in Western immunoblotting. Recombinant peptide (Recomb.) corresponds to a polypeptide for the C-terminal 65 amino acids (11.9 kDa) of sheep MSV. Molecular weights of a protein marker are also indicated.
    Custom Superscript Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher vilo kit
    Alternative splicing of sheep myostatin pre-mRNA and translation of MSV mRNA into protein. (A) A representative Northern blot identified canonical myostatin (Mstn) and MSV mRNAs in poly(A) + <t>RNA</t> isolated from sheep skeletal muscle using a radiolabeled probe complementary to exon 1 2 sequence of sheep myostatin (nt 1–621). (B) Schematic representation of alternative splicing of the myostatin gene. Genomic structure, splicing of canonical myostatin and MSV mRNAs are shown as determined by RT-PCR amplification and sequencing. The sheep myostatin gene has a cryptic third intron sequence (Int 3, 1011 bp) located 21 bp downstream of the intron 2/exon 3 boundary, thereby removing the coding sequence of the canonical mature myostatin protein. Alternate splicing creates a new ORF (966 bp) by appending a novel C-terminal coding sequence (exon 3b, 198 bp) to a truncated propeptide coding sequence of myostatin (exon 1 2 and 3a) in the MSV transcript. Open boxes show 5′ and 3′ untranslated regions, filled boxes represent translated sequences. Also shown are exons (Ex), introns (Int), translation start (ATG) and stop (TGA, TAA) sites, and the size of each transcript. Location of the 11 bp deletion in exon 3 identified in Belgian Blue cattle is also indicated. (C) Tissue-specific mRNA expression of MSV and myostatin was analyzed in biceps femoris (Biceps), quadriceps (Quad.) and semitendinosus (Semit.) muscles, and heart, liver, brain, kidney, testicle, ovary, gut, skin and aorta tissues of <t>three</t> months old sheep using RT-PCR. Actin was used as a positive control for each tissue sample. NTC is a no template PCR control. (D) Multiple polypeptide sequence alignment of the predicted C-terminus of MSV in sheep, cattle, pig and dolphin. A consensus proteolytic cleavage site [(K/R)-(X) n -(K/R)↓ where n = 0, 2, 4, 6 and X is any amino acid except cysteine at aa 271–274] has been identified for precursor convertases. A dotted line indicates the location of the putative cleavage site. The scale shows the positions of the amino acid residues in the MSV polypeptide sequence. The unshaded background highlights residues that are different from the consensus sequence. An in-silico predicted secondary structure of mature sheep MSV is also shown. (E) Schematic representation of the known and proposed proteolytic processing of canonical myostatin and MSV precursors, respectively. The location of the secretion signal peptide and the C-terminal cleavage sites are indicated. Grey filling shows the novel C-terminus of the MSV precursor. Black bars denote the location of polypeptide sequences used to raise MSV-specific polyclonal antibodies (MSVab and MSVab65). (F) Detection of MSV-immunoreactive proteins in semitendinosus muscles of sheep and cattle and its absence in gastrocnemius muscles of mouse and rat (20 µg of total protein per lane) using an anti-MSVab in Western immunoblotting. Recombinant peptide (Recomb.) corresponds to a polypeptide for the C-terminal 65 amino acids (11.9 kDa) of sheep MSV. Molecular weights of a protein marker are also indicated.
    Vilo Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 257 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher superscrippt iii first strand synthesis super mix kit
    Alternative splicing of sheep myostatin pre-mRNA and translation of MSV mRNA into protein. (A) A representative Northern blot identified canonical myostatin (Mstn) and MSV mRNAs in poly(A) + <t>RNA</t> isolated from sheep skeletal muscle using a radiolabeled probe complementary to exon 1 2 sequence of sheep myostatin (nt 1–621). (B) Schematic representation of alternative splicing of the myostatin gene. Genomic structure, splicing of canonical myostatin and MSV mRNAs are shown as determined by RT-PCR amplification and sequencing. The sheep myostatin gene has a cryptic third intron sequence (Int 3, 1011 bp) located 21 bp downstream of the intron 2/exon 3 boundary, thereby removing the coding sequence of the canonical mature myostatin protein. Alternate splicing creates a new ORF (966 bp) by appending a novel C-terminal coding sequence (exon 3b, 198 bp) to a truncated propeptide coding sequence of myostatin (exon 1 2 and 3a) in the MSV transcript. Open boxes show 5′ and 3′ untranslated regions, filled boxes represent translated sequences. Also shown are exons (Ex), introns (Int), translation start (ATG) and stop (TGA, TAA) sites, and the size of each transcript. Location of the 11 bp deletion in exon 3 identified in Belgian Blue cattle is also indicated. (C) Tissue-specific mRNA expression of MSV and myostatin was analyzed in biceps femoris (Biceps), quadriceps (Quad.) and semitendinosus (Semit.) muscles, and heart, liver, brain, kidney, testicle, ovary, gut, skin and aorta tissues of <t>three</t> months old sheep using RT-PCR. Actin was used as a positive control for each tissue sample. NTC is a no template PCR control. (D) Multiple polypeptide sequence alignment of the predicted C-terminus of MSV in sheep, cattle, pig and dolphin. A consensus proteolytic cleavage site [(K/R)-(X) n -(K/R)↓ where n = 0, 2, 4, 6 and X is any amino acid except cysteine at aa 271–274] has been identified for precursor convertases. A dotted line indicates the location of the putative cleavage site. The scale shows the positions of the amino acid residues in the MSV polypeptide sequence. The unshaded background highlights residues that