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Routledge Ltd york 334 54 derkzen p
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msirt3l 54 334  (Danaher Inc)


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    Danaher Inc msirt3l 54 334
    Msirt3l 54 334, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    msirt3 l 54 334  (GE Healthcare)


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    GE Healthcare msirt3 l 54 334
    The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long <t>mSIRT3.</t> The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.
    Msirt3 L 54 334, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3"

    Article Title: Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3

    Journal: Protein Science : A Publication of the Protein Society

    doi: 10.1002/pro.50

    The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long mSIRT3. The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.
    Figure Legend Snippet: The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long mSIRT3. The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.

    Techniques Used: Sequencing, Labeling, Generated, Activity Assay

    Long mSIRT3 localizes to mitochondria. (A) Schematic drawing of SIRT3 constructs. mSIRT3L-1-334 begins at the most N-terminal Met, mSIRT3L-15-334 starts at the second Met, and mSIRT3L-78-334 represents the short mSIRT3 previously believed to be the full-length protein. (B) Mouse embryonic fibroblasts were transfected with C-terminal FLAG-tagged SIRT3 constructs and stained with both anti-FLAG (green) antibody to detect over-expressed mSIRT3 and anti-cytochrome c (red) to label mitochondria. Data are representative of three independent experiments. (C) Cell fractionation of MEFs transfected with either empty vector or plasmids shown in A. mSIRT3L-1-334 and mSIRT3L-15-334 are found predominantly in the mitochondrial fraction, whereas mSIRT3L-78-334 is distributed throughout both cytosolic and mitochondrial fractions. Arrows point out the mSIRT3 protein bands that are discussed in the text.
    Figure Legend Snippet: Long mSIRT3 localizes to mitochondria. (A) Schematic drawing of SIRT3 constructs. mSIRT3L-1-334 begins at the most N-terminal Met, mSIRT3L-15-334 starts at the second Met, and mSIRT3L-78-334 represents the short mSIRT3 previously believed to be the full-length protein. (B) Mouse embryonic fibroblasts were transfected with C-terminal FLAG-tagged SIRT3 constructs and stained with both anti-FLAG (green) antibody to detect over-expressed mSIRT3 and anti-cytochrome c (red) to label mitochondria. Data are representative of three independent experiments. (C) Cell fractionation of MEFs transfected with either empty vector or plasmids shown in A. mSIRT3L-1-334 and mSIRT3L-15-334 are found predominantly in the mitochondrial fraction, whereas mSIRT3L-78-334 is distributed throughout both cytosolic and mitochondrial fractions. Arrows point out the mSIRT3 protein bands that are discussed in the text.

    Techniques Used: Construct, Transfection, Staining, Cell Fractionation, Plasmid Preparation

    msirt3 l 54 334  (GE Healthcare)


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    GE Healthcare msirt3 l 54 334
    The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long <t>mSIRT3.</t> The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.
    Msirt3 L 54 334, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3"

    Article Title: Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3

    Journal: Protein Science : A Publication of the Protein Society

    doi: 10.1002/pro.50

    The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long mSIRT3. The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.
    Figure Legend Snippet: The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long mSIRT3. The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.

    Techniques Used: Sequencing, Labeling, Generated, Activity Assay

    Long mSIRT3 localizes to mitochondria. (A) Schematic drawing of SIRT3 constructs. mSIRT3L-1-334 begins at the most N-terminal Met, mSIRT3L-15-334 starts at the second Met, and mSIRT3L-78-334 represents the short mSIRT3 previously believed to be the full-length protein. (B) Mouse embryonic fibroblasts were transfected with C-terminal FLAG-tagged SIRT3 constructs and stained with both anti-FLAG (green) antibody to detect over-expressed mSIRT3 and anti-cytochrome c (red) to label mitochondria. Data are representative of three independent experiments. (C) Cell fractionation of MEFs transfected with either empty vector or plasmids shown in A. mSIRT3L-1-334 and mSIRT3L-15-334 are found predominantly in the mitochondrial fraction, whereas mSIRT3L-78-334 is distributed throughout both cytosolic and mitochondrial fractions. Arrows point out the mSIRT3 protein bands that are discussed in the text.
    Figure Legend Snippet: Long mSIRT3 localizes to mitochondria. (A) Schematic drawing of SIRT3 constructs. mSIRT3L-1-334 begins at the most N-terminal Met, mSIRT3L-15-334 starts at the second Met, and mSIRT3L-78-334 represents the short mSIRT3 previously believed to be the full-length protein. (B) Mouse embryonic fibroblasts were transfected with C-terminal FLAG-tagged SIRT3 constructs and stained with both anti-FLAG (green) antibody to detect over-expressed mSIRT3 and anti-cytochrome c (red) to label mitochondria. Data are representative of three independent experiments. (C) Cell fractionation of MEFs transfected with either empty vector or plasmids shown in A. mSIRT3L-1-334 and mSIRT3L-15-334 are found predominantly in the mitochondrial fraction, whereas mSIRT3L-78-334 is distributed throughout both cytosolic and mitochondrial fractions. Arrows point out the mSIRT3 protein bands that are discussed in the text.

