20 amino acid farnesylation signal Search Results


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  • 99
    Thermo Fisher ecori
    Ecori, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 12201 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore signal peptide
    Structural analysis of <t>MaltOBP1.</t> (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.
    Signal Peptide, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 586 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    OriGene bamhi
    Structural analysis of <t>MaltOBP1.</t> (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.
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    nhei  (TaKaRa)
    99
    TaKaRa nhei
    Structural analysis of <t>MaltOBP1.</t> (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.
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    TaKaRa bglii
    Structural analysis of <t>MaltOBP1.</t> (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.
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    OriGene bglii
    Structural analysis of <t>MaltOBP1.</t> (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.
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    OriGene bspei
    Structural analysis of <t>MaltOBP1.</t> (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.
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    Thermo Fisher human keratin 18
    Structural analysis of <t>MaltOBP1.</t> (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.
    Human Keratin 18, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    OriGene human pyruvate dehydrogenase
    Structural analysis of <t>MaltOBP1.</t> (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.
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    OriGene human calnexin
    Structural analysis of <t>MaltOBP1.</t> (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.
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    Thermo Fisher mkate2 f sequence
    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with <t>mKate2-F,</t> which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.
    Mkate2 F Sequence, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexafluor488 nhs ester
    (a) SDS-PAGE gel of [1] protein ladder, [2] unmodified CodA, and [3] CodA after DBCO and <t>AlexaFluor488</t> conjugation and after reacting with [4] A10 and [5] T10 DNA. (b, c) UV–vis absorbance of the dye and DNA-conjugated CodA.
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    Cell Signaling Technology Inc antibodies lats1 antibody
    Kinase activity measured by LATS in vitro kinase assay HEK293A cells were serum starved or treated with 0.2 M sorbitol for 30 min. <t>LATS1</t> was immunoprecipitated and an in vitro kinase assay was performed using recombinant GST-YAP as a substrate. Phosphorylation of YAP was determined by immunoblotting with a phospho-YAP (S127) antibody. (pYAP S127 Ab 1:1,000 dilution, GST Ab 1:2,000 dilution, LATS1 Ab 1:2,000 dilution in 5% BSA containing TBST).
    Antibodies Lats1 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher bca assay
    Kinase activity measured by LATS in vitro kinase assay HEK293A cells were serum starved or treated with 0.2 M sorbitol for 30 min. <t>LATS1</t> was immunoprecipitated and an in vitro kinase assay was performed using recombinant GST-YAP as a substrate. Phosphorylation of YAP was determined by immunoblotting with a phospho-YAP (S127) antibody. (pYAP S127 Ab 1:1,000 dilution, GST Ab 1:2,000 dilution, LATS1 Ab 1:2,000 dilution in 5% BSA containing TBST).
    Bca Assay, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 47051 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    PeproTech recombinant human bdnf
    Kinase activity measured by LATS in vitro kinase assay HEK293A cells were serum starved or treated with 0.2 M sorbitol for 30 min. <t>LATS1</t> was immunoprecipitated and an in vitro kinase assay was performed using recombinant GST-YAP as a substrate. Phosphorylation of YAP was determined by immunoblotting with a phospho-YAP (S127) antibody. (pYAP S127 Ab 1:1,000 dilution, GST Ab 1:2,000 dilution, LATS1 Ab 1:2,000 dilution in 5% BSA containing TBST).
    Recombinant Human Bdnf, supplied by PeproTech, used in various techniques. Bioz Stars score: 99/100, based on 226 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    PeproTech recombinant interferon ifn γ