are different from the consensus sequence. An in-silico predicted secondary structure of mature sheep MSV is also shown. (E) Schematic representation of the known and proposed proteolytic processing of canonical myostatin and MSV precursors, respectively. The location of the secretion signal peptide and the C-terminal cleavage sites are indicated. Grey filling shows the novel C-terminus of the MSV precursor. Black bars denote the location of polypeptide sequences used to raise MSV-specific polyclonal antibodies (MSVab and MSVab65). (F) Detection of MSV-immunoreactive proteins in semitendinosus muscles of sheep and cattle and its absence in gastrocnemius muscles of mouse and rat (20 µg of total protein per lane) using an anti-MSVab in Western immunoblotting. Recombinant peptide (Recomb.) corresponds to a polypeptide for the C-terminal 65 amino acids (11.9 kDa) of sheep MSV. Molecular weights of a protein marker are also indicated.
    Superscrippt Iii First Strand Synthesis Super Mix Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 83/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher superscript ii rt kit
    Alternative splicing of sheep myostatin pre-mRNA and translation of MSV mRNA into protein. (A) A representative Northern blot identified canonical myostatin (Mstn) and MSV mRNAs in poly(A) + <t>RNA</t> isolated from sheep skeletal muscle using a radiolabeled probe complementary to exon 1 2 sequence of sheep myostatin (nt 1–621). (B) Schematic representation of alternative splicing of the myostatin gene. Genomic structure, splicing of canonical myostatin and MSV mRNAs are shown as determined by RT-PCR amplification and sequencing. The sheep myostatin gene has a cryptic third intron sequence (Int 3, 1011 bp) located 21 bp downstream of the intron 2/exon 3 boundary, thereby removing the coding sequence of the canonical mature myostatin protein. Alternate splicing creates a new ORF (966 bp) by appending a novel C-terminal coding sequence (exon 3b, 198 bp) to a truncated propeptide coding sequence of myostatin (exon 1 2 and 3a) in the MSV transcript. Open boxes show 5′ and 3′ untranslated regions, filled boxes represent translated sequences. Also shown are exons (Ex), introns (Int), translation start (ATG) and stop (TGA, TAA) sites, and the size of each transcript. Location of the 11 bp deletion in exon 3 identified in Belgian Blue cattle is also indicated. (C) Tissue-specific mRNA expression of MSV and myostatin was analyzed in biceps femoris (Biceps), quadriceps (Quad.) and semitendinosus (Semit.) muscles, and heart, liver, brain, kidney, testicle, ovary, gut, skin and aorta tissues of <t>three</t> months old sheep using RT-PCR. Actin was used as a positive control for each tissue sample. NTC is a no template PCR control. (D) Multiple polypeptide sequence alignment of the predicted C-terminus of MSV in sheep, cattle, pig and dolphin. A consensus proteolytic cleavage site [(K/R)-(X) n -(K/R)↓ where n = 0, 2, 4, 6 and X is any amino acid except cysteine at aa 271–274] has been identified for precursor convertases. A dotted line indicates the location of the putative cleavage site. The scale shows the positions of the amino acid residues in the MSV polypeptide sequence. The unshaded background highlights residues that are different from the consensus sequence. An in-silico predicted secondary structure of mature sheep MSV is also shown. (E) Schematic representation of the known and proposed proteolytic processing of canonical myostatin and MSV precursors, respectively. The location of the secretion signal peptide and the C-terminal cleavage sites are indicated. Grey filling shows the novel C-terminus of the MSV precursor. Black bars denote the location of polypeptide sequences used to raise MSV-specific polyclonal antibodies (MSVab and MSVab65). (F) Detection of MSV-immunoreactive proteins in semitendinosus muscles of sheep and cattle and its absence in gastrocnemius muscles of mouse and rat (20 µg of total protein per lane) using an anti-MSVab in Western immunoblotting. Recombinant peptide (Recomb.) corresponds to a polypeptide for the C-terminal 65 amino acids (11.9 kDa) of sheep MSV. Molecular weights of a protein marker are also indicated.
    Superscript Ii Rt Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1058 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher superscript first strand synthesis kit
    Alternative splicing of sheep myostatin pre-mRNA and translation of MSV mRNA into protein. (A) A representative Northern blot identified canonical myostatin (Mstn) and MSV mRNAs in poly(A) + <t>RNA</t> isolated from sheep skeletal muscle using a radiolabeled probe complementary to exon 1 2 sequence of sheep myostatin (nt 1–621). (B) Schematic representation of alternative splicing of the myostatin gene. Genomic structure, splicing of canonical myostatin and MSV mRNAs are shown as determined by RT-PCR amplification and sequencing. The sheep myostatin gene has a cryptic third intron sequence (Int 3, 1011 bp) located 21 bp downstream of the intron 2/exon 3 boundary, thereby removing the coding sequence of the canonical mature myostatin protein. Alternate splicing creates a new ORF (966 bp) by appending a novel C-terminal coding sequence (exon 3b, 198 bp) to a truncated propeptide coding sequence of myostatin (exon 1 2 and 3a) in the MSV transcript. Open boxes show 5′ and 3′ untranslated regions, filled boxes represent translated sequences. Also shown are exons (Ex), introns (Int), translation start (ATG) and stop (TGA, TAA) sites, and the size of each transcript. Location of the 11 bp deletion in exon 3 identified in Belgian Blue cattle is also indicated. (C) Tissue-specific mRNA expression