human light chain clathrin Search Results


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  • 85
    OriGene bglii
    Bglii, supplied by OriGene, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    OriGene human light chain clathrin
    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 ) <t>mNG-Clathrin-C-15</t> (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.
    Human Light Chain Clathrin, supplied by OriGene, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Sino Biological clathrin gfp plasmid
    The uptake of exogenous CnB occurred via TLR4 receptor-mediated internalization. ( a ) Co-localization of rhodamine-labelled CnB with <t>clathrin-GFP</t> (upper panel) or CnB-GFP with rhodamine-labelled transferrin (lower panel) in SK-HEP-1 cells. The clathrin-GFP transfected cells were co-incubated with 5 μM CnB-rhodamine, or SK-HEP-1 cells were co-incubated with 5 μM CnB-GFP mixed with 5 μM rhodamine-labelled transferrin for 30 min, and visualized using a confocal laser scanning microscope (×63, scale bar 10 μm). ( b ) Free CnB inhibits the uptake of the fluorescently labelled CnB. The cells were co-incubated with excess CnB and DyLight 488-labeled CnB or labelled CnB alone for 30 min and visualized using an inverted fluorescence microscope (upper panel, scale bar 50 μm, 20×). The fluorescence intensity was quantified using a microplate reader (lower panel). ( c ) Positive correlation between CnB uptake and TLR4 expression. 5 × 10 5 cells from different cell lines were co-incubated with 5 μM CnB for 10 min, subjected to Trizol treatment and RNA extraction. Extracted mRNA was used for qPCR analysis of TLR4. The qPCR results were analyzed and compared with CnB-GFP uptake (lower panel). 5 × 10 6 cells from different cell lines were co-incubated with 5 μM CnB for 10 min and lysed with RIPA buffer, the samples were used for detecting the protein level of TLR4 by western blot analysis (upper panel). ( d ) Co-localization of exogenous CnB-GFP and TLR4-cherry. The TLR4-cherry- or cherry-transfected Hek293 cells were co-incubated with 5 μM CnB-GFP for 30 min, and visualized using a confocal laser scanning microscope (63×, scale bar 20 μm). ( e,f ) Effect of TLR4 knock down on CnB uptake. The influence of TLR4 knock down on CnB uptake was analysed by western blot analysis ( e ) or FI ( f ), (scale bar 50 μm, 20×). ( g ) TAK242 inhibited CnB uptake. The SK-HEP-1 cells were pre-incubated with 10 μM or 5 μM TAK242 or vehicle for 3 h, followed by co-incubation with CnB-GFP for 30 min. The co-incubated cells were washed, acid-stripped and quantified by a microplate reader. Bars represent mean ± s.e.m. from three independent experiments. *P
    Clathrin Gfp Plasmid, supplied by Sino Biological, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Abcam human clathrin
    Representative confocal images of Huh7.5 cells infected with HCVpp labeled with L‐20K3H‐A, after a 10 min A) or 30 min contact B) at 37 °C before cell fixation (scale bar 5 μm). Cells were immuno‐stained for Gag (HCVpp retroviral core protein, red) and for <t>clathrin</t> (as a marker of endocytosis, green). L‐20K3H‐A fluorescence is presented as a false blue color. Inset: zoom of selected cellular area; asterisks denote HCVpp fluorescence signals merging with clathrin (red + blue + green).
    Human Clathrin, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    N/A
    Mouse monoclonal antibody to Clatherin Light Chain Isotype Note IgG2b kappa Host Note Mouse Reactivity Note Human Application Note WB IHC P IF ICC FACS
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    N/A
    Recognizes proteins of 31 44kDa which are identified as Clathrin Light Chains both A amp B Clathrin is composed of three heavy chains and three light chains which associate non
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    N/A
    Rabbit polyclonal antibody to Clathrin light chain B Isotype Note IgG Host Note Rabbit Conjugation Note Unconjugated Reactivity Note Human Application Note ELISA WB
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    Image Search Results


    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

    The uptake of exogenous CnB occurred via TLR4 receptor-mediated internalization. ( a ) Co-localization of rhodamine-labelled CnB with clathrin-GFP (upper panel) or CnB-GFP with rhodamine-labelled transferrin (lower panel) in SK-HEP-1 cells. The clathrin-GFP transfected cells were co-incubated with 5 μM CnB-rhodamine, or SK-HEP-1 cells were co-incubated with 5 μM CnB-GFP mixed with 5 μM rhodamine-labelled transferrin for 30 min, and visualized using a confocal laser scanning microscope (×63, scale bar 10 μm). ( b ) Free CnB inhibits the uptake of the fluorescently labelled CnB. The cells were co-incubated with excess CnB and DyLight 488-labeled CnB or labelled CnB alone for 30 min and visualized using an inverted fluorescence microscope (upper panel, scale bar 50 μm, 20×). The fluorescence intensity was quantified using a microplate reader (lower panel). ( c ) Positive correlation between CnB uptake and TLR4 expression. 5 × 10 5 cells from different cell lines were co-incubated with 5 μM CnB for 10 min, subjected to Trizol treatment and RNA extraction. Extracted mRNA was used for qPCR analysis of TLR4. The qPCR results were analyzed and compared with CnB-GFP uptake (lower panel). 5 × 10 6 cells from different cell lines were co-incubated with 5 μM CnB for 10 min and lysed with RIPA buffer, the samples were used for detecting the protein level of TLR4 by western blot analysis (upper panel). ( d ) Co-localization of exogenous CnB-GFP and TLR4-cherry. The TLR4-cherry- or cherry-transfected Hek293 cells were co-incubated with 5 μM CnB-GFP for 30 min, and visualized using a confocal laser scanning microscope (63×, scale bar 20 μm). ( e,f ) Effect of TLR4 knock down on CnB uptake. The influence of TLR4 knock down on CnB uptake was analysed by western blot analysis ( e ) or FI ( f ), (scale bar 50 μm, 20×). ( g ) TAK242 inhibited CnB uptake. The SK-HEP-1 cells were pre-incubated with 10 μM or 5 μM TAK242 or vehicle for 3 h, followed by co-incubation with CnB-GFP for 30 min. The co-incubated cells were washed, acid-stripped and quantified by a microplate reader. Bars represent mean ± s.e.m. from three independent experiments. *P