    Flow cytometry analysis for the change of immune-related surface markers on <t>IFN-γ</t> treated hChonJ. After hChonJ cells were exposed to 300 IU/mL of IFN-γ, the cells were labeled with antibodies against immune-related surface markers, including MHC class I (HLA-ABC), MHC class II (HLA-DR), co-stimulatory molecules (CD80 and CD86), co-inhibitory molecules (PD-L1 and PD-L2) and immunoglobulin G1 isotype control. The expression of MHC class I and II molecules ( a ) was increased, but there was no change in the expression level of the co-stimulatory molecules CD80 and CD86 ( b ). In the case of co-inhibitory molecules, PD-L1 expression was increased and the expression of PD-L2 was detected which was not expressed on IFN-γ untreated hChonJ cells ( c ). These results are the representative of at least 3 independent experiments
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    Thermo Fisher pcdna3 1
    Flow cytometry analysis for the change of immune-related surface markers on <t>IFN-γ</t> treated hChonJ. After hChonJ cells were exposed to 300 IU/mL of IFN-γ, the cells were labeled with antibodies against immune-related surface markers, including MHC class I (HLA-ABC), MHC class II (HLA-DR), co-stimulatory molecules (CD80 and CD86), co-inhibitory molecules (PD-L1 and PD-L2) and immunoglobulin G1 isotype control. The expression of MHC class I and II molecules ( a ) was increased, but there was no change in the expression level of the co-stimulatory molecules CD80 and CD86 ( b ). In the case of co-inhibitory molecules, PD-L1 expression was increased and the expression of PD-L2 was detected which was not expressed on IFN-γ untreated hChonJ cells ( c ). These results are the representative of at least 3 independent experiments
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    OriGene β catenin
    Fluorescence imaging of mNeonGreen (mNG) fusion vectors. C-terminal mNG fusion constructs (with respect to the fluorescent protein); for each fusion, the linker amino acid length is indicated after the name of the targeted organelle or fusion partner: ( a ) mNG-Annexin (A4)-C-12 (human; plasma membrane); ( b ) mNG-β-actin-C-18 (human; actin cytoskeleton); ( c ) <t>mNG-β-Catenin-C-20</t> (mouse; tight junctions); ( d ) mNG-CAAX-C-5 (20-amino acid farnesylation signal from c-Ha-Ras; plasma membrane); (e) mNG-CAF1-C-10 (mouse chromatin assembly factor); ( f ) mNG-Caveolin1-C-10 (human); ( g ) mNG-Endosomes-C-14 (human RhoB GTPase); ( h ) mNG-Fascin-C-10 (human; actin bundling); ( i ) mNG-Fibrillarin-C-7 (human; nucleoli); ( j ) mNG-FilaminA-C-14 (human; cytoskeleton); ( k ) mNG-LAMP1-C-20 (rat; lysosomal membrane glycoprotein 1; lysosomes); ( l ) mNG-Clathrin-C-15 (human, light chain B); ( m ) mNG-Myotilin-C-14 (human; actin filaments); ( n ) mNG-PCNA-C-19 (human; replication foci); ( o ) mNG-Plastin-C-10 (human; actin binding); ( p ) mNG-Rab4a-C-7 (human; endosomes); ( q ) mNG-LC3B-C-7 (rat light chain; autophagosoms; ( r ) mNG-Talin-C-18 (mouse; focal adhesions); ( s ) mNG-Tubulin-C-35 (human; microtubules); ( t ) mNG-ZO1-C-14 (human; tight junctions). The cell line used for expression of C-terminal mNG constructs was Madin-Darby canine kidney (MDCK; ATCC, CCL-34) cells in panels ( c ) and ( t ). HeLa CCL2 (ATCC) cells were used in the remaining panels. Scale bars represent 10 μm.
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    Mediatech dmem
    Fluorescence imaging of mNeonGreen (mNG) fusion vectors. C-terminal mNG fusion constructs (with respect to the fluorescent protein); for each fusion, the linker amino acid length is indicated after the name of the targeted organelle or fusion partner: ( a ) mNG-Annexin (A4)-C-12 (human; plasma membrane); ( b ) mNG-β-actin-C-18 (human; actin cytoskeleton); ( c ) <t>mNG-β-Catenin-C-20</t> (mouse; tight junctions); ( d ) mNG-CAAX-C-5 (20-amino acid farnesylation signal from c-Ha-Ras; plasma membrane); (e) mNG-CAF1-C-10 (mouse chromatin assembly factor); ( f ) mNG-Caveolin1-C-10 (human); ( g ) mNG-Endosomes-C-14 (human RhoB GTPase); ( h ) mNG-Fascin-C-10 (human; actin bundling); ( i ) mNG-Fibrillarin-C-7 (human; nucleoli); ( j ) mNG-FilaminA-C-14 (human; cytoskeleton); ( k ) mNG-LAMP1-C-20 (rat; lysosomal membrane glycoprotein 1; lysosomes); ( l ) mNG-Clathrin-C-15 (human, light chain B); ( m ) mNG-Myotilin-C-14 (human; actin filaments); ( n ) mNG-PCNA-C-19 (human; replication foci); ( o ) mNG-Plastin-C-10 (human; actin binding); ( p ) mNG-Rab4a-C-7 (human; endosomes); ( q ) mNG-LC3B-C-7 (rat light chain; autophagosoms; ( r ) mNG-Talin-C-18 (mouse; focal adhesions); ( s ) mNG-Tubulin-C-35 (human; microtubules); ( t ) mNG-ZO1-C-14 (human; tight junctions). The cell line used for expression of C-terminal mNG constructs was Madin-Darby canine kidney (MDCK; ATCC, CCL-34) cells in panels ( c ) and ( t ). HeLa CCL2 (ATCC) cells were used in the remaining panels. Scale bars represent 10 μm.
    Dmem, supplied by Mediatech, used in various techniques. Bioz Stars score: 99/100, based on 4400 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bgl ii  (ATUM)
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    ATUM bgl ii