of MSV and myostatin was analyzed in biceps femoris (Biceps), quadriceps (Quad.) and semitendinosus (Semit.) muscles, and heart, liver, brain, kidney, testicle, ovary, gut, skin and aorta tissues of <t>three</t> months old sheep using RT-PCR. Actin was used as a positive control for each tissue sample. NTC is a no template PCR control. (D) Multiple polypeptide sequence alignment of the predicted C-terminus of MSV in sheep, cattle, pig and dolphin. A consensus proteolytic cleavage site [(K/R)-(X) n -(K/R)↓ where n = 0, 2, 4, 6 and X is any amino acid except cysteine at aa 271–274] has been identified for precursor convertases. A dotted line indicates the location of the putative cleavage site. The scale shows the positions of the amino acid residues in the MSV polypeptide sequence. The unshaded background highlights residues that are different from the consensus sequence. An in-silico predicted secondary structure of mature sheep MSV is also shown. (E) Schematic representation of the known and proposed proteolytic processing of canonical myostatin and MSV precursors, respectively. The location of the secretion signal peptide and the C-terminal cleavage sites are indicated. Grey filling shows the novel C-terminus of the MSV precursor. Black bars denote the location of polypeptide sequences used to raise MSV-specific polyclonal antibodies (MSVab and MSVab65). (F) Detection of MSV-immunoreactive proteins in semitendinosus muscles of sheep and cattle and its absence in gastrocnemius muscles of mouse and rat (20 µg of total protein per lane) using an anti-MSVab in Western immunoblotting. Recombinant peptide (Recomb.) corresponds to a polypeptide for the C-terminal 65 amino acids (11.9 kDa) of sheep MSV. Molecular weights of a protein marker are also indicated.
    Superscript First Strand Synthesis Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2765 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher superscript preamplification system kit
    Alternative splicing of sheep myostatin pre-mRNA and translation of MSV mRNA into protein. (A) A representative Northern blot identified canonical myostatin (Mstn) and MSV mRNAs in poly(A) + <t>RNA</t> isolated from sheep skeletal muscle using a radiolabeled probe complementary to exon 1 2 sequence of sheep myostatin (nt 1–621). (B) Schematic representation of alternative splicing of the myostatin gene. Genomic structure, splicing of canonical myostatin and MSV mRNAs are shown as determined by RT-PCR amplification and sequencing. The sheep myostatin gene has a cryptic third intron sequence (Int 3, 1011 bp) located 21 bp downstream of the intron 2/exon 3 boundary, thereby removing the coding sequence of the canonical mature myostatin protein. Alternate splicing creates a new ORF (966 bp) by appending a novel C-terminal coding sequence (exon 3b, 198 bp) to a truncated propeptide coding sequence of myostatin (exon 1 2 and 3a) in the MSV transcript. Open boxes show 5′ and 3′ untranslated regions, filled boxes represent translated sequences. Also shown are exons (Ex), introns (Int), translation start (ATG) and stop (TGA, TAA) sites, and the size of each transcript. Location of the 11 bp deletion in exon 3 identified in Belgian Blue cattle is also indicated. (C) Tissue-specific mRNA expression of MSV and myostatin was analyzed in biceps femoris (Biceps), quadriceps (Quad.) and semitendinosus (Semit.) muscles, and heart, liver, brain, kidney, testicle, ovary, gut, skin and aorta tissues of <t>three</t> months old sheep using RT-PCR. Actin was used as a positive control for each tissue sample. NTC is a no template PCR control. (D) Multiple polypeptide sequence alignment of the predicted C-terminus of MSV in sheep, cattle, pig and dolphin. A consensus proteolytic cleavage site [(K/R)-(X) n -(K/R)↓ where n = 0, 2, 4, 6 and X is any amino acid except cysteine at aa 271–274] has been identified for precursor convertases. A dotted line indicates the location of the putative cleavage site. The scale shows the positions of the amino acid residues in the MSV polypeptide sequence. The unshaded background highlights residues that are different from the consensus sequence. An in-silico predicted secondary structure of mature sheep MSV is also shown. (E) Schematic representation of the known and proposed proteolytic processing of canonical myostatin and MSV precursors, respectively. The location of the secretion signal peptide and the C-terminal cleavage sites are indicated. Grey filling shows the novel C-terminus of the MSV precursor. Black bars denote the location of polypeptide sequences used to raise MSV-specific polyclonal antibodies (MSVab and MSVab65). (F) Detection of MSV-immunoreactive proteins in semitendinosus muscles of sheep and cattle and its absence in gastrocnemius muscles of mouse and rat (20 µg of total protein per lane) using an anti-MSVab in Western immunoblotting. Recombinant peptide (Recomb.) corresponds to a polypeptide for the C-terminal 65 amino acids (11.9 kDa) of sheep MSV. Molecular weights of a protein marker are also indicated.
    Superscript Preamplification System Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 87/100, based on 71 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher superscript reverse transcriptase kit
    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
    Superscript Reverse Transcriptase Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1230 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for <t>RNA</t> sequencing. Hofstenia miamia were injected once a day for <t>three</t> consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.
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    Image Search Results