    Journal: Scientific Reports

    Article Title: Cellular uptake of exogenous calcineurin B is dependent on TLR4/MD2/CD14 complexes, and CnB is an endogenous ligand of TLR4

    doi: 10.1038/srep24346

    Figure Lengend Snippet: The uptake of exogenous CnB occurred via TLR4 receptor-mediated internalization. ( a ) Co-localization of rhodamine-labelled CnB with clathrin-GFP (upper panel) or CnB-GFP with rhodamine-labelled transferrin (lower panel) in SK-HEP-1 cells. The clathrin-GFP transfected cells were co-incubated with 5 μM CnB-rhodamine, or SK-HEP-1 cells were co-incubated with 5 μM CnB-GFP mixed with 5 μM rhodamine-labelled transferrin for 30 min, and visualized using a confocal laser scanning microscope (×63, scale bar 10 μm). ( b ) Free CnB inhibits the uptake of the fluorescently labelled CnB. The cells were co-incubated with excess CnB and DyLight 488-labeled CnB or labelled CnB alone for 30 min and visualized using an inverted fluorescence microscope (upper panel, scale bar 50 μm, 20×). The fluorescence intensity was quantified using a microplate reader (lower panel). ( c ) Positive correlation between CnB uptake and TLR4 expression. 5 × 10 5 cells from different cell lines were co-incubated with 5 μM CnB for 10 min, subjected to Trizol treatment and RNA extraction. Extracted mRNA was used for qPCR analysis of TLR4. The qPCR results were analyzed and compared with CnB-GFP uptake (lower panel). 5 × 10 6 cells from different cell lines were co-incubated with 5 μM CnB for 10 min and lysed with RIPA buffer, the samples were used for detecting the protein level of TLR4 by western blot analysis (upper panel). ( d ) Co-localization of exogenous CnB-GFP and TLR4-cherry. The TLR4-cherry- or cherry-transfected Hek293 cells were co-incubated with 5 μM CnB-GFP for 30 min, and visualized using a confocal laser scanning microscope (63×, scale bar 20 μm). ( e,f ) Effect of TLR4 knock down on CnB uptake. The influence of TLR4 knock down on CnB uptake was analysed by western blot analysis ( e ) or FI ( f ), (scale bar 50 μm, 20×). ( g ) TAK242 inhibited CnB uptake. The SK-HEP-1 cells were pre-incubated with 10 μM or 5 μM TAK242 or vehicle for 3 h, followed by co-incubation with CnB-GFP for 30 min. The co-incubated cells were washed, acid-stripped and quantified by a microplate reader. Bars represent mean ± s.e.m. from three independent experiments. *P

    Article Snippet: The clathrin-GFP plasmid was a gift from the Yu lab (School of Life Science, Tsinghua University).

    Techniques: Transfection, Incubation, Laser-Scanning Microscopy, Labeling, Fluorescence, Microscopy, Expressing, RNA Extraction, Real-time Polymerase Chain Reaction, Western Blot

    Representative confocal images of Huh7.5 cells infected with HCVpp labeled with L‐20K3H‐A, after a 10 min A) or 30 min contact B) at 37 °C before cell fixation (scale bar 5 μm). Cells were immuno‐stained for Gag (HCVpp retroviral core protein, red) and for clathrin (as a marker of endocytosis, green). L‐20K3H‐A fluorescence is presented as a false blue color. Inset: zoom of selected cellular area; asterisks denote HCVpp fluorescence signals merging with clathrin (red + blue + green).

    Journal: Advanced Healthcare Materials

    Article Title: Far‐Red Fluorescent Lipid‐Polymer Probes for an Efficient Labeling of Enveloped Viruses

    doi: 10.1002/adhm.201600091

    Figure Lengend Snippet: Representative confocal images of Huh7.5 cells infected with HCVpp labeled with L‐20K3H‐A, after a 10 min A) or 30 min contact B) at 37 °C before cell fixation (scale bar 5 μm). Cells were immuno‐stained for Gag (HCVpp retroviral core protein, red) and for clathrin (as a marker of endocytosis, green). L‐20K3H‐A fluorescence is presented as a false blue color. Inset: zoom of selected cellular area; asterisks denote HCVpp fluorescence signals merging with clathrin (red + blue + green).

    Article Snippet: Rabbit polyclonal antibody to human clathrin was from Abcam.

    Techniques: Infection, Labeling, Staining, Marker, Fluorescence