    Fluorescence imaging of mNeonGreen (mNG) fusion vectors. C-terminal mNG fusion constructs (with respect to the fluorescent protein); for each fusion, the linker amino acid length is indicated after the name of the targeted organelle or fusion partner: ( a ) mNG-Annexin (A4)-C-12 (human; plasma membrane); ( b ) mNG-β-actin-C-18 (human; actin cytoskeleton); ( c ) <t>mNG-β-Catenin-C-20</t> (mouse; tight junctions); ( d ) mNG-CAAX-C-5 (20-amino acid farnesylation signal from c-Ha-Ras; plasma membrane); (e) mNG-CAF1-C-10 (mouse chromatin assembly factor); ( f ) mNG-Caveolin1-C-10 (human); ( g ) mNG-Endosomes-C-14 (human RhoB GTPase); ( h ) mNG-Fascin-C-10 (human; actin bundling); ( i ) mNG-Fibrillarin-C-7 (human; nucleoli); ( j ) mNG-FilaminA-C-14 (human; cytoskeleton); ( k ) mNG-LAMP1-C-20 (rat; lysosomal membrane glycoprotein 1; lysosomes); ( l ) mNG-Clathrin-C-15 (human, light chain B); ( m ) mNG-Myotilin-C-14 (human; actin filaments); ( n ) mNG-PCNA-C-19 (human; replication foci); ( o ) mNG-Plastin-C-10 (human; actin binding); ( p ) mNG-Rab4a-C-7 (human; endosomes); ( q ) mNG-LC3B-C-7 (rat light chain; autophagosoms; ( r ) mNG-Talin-C-18 (mouse; focal adhesions); ( s ) mNG-Tubulin-C-35 (human; microtubules); ( t ) mNG-ZO1-C-14 (human; tight junctions). The cell line used for expression of C-terminal mNG constructs was Madin-Darby canine kidney (MDCK; ATCC, CCL-34) cells in panels ( c ) and ( t ). HeLa CCL2 (ATCC) cells were used in the remaining panels. Scale bars represent 10 μm.
    Bgl Ii, supplied by ATUM, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Evrogen bglii
    Fluorescence imaging of mNeonGreen (mNG) fusion vectors. C-terminal mNG fusion constructs (with respect to the fluorescent protein); for each fusion, the linker amino acid length is indicated after the name of the targeted organelle or fusion partner: ( a ) mNG-Annexin (A4)-C-12 (human; plasma membrane); ( b ) mNG-β-actin-C-18 (human; actin cytoskeleton); ( c ) <t>mNG-β-Catenin-C-20</t> (mouse; tight junctions); ( d ) mNG-CAAX-C-5 (20-amino acid farnesylation signal from c-Ha-Ras; plasma membrane); (e) mNG-CAF1-C-10 (mouse chromatin assembly factor); ( f ) mNG-Caveolin1-C-10 (human); ( g ) mNG-Endosomes-C-14 (human RhoB GTPase); ( h ) mNG-Fascin-C-10 (human; actin bundling); ( i ) mNG-Fibrillarin-C-7 (human; nucleoli); ( j ) mNG-FilaminA-C-14 (human; cytoskeleton); ( k ) mNG-LAMP1-C-20 (rat; lysosomal membrane glycoprotein 1; lysosomes); ( l ) mNG-Clathrin-C-15 (human, light chain B); ( m ) mNG-Myotilin-C-14 (human; actin filaments); ( n ) mNG-PCNA-C-19 (human; replication foci); ( o ) mNG-Plastin-C-10 (human; actin binding); ( p ) mNG-Rab4a-C-7 (human; endosomes); ( q ) mNG-LC3B-C-7 (rat light chain; autophagosoms; ( r ) mNG-Talin-C-18 (mouse; focal adhesions); ( s ) mNG-Tubulin-C-35 (human; microtubules); ( t ) mNG-ZO1-C-14 (human; tight junctions). The cell line used for expression of C-terminal mNG constructs was Madin-Darby canine kidney (MDCK; ATCC, CCL-34) cells in panels ( c ) and ( t ). HeLa CCL2 (ATCC) cells were used in the remaining panels. Scale bars represent 10 μm.
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    88
    Evrogen bsp ei
    Fluorescence imaging of mNeonGreen (mNG) fusion vectors. C-terminal mNG fusion constructs (with respect to the fluorescent protein); for each fusion, the linker amino acid length is indicated after the name of the targeted organelle or fusion partner: ( a ) mNG-Annexin (A4)-C-12 (human; plasma membrane); ( b ) mNG-β-actin-C-18 (human; actin cytoskeleton); ( c ) <t>mNG-β-Catenin-C-20</t> (mouse; tight junctions); ( d ) mNG-CAAX-C-5 (20-amino acid farnesylation signal from c-Ha-Ras; plasma membrane); (e) mNG-CAF1-C-10 (mouse chromatin assembly factor); ( f ) mNG-Caveolin1-C-10 (human); ( g ) mNG-Endosomes-C-14 (human RhoB GTPase); ( h ) mNG-Fascin-C-10 (human; actin bundling); ( i ) mNG-Fibrillarin-C-7 (human; nucleoli); ( j ) mNG-FilaminA-C-14 (human; cytoskeleton); ( k ) mNG-LAMP1-C-20 (rat; lysosomal membrane glycoprotein 1; lysosomes); ( l ) mNG-Clathrin-C-15 (human, light chain B); ( m ) mNG-Myotilin-C-14 (human; actin filaments); ( n ) mNG-PCNA-C-19 (human; replication foci); ( o ) mNG-Plastin-C-10 (human; actin binding); ( p ) mNG-Rab4a-C-7 (human; endosomes); ( q ) mNG-LC3B-C-7 (rat light chain; autophagosoms; ( r ) mNG-Talin-C-18 (mouse; focal adhesions); ( s ) mNG-Tubulin-C-35 (human; microtubules); ( t ) mNG-ZO1-C-14 (human; tight junctions). The cell line used for expression of C-terminal mNG constructs was Madin-Darby canine kidney (MDCK; ATCC, CCL-34) cells in panels ( c ) and ( t ). HeLa CCL2 (ATCC) cells were used in the remaining panels. Scale bars represent 10 μm.
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    Image Search Results


