goat anti rabbit igg h l secondary antibody Thermo Fisher Search Results


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  • 90
    Thermo Fisher goat anti rabbit igg h l cross adsorbed
    Goat Anti Rabbit Igg H L Cross Adsorbed, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti rabbit igg h l
    Reactivity of anti-hdsg3 Abs with cells expressing mdsg3. The 293 cells were transfected with pSR α neo vector containing full-length mdsg3 cDNA, and stable cell lines were established (293 mdsg3). Cells were analysed by flow cytometry for the expression of mdsg3 by staining with rabbit anti-hdsg3 antibody (1 : 100), followed by FITC- conjugated goat <t>antirabbit</t> <t>IgG</t> (1 : 100). Propidium iodide was used to distinguish live from dead cells. — , 293 cells; ···, 293 mdsg3 cells.
    Goat Anti Rabbit Igg H L, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1133 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher goat anti rabbit igg h l alexa594
    Reactivity of anti-hdsg3 Abs with cells expressing mdsg3. The 293 cells were transfected with pSR α neo vector containing full-length mdsg3 cDNA, and stable cell lines were established (293 mdsg3). Cells were analysed by flow cytometry for the expression of mdsg3 by staining with rabbit anti-hdsg3 antibody (1 : 100), followed by FITC- conjugated goat <t>antirabbit</t> <t>IgG</t> (1 : 100). Propidium iodide was used to distinguish live from dead cells. — , 293 cells; ···, 293 mdsg3 cells.
    Goat Anti Rabbit Igg H L Alexa594, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher anti rabbit igg dylight 800
    Reactivity of anti-hdsg3 Abs with cells expressing mdsg3. The 293 cells were transfected with pSR α neo vector containing full-length mdsg3 cDNA, and stable cell lines were established (293 mdsg3). Cells were analysed by flow cytometry for the expression of mdsg3 by staining with rabbit anti-hdsg3 antibody (1 : 100), followed by FITC- conjugated goat <t>antirabbit</t> <t>IgG</t> (1 : 100). Propidium iodide was used to distinguish live from dead cells. — , 293 cells; ···, 293 mdsg3 cells.
    Anti Rabbit Igg Dylight 800, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa fluor goat anti rabbit igg h l
    Reactivity of anti-hdsg3 Abs with cells expressing mdsg3. The 293 cells were transfected with pSR α neo vector containing full-length mdsg3 cDNA, and stable cell lines were established (293 mdsg3). Cells were analysed by flow cytometry for the expression of mdsg3 by staining with rabbit anti-hdsg3 antibody (1 : 100), followed by FITC- conjugated goat <t>antirabbit</t> <t>IgG</t> (1 : 100). Propidium iodide was used to distinguish live from dead cells. — , 293 cells; ···, 293 mdsg3 cells.
    Alexa Fluor Goat Anti Rabbit Igg H L, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 80/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa fluor 488 goat anti rabbit igg
    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. <t>Alexa</t> fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.
    Alexa Fluor 488 Goat Anti Rabbit Igg, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 6452 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti rabbit igg h l hrp
    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. <t>Alexa</t> fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.
    Goat Anti Rabbit Igg H L Hrp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 82 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher anti rabbit
    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. <t>Alexa</t> fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.
    Anti Rabbit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 10505 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher antirabbit igg
    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. <t>Alexa</t> fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.
    Antirabbit Igg, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 148 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher alexa fluor 546 goat anti rabbit igg h l
    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. <t>Alexa</t> fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.
    Alexa Fluor 546 Goat Anti Rabbit Igg H L, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 117 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa fluor 405 goat anti rabbit igg h l
    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. <t>Alexa</t> fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.
    Alexa Fluor 405 Goat Anti Rabbit Igg H L, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa546 labeled goat anti rabbit igg h l
    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. <t>Alexa</t> fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.
    Alexa546 Labeled Goat Anti Rabbit Igg H L, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa fluor 680 goat anti rabbit igg h l
    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. <t>Alexa</t> fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.
    Alexa Fluor 680 Goat Anti Rabbit Igg H L, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    75
    Thermo Fisher goat anti rabbit igg alexa 647 h l invitrogen
    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. <t>Alexa</t> fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.
    Goat Anti Rabbit Igg Alexa 647 H L Invitrogen, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 75/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher fitc goat anti rabbit igg h l fitc
    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. <t>Alexa</t> fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.