    Alternative splicing of sheep myostatin pre-mRNA and translation of MSV mRNA into protein. (A) A representative Northern blot identified canonical myostatin (Mstn) and MSV mRNAs in poly(A) + RNA isolated from sheep skeletal muscle using a radiolabeled probe complementary to exon 1 2 sequence of sheep myostatin (nt 1–621). (B) Schematic representation of alternative splicing of the myostatin gene. Genomic structure, splicing of canonical myostatin and MSV mRNAs are shown as determined by RT-PCR amplification and sequencing. The sheep myostatin gene has a cryptic third intron sequence (Int 3, 1011 bp) located 21 bp downstream of the intron 2/exon 3 boundary, thereby removing the coding sequence of the canonical mature myostatin protein. Alternate splicing creates a new ORF (966 bp) by appending a novel C-terminal coding sequence (exon 3b, 198 bp) to a truncated propeptide coding sequence of myostatin (exon 1 2 and 3a) in the MSV transcript. Open boxes show 5′ and 3′ untranslated regions, filled boxes represent translated sequences. Also shown are exons (Ex), introns (Int), translation start (ATG) and stop (TGA, TAA) sites, and the size of each transcript. Location of the 11 bp deletion in exon 3 identified in Belgian Blue cattle is also indicated. (C) Tissue-specific mRNA expression of MSV and myostatin was analyzed in biceps femoris (Biceps), quadriceps (Quad.) and semitendinosus (Semit.) muscles, and heart, liver, brain, kidney, testicle, ovary, gut, skin and aorta tissues of three months old sheep using RT-PCR. Actin was used as a positive control for each tissue sample. NTC is a no template PCR control. (D) Multiple polypeptide sequence alignment of the predicted C-terminus of MSV in sheep, cattle, pig and dolphin. A consensus proteolytic cleavage site [(K/R)-(X) n -(K/R)↓ where n = 0, 2, 4, 6 and X is any amino acid except cysteine at aa 271–274] has been identified for precursor convertases. A dotted line indicates the location of the putative cleavage site. The scale shows the positions of the amino acid residues in the MSV polypeptide sequence. The unshaded background highlights residues that are different from the consensus sequence. An in-silico predicted secondary structure of mature sheep MSV is also shown. (E) Schematic representation of the known and proposed proteolytic processing of canonical myostatin and MSV precursors, respectively. The location of the secretion signal peptide and the C-terminal cleavage sites are indicated. Grey filling shows the novel C-terminus of the MSV precursor. Black bars denote the location of polypeptide sequences used to raise MSV-specific polyclonal antibodies (MSVab and MSVab65). (F) Detection of MSV-immunoreactive proteins in semitendinosus muscles of sheep and cattle and its absence in gastrocnemius muscles of mouse and rat (20 µg of total protein per lane) using an anti-MSVab in Western immunoblotting. Recombinant peptide (Recomb.) corresponds to a polypeptide for the C-terminal 65 amino acids (11.9 kDa) of sheep MSV. Molecular weights of a protein marker are also indicated.