    Structural analysis of MaltOBP1. (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.

    Journal: Frontiers in Physiology

    Article Title: Characterization of MaltOBP1, a Minus-C Odorant-Binding Protein, From the Japanese Pine Sawyer Beetle, Monochamus alternatus Hope (Coleoptera: Cerambycidae)

    doi: 10.3389/fphys.2020.00212

    Figure Lengend Snippet: Structural analysis of MaltOBP1. (A) The secondary structure of MaltOBP1. (B) The 3D structure of MaltOBP1. The six α-helices are labeled as α 1 –α 6 . DB-I, Disulfide bridge-I; DB-II, Disulfide bridge-II.

    Article Snippet: Recombinant Protein Expression and Purification The recombinant MaltOBP1 gene (without signal peptide) was inserted into Escherichia coli expression vector pET32a (Novagen, Madison, WI, United States) with N-terminus 6 × His tag and subsequent TEV cleavage site using recombinant PCR.

    Techniques: Labeling

    Sex- and tissue-expression profile of MaltOBP1. (A) Electrophoretic analysis of soluble proteins from Monochamus alternatus under 15% native PAGE. M1: Protein molecular weight marker. (B) Recombinant protein analyzed by SDS-PAGE. M2: Protein molecular weight marker; Lane 1: Non-induced pET32a-MaltOBP1 in Escherichia coli ; Lane 2: Expressed protein pET32a-MaltOBP1-His after induction by IPTG; Lane 3: pET32a-MaltOBP1 protein purified through Ni-NTA column; (C) Western blot analysis of MaltOBP1 expression in total protein extracts of male and female adults of M. alternatus . AT, antennae; H, head; T, thorax; AD, abdomen; L, leg; W, wing; OBP1, Recombinant MaltOBP1.

    Journal: Frontiers in Physiology

    Article Title: Characterization of MaltOBP1, a Minus-C Odorant-Binding Protein, From the Japanese Pine Sawyer Beetle, Monochamus alternatus Hope (Coleoptera: Cerambycidae)

    doi: 10.3389/fphys.2020.00212

    Figure Lengend Snippet: Sex- and tissue-expression profile of MaltOBP1. (A) Electrophoretic analysis of soluble proteins from Monochamus alternatus under 15% native PAGE. M1: Protein molecular weight marker. (B) Recombinant protein analyzed by SDS-PAGE. M2: Protein molecular weight marker; Lane 1: Non-induced pET32a-MaltOBP1 in Escherichia coli ; Lane 2: Expressed protein pET32a-MaltOBP1-His after induction by IPTG; Lane 3: pET32a-MaltOBP1 protein purified through Ni-NTA column; (C) Western blot analysis of MaltOBP1 expression in total protein extracts of male and female adults of M. alternatus . AT, antennae; H, head; T, thorax; AD, abdomen; L, leg; W, wing; OBP1, Recombinant MaltOBP1.

    Article Snippet: Recombinant Protein Expression and Purification The recombinant MaltOBP1 gene (without signal peptide) was inserted into Escherichia coli expression vector pET32a (Novagen, Madison, WI, United States) with N-terminus 6 × His tag and subsequent TEV cleavage site using recombinant PCR.

    Techniques: Expressing, Clear Native PAGE, Molecular Weight, Marker, Recombinant, SDS Page, Purification, Western Blot

    Binding affinity of MaltOBP1. (A) Binding curve and relative Scatchard plot of MaltOBP1 and 1-NPN. (B) Competitive binding curves of selected volatile host plant compounds to MaltOBP1.

    Journal: Frontiers in Physiology

    Article Title: Characterization of MaltOBP1, a Minus-C Odorant-Binding Protein, From the Japanese Pine Sawyer Beetle, Monochamus alternatus Hope (Coleoptera: Cerambycidae)

    doi: 10.3389/fphys.2020.00212

    Figure Lengend Snippet: Binding affinity of MaltOBP1. (A) Binding curve and relative Scatchard plot of MaltOBP1 and 1-NPN. (B) Competitive binding curves of selected volatile host plant compounds to MaltOBP1.

    Article Snippet: Recombinant Protein Expression and Purification The recombinant MaltOBP1 gene (without signal peptide) was inserted into Escherichia coli expression vector pET32a (Novagen, Madison, WI, United States) with N-terminus 6 × His tag and subsequent TEV cleavage site using recombinant PCR.

    Techniques: Binding Assay

    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with mKate2-F, which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.

    Journal: PLoS ONE

    Article Title: Tyrosine 416 Is Phosphorylated in the Closed, Repressed Conformation of c-Src

    doi: 10.1371/journal.pone.0071035

    Figure Lengend Snippet: Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with mKate2-F, which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.

    Article Snippet: The mKate2-F sequence was commercially synthesized (GeneArt) with human optimized codons and appended at the C-terminus with the sequence SGLRTKLNPPDESGPGCMSCKCVLS, which includes C-terminal 20 amino acid farnesylation signal sequence from the c-HA-Ras protein , .

    Techniques: Transfection, Western Blot, Construct, Mutagenesis, Plasmid Preparation

    (a) SDS-PAGE gel of [1] protein ladder, [2] unmodified CodA, and [3] CodA after DBCO and AlexaFluor488 conjugation and after reacting with [4] A10 and [5] T10 DNA. (b, c) UV–vis absorbance of the dye and DNA-conjugated CodA.