    Fitc Goat Anti Rabbit Igg H L Fitc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa fluor 647 goat anti rabbit igg h l
    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by <t>Alexa</t> <t>Fluor</t> 647 goat anti rabbit
    Alexa Fluor 647 Goat Anti Rabbit Igg H L, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 86 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti rabbit igg h l horseradish peroxidase
    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by <t>Alexa</t> <t>Fluor</t> 647 goat anti rabbit
    Goat Anti Rabbit Igg H L Horseradish Peroxidase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa fluor 568 goat anti rabbit igg h l
    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by <t>Alexa</t> <t>Fluor</t> 647 goat anti rabbit
    Alexa Fluor 568 Goat Anti Rabbit Igg H L, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 129 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti rabbit igg h l superclonal secondary antibody
    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by <t>Alexa</t> <t>Fluor</t> 647 goat anti rabbit
    Goat Anti Rabbit Igg H L Superclonal Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 498 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rhodamine red x goat anti rabbit igg h l
    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by <t>Alexa</t> <t>Fluor</t> 647 goat anti rabbit
    Rhodamine Red X Goat Anti Rabbit Igg H L, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher biotin goat anti rabbit igg h l ds grade
    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by <t>Alexa</t> <t>Fluor</t> 647 goat anti rabbit
    Biotin Goat Anti Rabbit Igg H L Ds Grade, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher alexafluor 488 conjugated goat anti rabbit igg h l
    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by <t>Alexa</t> <t>Fluor</t> 647 goat anti rabbit
    Alexafluor 488 Conjugated Goat Anti Rabbit Igg H L, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 76 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa fluor 546 goat anti rabbit igg h l conjugate
    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by <t>Alexa</t> <t>Fluor</t> 647 goat anti rabbit
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    Thermo Fisher alexa fluor 555 goat anti rabbit igg h l
    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by <t>Alexa</t> <t>Fluor</t> 647 goat anti rabbit
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    Thermo Fisher alexa fluor 488 goat anti rabbit igg h l green
    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by <t>Alexa</t> <t>Fluor</t> 647 goat anti rabbit
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    Thermo Fisher goat anti rabbit igg h l cross adsorbed secondary antibody
    In vitro binding studies of the peptide <t>FnBPA5-Alexa-488</t> and the scrambled control (scraFnBPA5-Alexa-488) to soluble and fibrillar Fn. a Mechanosensitive binding of FnBPA5 was tested using relaxed (7% strain) and stretched (380% strain) fibers. Color-coded intensity ratio images of FnBPA5-Alexa488 divided by Fn-Cy5 of manually pulled Fn fibers of different mechanical state show higher binding to relaxed fibers than to stretched ones, leading to a higher FnBPA5/Fn ratio (representative images). Scale bar, 50 μm. b Normalized analysis of relaxed and stretched fibers showing a significant decrease in binding ratio of FnBPA5 from relaxed to stretched fibers. Data from 30 fibers from three independent experiments with error bars being standard deviations. p -value was obtained from a Student’s t test. c Schematic of manual fiber pulling, using a sharp pipette tip dipping into a Fn solution and pulling Fn fibers onto a flexible silicone sheet. d The binding of FnBPA5-Alexa-488 and scraFnBPA5-Alexa488 to soluble plasma Fn was determined using an anisotropy measurement (Methods). The results show a K d of 75 ± 8 nM for FnBPA5-Alexa488 and no specific binding for the scrambled control peptide. e Measurements of affinity of FnBPA5-Alexa488 to single relaxed Fn fibers showed a K d of 28 ± 6 nM. f Fluorescence images showing the binding of FnBPA5-Alexa488 and scraFnBPA5-Alexa488 to single relaxed Fn fibers (7% strain) using a previously described stretch assay 41 . For this experiment Cy5-labeled Fn was used (images on the left side). Scale bar, 50 μm. g The quantification of the fluorescence intensity showed a significant higher binding of FnBPA5-Alexa488 compared to the control. Data from 30 fibers from three independent experiments were analyzed. Shown error bars represent the standard deviation. p -value was obtained from a Student’s t test. h Human dermal fibroblast ECM was stained for Fn and incubated with FnBPA5-Alexa488 and the scrambled control peptide, respectively. Representative images show specific binding of FnBPA5-Alexa488 to Fn. Scale bar, 10 μm
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    Thermo Fisher fluorophore tagged secondary goat anti rabbit igg h l antibody