    Journal: PLoS ONE

    Article Title: Discovery of a Mammalian Splice Variant of Myostatin That Stimulates Myogenesis

    doi: 10.1371/journal.pone.0081713

    Figure Lengend Snippet: Alternative splicing of sheep myostatin pre-mRNA and translation of MSV mRNA into protein. (A) A representative Northern blot identified canonical myostatin (Mstn) and MSV mRNAs in poly(A) + RNA isolated from sheep skeletal muscle using a radiolabeled probe complementary to exon 1 2 sequence of sheep myostatin (nt 1–621). (B) Schematic representation of alternative splicing of the myostatin gene. Genomic structure, splicing of canonical myostatin and MSV mRNAs are shown as determined by RT-PCR amplification and sequencing. The sheep myostatin gene has a cryptic third intron sequence (Int 3, 1011 bp) located 21 bp downstream of the intron 2/exon 3 boundary, thereby removing the coding sequence of the canonical mature myostatin protein. Alternate splicing creates a new ORF (966 bp) by appending a novel C-terminal coding sequence (exon 3b, 198 bp) to a truncated propeptide coding sequence of myostatin (exon 1 2 and 3a) in the MSV transcript. Open boxes show 5′ and 3′ untranslated regions, filled boxes represent translated sequences. Also shown are exons (Ex), introns (Int), translation start (ATG) and stop (TGA, TAA) sites, and the size of each transcript. Location of the 11 bp deletion in exon 3 identified in Belgian Blue cattle is also indicated. (C) Tissue-specific mRNA expression of MSV and myostatin was analyzed in biceps femoris (Biceps), quadriceps (Quad.) and semitendinosus (Semit.) muscles, and heart, liver, brain, kidney, testicle, ovary, gut, skin and aorta tissues of three months old sheep using RT-PCR. Actin was used as a positive control for each tissue sample. NTC is a no template PCR control. (D) Multiple polypeptide sequence alignment of the predicted C-terminus of MSV in sheep, cattle, pig and dolphin. A consensus proteolytic cleavage site [(K/R)-(X) n -(K/R)↓ where n = 0, 2, 4, 6 and X is any amino acid except cysteine at aa 271–274] has been identified for precursor convertases. A dotted line indicates the location of the putative cleavage site. The scale shows the positions of the amino acid residues in the MSV polypeptide sequence. The unshaded background highlights residues that are different from the consensus sequence. An in-silico predicted secondary structure of mature sheep MSV is also shown. (E) Schematic representation of the known and proposed proteolytic processing of canonical myostatin and MSV precursors, respectively. The location of the secretion signal peptide and the C-terminal cleavage sites are indicated. Grey filling shows the novel C-terminus of the MSV precursor. Black bars denote the location of polypeptide sequences used to raise MSV-specific polyclonal antibodies (MSVab and MSVab65). (F) Detection of MSV-immunoreactive proteins in semitendinosus muscles of sheep and cattle and its absence in gastrocnemius muscles of mouse and rat (20 µg of total protein per lane) using an anti-MSVab in Western immunoblotting. Recombinant peptide (Recomb.) corresponds to a polypeptide for the C-terminal 65 amino acids (11.9 kDa) of sheep MSV. Molecular weights of a protein marker are also indicated.