    Journal: Biomacromolecules

    Article Title: Click Nucleic Acid Mediated Loading of Prodrug Activating Enzymes in PEG-PLGA Nanoparticles for Combination Chemotherapy

    doi: 10.1021/acs.biomac.9b00040

    Figure Lengend Snippet: (a) SDS-PAGE gel of [1] protein ladder, [2] unmodified CodA, and [3] CodA after DBCO and AlexaFluor488 conjugation and after reacting with [4] A10 and [5] T10 DNA. (b, c) UV–vis absorbance of the dye and DNA-conjugated CodA.

    Article Snippet: AlexaFluor488 NHS ester (Invitrogen), DNA sequences (Integrated DNA Tech.), ammonium chloride (Fisher), amphicillin (Sigma), biuret reagent (Sigma), coomassie stain (simplyblue safestain; Invitrogen), DBCO-NHS (Sigma), doxorubicin (DOX, Tokyo chem.

    Techniques: SDS Page, Conjugation Assay

    Confocal imaging of MDA-MB-468 incubated for 24h with 1 mg/mL of unconjugated NPs as well as particles reacted with AlexaFluor 488 modified cytosine deaminase conjugated with either polyadenine or polythymine DNA. As shown, green fluorescence from the AlexaFluor488 dye was only detected from cells incubated with PEG-CNA(T10)-PLGA nanoparticles reacted with poly-A conjugated CodA, demonstrating the specificity of CNA-DNA hybridization. Scale bars represent 50 μ m.

    Journal: Biomacromolecules

    Article Title: Click Nucleic Acid Mediated Loading of Prodrug Activating Enzymes in PEG-PLGA Nanoparticles for Combination Chemotherapy

    doi: 10.1021/acs.biomac.9b00040

    Figure Lengend Snippet: Confocal imaging of MDA-MB-468 incubated for 24h with 1 mg/mL of unconjugated NPs as well as particles reacted with AlexaFluor 488 modified cytosine deaminase conjugated with either polyadenine or polythymine DNA. As shown, green fluorescence from the AlexaFluor488 dye was only detected from cells incubated with PEG-CNA(T10)-PLGA nanoparticles reacted with poly-A conjugated CodA, demonstrating the specificity of CNA-DNA hybridization. Scale bars represent 50 μ m.

    Article Snippet: AlexaFluor488 NHS ester (Invitrogen), DNA sequences (Integrated DNA Tech.), ammonium chloride (Fisher), amphicillin (Sigma), biuret reagent (Sigma), coomassie stain (simplyblue safestain; Invitrogen), DBCO-NHS (Sigma), doxorubicin (DOX, Tokyo chem.

    Techniques: Imaging, Multiple Displacement Amplification, Incubation, Modification, Fluorescence, DNA Hybridization

    Kinase activity measured by LATS in vitro kinase assay HEK293A cells were serum starved or treated with 0.2 M sorbitol for 30 min. LATS1 was immunoprecipitated and an in vitro kinase assay was performed using recombinant GST-YAP as a substrate. Phosphorylation of YAP was determined by immunoblotting with a phospho-YAP (S127) antibody. (pYAP S127 Ab 1:1,000 dilution, GST Ab 1:2,000 dilution, LATS1 Ab 1:2,000 dilution in 5% BSA containing TBST).

    Journal: Bio-protocol

    Article Title: Non-radioactive LATS in vitro Kinase Assay

    doi: 10.21769/BioProtoc.2391

    Figure Lengend Snippet: Kinase activity measured by LATS in vitro kinase assay HEK293A cells were serum starved or treated with 0.2 M sorbitol for 30 min. LATS1 was immunoprecipitated and an in vitro kinase assay was performed using recombinant GST-YAP as a substrate. Phosphorylation of YAP was determined by immunoblotting with a phospho-YAP (S127) antibody. (pYAP S127 Ab 1:1,000 dilution, GST Ab 1:2,000 dilution, LATS1 Ab 1:2,000 dilution in 5% BSA containing TBST).