    Techniques Used: Construct, Transfection, Staining, Cell Fractionation, Plasmid Preparation


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    Oldenbourg Wissenschaftsverlag auto 2006 54 7 334 oldenbourg wissenschaftsverlag
    Auto 2006 54 7 334 Oldenbourg Wissenschaftsverlag, supplied by Oldenbourg Wissenschaftsverlag, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Wiley Liss Inc 54 327 334 2001 2001 wiley liss
    54 327 334 2001 2001 Wiley Liss, supplied by Wiley Liss Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    334 permissio cultus pro aliquibus determi nantis locis 72 459 permutatio beneficiorum 54  (Persen Technologies Inc)

     
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    Persen Technologies Inc 334 permissio cultus pro aliquibus determi nantis locis 72 459 permutatio beneficiorum 54
    334 Permissio Cultus Pro Aliquibus Determi Nantis Locis 72 459 Permutatio Beneficiorum 54, supplied by Persen Technologies Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare msirt3 l 54 334
    The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long <t>mSIRT3.</t> The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.
    Msirt3 L 54 334, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Oldenbourg Wissenschaftsverlag auto 2006 54 7 334 oldenbourg wissenschaftsverlag
    The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long <t>mSIRT3.</t> The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.
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    The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long <t>mSIRT3.</t> The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.
    54 327 334 2001 2001 Wiley Liss, supplied by Wiley Liss Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Persen Technologies Inc 334 permissio cultus pro aliquibus determi nantis locis 72 459 permutatio beneficiorum 54
    The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long <t>mSIRT3.</t> The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.
    334 Permissio Cultus Pro Aliquibus Determi Nantis Locis 72 459 Permutatio Beneficiorum 54, supplied by Persen Technologies Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long mSIRT3. The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3

    doi: 10.1002/pro.50

    Figure Lengend Snippet: The cDNA and amino acid sequence of the longer mouse SIRT3. (A) Schematic representation of the mouse SIRT3 gene. The exons are presented as rectangular boxes with the exon number labeled in each box and the base pair numbers of the coding sequences are labeled above each box. The 5′ and 3′ untranslated regions (UTR) are colored in dark blue. Coding sequences are colored in light blue. The location of the eight base pair insertion is colored in red. The three potential start codons and the stop codon are indicated. (B) The sequence of long mSIRT3. The three methionine residues that have been considered as the starting residue are in bold character and underlined. The other residues in bold are the starting residues for different N-terminal truncations that we generated and listed in Figure ​Figure1(C).1(C). (C) Schematic representation of all the mSIRT3 proteins that were generated for enzyme activity testing. The starting and ending residue numbers are labeled. The deacetylation activity for each protein is indicated as “−” no activity, “++” high activity, and “+” low activity.

    Article Snippet: The mSIRT3 L -54-334 was further purified to >95% purity by an S200 column (GE) judged by SDS-PAGE.

    Techniques: Sequencing, Labeling, Generated, Activity Assay

    Long mSIRT3 localizes to mitochondria. (A) Schematic drawing of SIRT3 constructs. mSIRT3L-1-334 begins at the most N-terminal Met, mSIRT3L-15-334 starts at the second Met, and mSIRT3L-78-334 represents the short mSIRT3 previously believed to be the full-length protein. (B) Mouse embryonic fibroblasts were transfected with C-terminal FLAG-tagged SIRT3 constructs and stained with both anti-FLAG (green) antibody to detect over-expressed mSIRT3 and anti-cytochrome c (red) to label mitochondria. Data are representative of three independent experiments. (C) Cell fractionation of MEFs transfected with either empty vector or plasmids shown in A. mSIRT3L-1-334 and mSIRT3L-15-334 are found predominantly in the mitochondrial fraction, whereas mSIRT3L-78-334 is distributed throughout both cytosolic and mitochondrial fractions. Arrows point out the mSIRT3 protein bands that are discussed in the text.

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3

    doi: 10.1002/pro.50

    Figure Lengend Snippet: Long mSIRT3 localizes to mitochondria. (A) Schematic drawing of SIRT3 constructs. mSIRT3L-1-334 begins at the most N-terminal Met, mSIRT3L-15-334 starts at the second Met, and mSIRT3L-78-334 represents the short mSIRT3 previously believed to be the full-length protein. (B) Mouse embryonic fibroblasts were transfected with C-terminal FLAG-tagged SIRT3 constructs and stained with both anti-FLAG (green) antibody to detect over-expressed mSIRT3 and anti-cytochrome c (red) to label mitochondria. Data are representative of three independent experiments. (C) Cell fractionation of MEFs transfected with either empty vector or plasmids shown in A. mSIRT3L-1-334 and mSIRT3L-15-334 are found predominantly in the mitochondrial fraction, whereas mSIRT3L-78-334 is distributed throughout both cytosolic and mitochondrial fractions. Arrows point out the mSIRT3 protein bands that are discussed in the text.

    Article Snippet: The mSIRT3 L -54-334 was further purified to >95% purity by an S200 column (GE) judged by SDS-PAGE.

    Techniques: Construct, Transfection, Staining, Cell Fractionation, Plasmid Preparation