    Article Snippet: Quantitative and Non-quantitative RT-PCR Total RNA was extracted from cultured cells, skeletal muscles, heart, liver, brain, kidneys, testes, ovaries, gut, skin and aorta using Trizol reagent (Invitrogen) and 5 µg of total RNA was reverse transcribed into cDNA using the Superscript III Pre-Amplification kit (Invitrogen) according to the manufacturer's instructions.

    Techniques: Northern Blot, Isolation, Sequencing, Reverse Transcription Polymerase Chain Reaction, Amplification, Expressing, Positive Control, Polymerase Chain Reaction, In Silico, Western Blot, Recombinant, Marker

    A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for RNA sequencing. Hofstenia miamia were injected once a day for three consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.

    Journal: PLoS Genetics

    Article Title: A small set of conserved genes, including sp5 and Hox, are activated by Wnt signaling in the posterior of planarians and acoels

    doi: 10.1371/journal.pgen.1008401

    Figure Lengend Snippet: A posterior program of gene expression is down-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for RNA sequencing. Hofstenia miamia were injected once a day for three consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) A cluster of 66 genes is down-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as z-scores for indicated timepoints post first RNAi injection. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Left: Validation of β-catenin-1 RNAi-dependent down-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Right: Genes down-regulated after β-catenin-1 RNAi are expressed in the posterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. Scale bars, 200μm.

    Article Snippet: 1μg RNA input was used to prepare cDNA with the SuperScript III Reverse Transcriptase kit (Invitrogen).

    Techniques: Expressing, Inhibition, RNA Sequencing Assay, Injection, Fluorescence In Situ Hybridization

    An anterior program of gene expression is up-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for RNA sequencing. Hofstenia miamia were injected once a day for three consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) 92 genes are up-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as a z-score for indicated time-points post-RNAi initiation. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Top: Validation of β-catenin-1 RNAi dependent up-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Bottom: Genes up-regulated after β-catenin-1 RNAi are expressed in the anterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. All scale bars, 200μm.

    Journal: PLoS Genetics

    Article Title: A small set of conserved genes, including sp5 and Hox, are activated by Wnt signaling in the posterior of planarians and acoels

    doi: 10.1371/journal.pgen.1008401

    Figure Lengend Snippet: An anterior program of gene expression is up-regulated after β-catenin-1 inhibition in acoels. (A) Experimental scheme for RNA sequencing. Hofstenia miamia were injected once a day for three consecutive days with control or β-catenin-1 dsRNA. Tails were collected in trizol at 3, 7, and 14 days after the first injection for RNA sequencing. Red box indicates tissue collected. (B) 92 genes are up-regulated early after β-catenin-1 RNAi. Heatmap displaying gene expression counts as a z-score for indicated time-points post-RNAi initiation. *indicates annotation by best BLAST hit. Gene list provided in S5 Table . (C) Top: Validation of β-catenin-1 RNAi dependent up-regulation of gene expression. FISH for indicated transcripts at day 9 post-RNAi initiation in homeostasis. Images are presented in grayscale with color inverted. Bottom: Genes up-regulated after β-catenin-1 RNAi are expressed in the anterior. FISH for indicated transcripts in two week old hatchlings. Transcript ID provided in parentheses. Images are presented in grayscale with color inverted. All scale bars, 200μm.

    Article Snippet: 1μg RNA input was used to prepare cDNA with the SuperScript III Reverse Transcriptase kit (Invitrogen).

    Techniques: Expressing, Inhibition, RNA Sequencing Assay, Injection, Fluorescence In Situ Hybridization