    Article Snippet: Pipette tips 10 cm plates 1.5 ml Eppendorf tube Dialyzer (EMD Millipore, catalog number: 71507-3) pGEX-KG-GST-YAP plasmid (Addgene, catalog number: 33052) BL21(DE3) competent cells (Agilent Technologies, catalog number: 230134) HEK293A cells LB broth (Fisher Scientific, catalog number: BP1426-2) Carbenicillin disodium salt (Sigma-Aldrich, catalog number: 205805-250MG) Isopropyl β-D-1-thiogalactopyranoside (IPTG) (Sigma-Aldrich, catalog number: I5502) Phosphate buffered saline (PBS) (Thermo Fisher Scientific, Gibco™, catalog number: 10010049) Protease inhibitor cocktail tablet (Roche Diagnostics, catalog number: 11873580001) Phenylmethanesulfonyl fluoride (PMSF) (Sigma-Aldrich, catalog number: P7626-5G) Dithiothreitol (DTT) (Bio-Rad Laboratories, catalog number: 1610611) Triton X-100 (Sigma-Aldrich, catalog number: T9284) Glutathione Sepharose 4B (GE Healthcare, catalog number: 17075601) Dulbecco’s modified Eagle’s medium (DMEM) (Thermo Fisher Scientific, Gibco™, catalog number: 11965092) Fetal bovine serum (FBS) (Thermo Fisher Scientific, Gibco™, catalog number: 10437028) Phosphatase inhibitor mini tablet (Thermo Fisher Scientific, Thermo Scientific™, catalog number: 88667) Protein A/G magnetic beads (Thermo Fisher Scientific, Thermo Scientific™, catalog number: 88802) Kinase buffer (New England Biolabs, catalog number: B6022S) Cold ATP (Sigma-Aldrich, catalog number: A2383) Sorbitol (Fisher Scientific, catalog number: S459-500) Antibodies Lats1 antibody (Cell Signaling Technology, catalog number: 3477S) pYAP S127 antibody (Cell Signaling Technology, catalog number: 4911S) pLATS-HM antibody (Cell Signaling Technology, catalog number: 8654S) GAPDH antibody (Santa Cruz Biotechnology, catalog number: sc-25778) GST antibody (Sigma-Aldrich, catalog number: SAB4200237) Bovine serum albumin (BSA) (Sigma-Aldrich, catalog number: A3294) Tris-base (Fisher Scientific, catalog number: BP152-10) L-glutathione reduced (Sigma-Aldrich, catalog number: G4251) β-mercaptoethanol (Sigma-Aldrich, catalog number: M6250) Sodium chloride (NaCl) (Fisher Scientific, catalog number: S271-10) Glycerol (Fisher Scientific, catalog number: G33-1) Sodium lauryl sulfate (SDS) (Fisher Scientific, catalog number: S529-500) Bromophenol blue (Bio-Rad Laboratories, catalog number: 1610404) Sodium fluoride (NaF) (Acros Organics, catalog number: 424325000) EDTA (Mediatech, catalog number: 46-034-CI) NP-40 substitute (Sigma-Aldrich, catalog number: 74385) Elution buffer (see Recipes) Dialysis buffer (see Recipes) 4× SDS sample buffer (see Recipes) Mild lysis buffer (see Recipes) TBS buffer (see Recipes)

    Techniques: Activity Assay, In Vitro, Kinase Assay, Immunoprecipitation, Recombinant

    Serum starvation and sorbitol-induced osmotic stress induce LATS HM phosphorylation HEK293A cells were treated with 0.2 M sorbitol for 30 or 60 min in the presence or absence of serum. LATS phosphorylation at the hydrophobic motif (HM) was detected with the phospho-specific pLATS antibody. (pLATS-HM Ab 1:1,000 dilution, LATS1 Ab 1:2,000 dilution, GAPDH Ab 1:2,000 dilution in 5% BSA containing TBST).

    Journal: Bio-protocol

    Article Title: Non-radioactive LATS in vitro Kinase Assay

    doi: 10.21769/BioProtoc.2391

    Figure Lengend Snippet: Serum starvation and sorbitol-induced osmotic stress induce LATS HM phosphorylation HEK293A cells were treated with 0.2 M sorbitol for 30 or 60 min in the presence or absence of serum. LATS phosphorylation at the hydrophobic motif (HM) was detected with the phospho-specific pLATS antibody. (pLATS-HM Ab 1:1,000 dilution, LATS1 Ab 1:2,000 dilution, GAPDH Ab 1:2,000 dilution in 5% BSA containing TBST).

    Article Snippet: Pipette tips 10 cm plates 1.5 ml Eppendorf tube Dialyzer (EMD Millipore, catalog number: 71507-3) pGEX-KG-GST-YAP plasmid (Addgene, catalog number: 33052) BL21(DE3) competent cells (Agilent Technologies, catalog number: 230134) HEK293A cells LB broth (Fisher Scientific, catalog number: BP1426-2) Carbenicillin disodium salt (Sigma-Aldrich, catalog number: 205805-250MG) Isopropyl β-D-1-thiogalactopyranoside (IPTG) (Sigma-Aldrich, catalog number: I5502) Phosphate buffered saline (PBS) (Thermo Fisher Scientific, Gibco™, catalog number: 10010049) Protease inhibitor cocktail tablet (Roche Diagnostics, catalog number: 11873580001) Phenylmethanesulfonyl fluoride (PMSF) (Sigma-Aldrich, catalog number: P7626-5G) Dithiothreitol (DTT) (Bio-Rad Laboratories, catalog number: 1610611) Triton X-100 (Sigma-Aldrich, catalog number: T9284) Glutathione Sepharose 4B (GE Healthcare, catalog number: 17075601) Dulbecco’s modified Eagle’s medium (DMEM) (Thermo Fisher Scientific, Gibco™, catalog number: 11965092) Fetal bovine serum (FBS) (Thermo Fisher Scientific, Gibco™, catalog number: 10437028) Phosphatase inhibitor mini tablet (Thermo Fisher Scientific, Thermo Scientific™, catalog number: 88667) Protein A/G magnetic beads (Thermo Fisher Scientific, Thermo Scientific™, catalog number: 88802) Kinase buffer (New England Biolabs, catalog number: B6022S) Cold ATP (Sigma-Aldrich, catalog number: A2383) Sorbitol (Fisher Scientific, catalog number: S459-500) Antibodies Lats1 antibody (Cell Signaling Technology, catalog number: 3477S) pYAP S127 antibody (Cell Signaling Technology, catalog number: 4911S) pLATS-HM antibody (Cell Signaling Technology, catalog number: 8654S) GAPDH antibody (Santa Cruz Biotechnology, catalog number: sc-25778) GST antibody (Sigma-Aldrich, catalog number: SAB4200237) Bovine serum albumin (BSA) (Sigma-Aldrich, catalog number: A3294) Tris-base (Fisher Scientific, catalog number: BP152-10) L-glutathione reduced (Sigma-Aldrich, catalog number: G4251) β-mercaptoethanol (Sigma-Aldrich, catalog number: M6250) Sodium chloride (NaCl) (Fisher Scientific, catalog number: S271-10) Glycerol (Fisher Scientific, catalog number: G33-1) Sodium lauryl sulfate (SDS) (Fisher Scientific, catalog number: S529-500) Bromophenol blue (Bio-Rad Laboratories, catalog number: 1610404) Sodium fluoride (NaF) (Acros Organics, catalog number: 424325000) EDTA (Mediatech, catalog number: 46-034-CI) NP-40 substitute (Sigma-Aldrich, catalog number: 74385) Elution buffer (see Recipes) Dialysis buffer (see Recipes) 4× SDS sample buffer (see Recipes) Mild lysis buffer (see Recipes) TBS buffer (see Recipes)

    Techniques:

    Flow cytometry analysis for the change of immune-related surface markers on IFN-γ treated hChonJ. After hChonJ cells were exposed to 300 IU/mL of IFN-γ, the cells were labeled with antibodies against immune-related surface markers, including MHC class I (HLA-ABC), MHC class II (HLA-DR), co-stimulatory molecules (CD80 and CD86), co-inhibitory molecules (PD-L1 and PD-L2) and immunoglobulin G1 isotype control. The expression of MHC class I and II molecules ( a ) was increased, but there was no change in the expression level of the co-stimulatory molecules CD80 and CD86 ( b ). In the case of co-inhibitory molecules, PD-L1 expression was increased and the expression of PD-L2 was detected which was not expressed on IFN-γ untreated hChonJ cells ( c ). These results are the representative of at least 3 independent experiments

    Journal: BMC Musculoskeletal Disorders

    Article Title: Immunogenicity and immunomodulatory effects of the human chondrocytes, hChonJ

    doi: 10.1186/s12891-017-1547-8

    Figure Lengend Snippet: Flow cytometry analysis for the change of immune-related surface markers on IFN-γ treated hChonJ. After hChonJ cells were exposed to 300 IU/mL of IFN-γ, the cells were labeled with antibodies against immune-related surface markers, including MHC class I (HLA-ABC), MHC class II (HLA-DR), co-stimulatory molecules (CD80 and CD86), co-inhibitory molecules (PD-L1 and PD-L2) and immunoglobulin G1 isotype control. The expression of MHC class I and II molecules ( a ) was increased, but there was no change in the expression level of the co-stimulatory molecules CD80 and CD86 ( b ). In the case of co-inhibitory molecules, PD-L1 expression was increased and the expression of PD-L2 was detected which was not expressed on IFN-γ untreated hChonJ cells ( c ). These results are the representative of at least 3 independent experiments

    Article Snippet: Recombinant interferon (IFN)-γ was purchased from Peprotech (NJ, USA), isopropyl alcohol, mitomycin C and phytohemagglutinin were purchased from Sigma Chemical (MO, USA) and 3 H-thymidine was purchased from American Radiolabeled Chemicals (MO, USA).

    Techniques: Flow Cytometry, Cytometry, Labeling, Expressing

    Fluorescence imaging of mNeonGreen (mNG) fusion vectors. C-terminal mNG fusion constructs (with respect to the fluorescent protein); for each fusion, the linker amino acid length is indicated after the name of the targeted organelle or fusion partner: ( a ) mNG-Annexin (A4)-C-12 (human; plasma membrane); ( b ) mNG-β-actin-C-18 (human; actin cytoskeleton); ( c ) mNG-β-Catenin-C-20 (mouse; tight junctions); ( d ) mNG-CAAX-C-5 (20-amino acid farnesylation signal from c-Ha-Ras; plasma membrane); (e) mNG-CAF1-C-10 (mouse chromatin assembly factor); ( f ) mNG-Caveolin1-C-10 (human); ( g ) mNG-Endosomes-C-14 (human RhoB GTPase); ( h ) mNG-Fascin-C-10 (human; actin bundling); ( i ) mNG-Fibrillarin-C-7 (human; nucleoli); ( j ) mNG-FilaminA-C-14 (human; cytoskeleton); ( k ) mNG-LAMP1-C-20 (rat; lysosomal membrane glycoprotein 1; lysosomes); ( l ) mNG-Clathrin-C-15 (human, light chain B); ( m ) mNG-Myotilin-C-14 (human; actin filaments); ( n ) mNG-PCNA-C-19 (human; replication foci); ( o ) mNG-Plastin-C-10 (human; actin binding); ( p ) mNG-Rab4a-C-7 (human; endosomes); ( q ) mNG-LC3B-C-7 (rat light chain; autophagosoms; ( r ) mNG-Talin-C-18 (mouse; focal adhesions); ( s ) mNG-Tubulin-C-35 (human; microtubules); ( t ) mNG-ZO1-C-14 (human; tight junctions). The cell line used for expression of C-terminal mNG constructs was Madin-Darby canine kidney (MDCK; ATCC, CCL-34) cells in panels ( c ) and ( t ). HeLa CCL2 (ATCC) cells were used in the remaining panels. Scale bars represent 10 μm.

    Journal: Nature methods

    Article Title: A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum

    doi: 10.1038/nmeth.2413

    Figure Lengend Snippet: Fluorescence imaging of mNeonGreen (mNG) fusion vectors. C-terminal mNG fusion constructs (with respect to the fluorescent protein); for each fusion, the linker amino acid length is indicated after the name of the targeted organelle or fusion partner: ( a ) mNG-Annexin (A4)-C-12 (human; plasma membrane); ( b ) mNG-β-actin-C-18 (human; actin cytoskeleton); ( c ) mNG-β-Catenin-C-20 (mouse; tight junctions); ( d ) mNG-CAAX-C-5 (20-amino acid farnesylation signal from c-Ha-Ras; plasma membrane); (e) mNG-CAF1-C-10 (mouse chromatin assembly factor); ( f ) mNG-Caveolin1-C-10 (human); ( g ) mNG-Endosomes-C-14 (human RhoB GTPase); ( h ) mNG-Fascin-C-10 (human; actin bundling); ( i ) mNG-Fibrillarin-C-7 (human; nucleoli); ( j ) mNG-FilaminA-C-14 (human; cytoskeleton); ( k ) mNG-LAMP1-C-20 (rat; lysosomal membrane glycoprotein 1; lysosomes); ( l ) mNG-Clathrin-C-15 (human, light chain B); ( m ) mNG-Myotilin-C-14 (human; actin filaments); ( n ) mNG-PCNA-C-19 (human; replication foci); ( o ) mNG-Plastin-C-10 (human; actin binding); ( p ) mNG-Rab4a-C-7 (human; endosomes); ( q ) mNG-LC3B-C-7 (rat light chain; autophagosoms; ( r ) mNG-Talin-C-18 (mouse; focal adhesions); ( s ) mNG-Tubulin-C-35 (human; microtubules); ( t ) mNG-ZO1-C-14 (human; tight junctions). The cell line used for expression of C-terminal mNG constructs was Madin-Darby canine kidney (MDCK; ATCC, CCL-34) cells in panels ( c ) and ( t ). HeLa CCL2 (ATCC) cells were used in the remaining panels. Scale bars represent 10 μm.

    Article Snippet: Thus, to prepare mNeonGreen C-terminal fusions (number of linker amino acids in parenthesis), the following digests were performed: annexin A4 (12), NheI and BspEI (Alen Piljic, EMBL, Heidelberg, Germany; NM_001153.3); β-actin (7), NheI and BglII (human β-actin cDNA source: Clontech; NM_001101.3); β-catenin (20), XhoI and BamHI (mouse β-catenin cDNA source: Origene, Rockville, MD; NM_001165902.1); 20 amino acid farnesylation signal from c-Ha-Ras (CAAX; 5), AgeI and BspEI (c-Ha-Ras cDNA source: Clontech; NM_001130442.1); CAF1 (10), AgeI and BspEI (mouse chromatin assembly factor cDNA source: Akash Gunjan, Florida State University; NM_013733.3); caveolin 1 (10), NheI and BglII (human caveolin 1 cDNA source: Origene; NM_001753); endosomes (14), NheI and BspEI (endosomes cDNA source: Clontech; NM_004040.2); fascin (10), BspEI and BamHI (human fascin cDNA source: Origene; NM_003088.2); fibrillarin (7), AgeI and BspEI (fibrillarin cDNA source: Evrogen, Moscow, Russia; NM_001436.3); filamin A (14), BspEI and HindIII (human filamin cDNA source: David Calderwood, Yale University; NM_001456.3); human lysosomal membrane glycoprotein 1 (20), BamHI and NotI (LAMP1; George Patterson, NIH, Bethesda MD, U.S.A.; NM_012857.1); human light chain clathrin (15), NheI and BglII (human clathrin light chain cDNA source: George Patterson, NIH; NM_001834.2); human myotilin, AgeI and BspEI (MYOT; Origene; NM_006790.1); PCNA (19), AgeI and BspEI (proliferating cell nuclear antigen cDNA source: David Gilbert, FSU; NM_002592.2); plastin (10), BspEI and XhoI (human plastin 1 (fimbrin) cDNA source: Origene; NM_002670.1); canine Rab4a, BglII and BamHI (Rab4a cDNA source: Viki Allen, U. Manchester, UK; NM_004578.2); LC3B (7), AgeI and BspEI (rat LC3B cDNA source: Jenny M. Tam, Harvard University; U05784.1); talin (22) AgeI and BspEI (mouse talin 1 cDNA source: Clare Waterman, NIH; NM_011602.5); α-tubulin (18), NheI and BglII (human α-tubulin cDNA source: Clontech; NM_006082).

    Techniques: Fluorescence, Imaging, Construct, Binding Assay, Expressing