    In vitro binding studies of the peptide <t>FnBPA5-Alexa-488</t> and the scrambled control (scraFnBPA5-Alexa-488) to soluble and fibrillar Fn. a Mechanosensitive binding of FnBPA5 was tested using relaxed (7% strain) and stretched (380% strain) fibers. Color-coded intensity ratio images of FnBPA5-Alexa488 divided by Fn-Cy5 of manually pulled Fn fibers of different mechanical state show higher binding to relaxed fibers than to stretched ones, leading to a higher FnBPA5/Fn ratio (representative images). Scale bar, 50 μm. b Normalized analysis of relaxed and stretched fibers showing a significant decrease in binding ratio of FnBPA5 from relaxed to stretched fibers. Data from 30 fibers from three independent experiments with error bars being standard deviations. p -value was obtained from a Student’s t test. c Schematic of manual fiber pulling, using a sharp pipette tip dipping into a Fn solution and pulling Fn fibers onto a flexible silicone sheet. d The binding of FnBPA5-Alexa-488 and scraFnBPA5-Alexa488 to soluble plasma Fn was determined using an anisotropy measurement (Methods). The results show a K d of 75 ± 8 nM for FnBPA5-Alexa488 and no specific binding for the scrambled control peptide. e Measurements of affinity of FnBPA5-Alexa488 to single relaxed Fn fibers showed a K d of 28 ± 6 nM. f Fluorescence images showing the binding of FnBPA5-Alexa488 and scraFnBPA5-Alexa488 to single relaxed Fn fibers (7% strain) using a previously described stretch assay 41 . For this experiment Cy5-labeled Fn was used (images on the left side). Scale bar, 50 μm. g The quantification of the fluorescence intensity showed a significant higher binding of FnBPA5-Alexa488 compared to the control. Data from 30 fibers from three independent experiments were analyzed. Shown error bars represent the standard deviation. p -value was obtained from a Student’s t test. h Human dermal fibroblast ECM was stained for Fn and incubated with FnBPA5-Alexa488 and the scrambled control peptide, respectively. Representative images show specific binding of FnBPA5-Alexa488 to Fn. Scale bar, 10 μm
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    Thermo Fisher goat anti rabbit igg h l highly cross adsorbed secondary antibody
    In vitro binding studies of the peptide <t>FnBPA5-Alexa-488</t> and the scrambled control (scraFnBPA5-Alexa-488) to soluble and fibrillar Fn. a Mechanosensitive binding of FnBPA5 was tested using relaxed (7% strain) and stretched (380% strain) fibers. Color-coded intensity ratio images of FnBPA5-Alexa488 divided by Fn-Cy5 of manually pulled Fn fibers of different mechanical state show higher binding to relaxed fibers than to stretched ones, leading to a higher FnBPA5/Fn ratio (representative images). Scale bar, 50 μm. b Normalized analysis of relaxed and stretched fibers showing a significant decrease in binding ratio of FnBPA5 from relaxed to stretched fibers. Data from 30 fibers from three independent experiments with error bars being standard deviations. p -value was obtained from a Student’s t test. c Schematic of manual fiber pulling, using a sharp pipette tip dipping into a Fn solution and pulling Fn fibers onto a flexible silicone sheet. d The binding of FnBPA5-Alexa-488 and scraFnBPA5-Alexa488 to soluble plasma Fn was determined using an anisotropy measurement (Methods). The results show a K d of 75 ± 8 nM for FnBPA5-Alexa488 and no specific binding for the scrambled control peptide. e Measurements of affinity of FnBPA5-Alexa488 to single relaxed Fn fibers showed a K d of 28 ± 6 nM. f Fluorescence images showing the binding of FnBPA5-Alexa488 and scraFnBPA5-Alexa488 to single relaxed Fn fibers (7% strain) using a previously described stretch assay 41 . For this experiment Cy5-labeled Fn was used (images on the left side). Scale bar, 50 μm. g The quantification of the fluorescence intensity showed a significant higher binding of FnBPA5-Alexa488 compared to the control. Data from 30 fibers from three independent experiments were analyzed. Shown error bars represent the standard deviation. p -value was obtained from a Student’s t test. h Human dermal fibroblast ECM was stained for Fn and incubated with FnBPA5-Alexa488 and the scrambled control peptide, respectively. Representative images show specific binding of FnBPA5-Alexa488 to Fn. Scale bar, 10 μm
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    Thermo Fisher alexa fluorò 555 goat anti rabbit igg
    In vitro binding studies of the peptide <t>FnBPA5-Alexa-488</t> and the scrambled control (scraFnBPA5-Alexa-488) to soluble and fibrillar Fn. a Mechanosensitive binding of FnBPA5 was tested using relaxed (7% strain) and stretched (380% strain) fibers. Color-coded intensity ratio images of FnBPA5-Alexa488 divided by Fn-Cy5 of manually pulled Fn fibers of different mechanical state show higher binding to relaxed fibers than to stretched ones, leading to a higher FnBPA5/Fn ratio (representative images). Scale bar, 50 μm. b Normalized analysis of relaxed and stretched fibers showing a significant decrease in binding ratio of FnBPA5 from relaxed to stretched fibers. Data from 30 fibers from three independent experiments with error bars being standard deviations. p -value was obtained from a Student’s t test. c Schematic of manual fiber pulling, using a sharp pipette tip dipping into a Fn solution and pulling Fn fibers onto a flexible silicone sheet. d The binding of FnBPA5-Alexa-488 and scraFnBPA5-Alexa488 to soluble plasma Fn was determined using an anisotropy measurement (Methods). The results show a K d of 75 ± 8 nM for FnBPA5-Alexa488 and no specific binding for the scrambled control peptide. e Measurements of affinity of FnBPA5-Alexa488 to single relaxed Fn fibers showed a K d of 28 ± 6 nM. f Fluorescence images showing the binding of FnBPA5-Alexa488 and scraFnBPA5-Alexa488 to single relaxed Fn fibers (7% strain) using a previously described stretch assay 41 . For this experiment Cy5-labeled Fn was used (images on the left side). Scale bar, 50 μm. g The quantification of the fluorescence intensity showed a significant higher binding of FnBPA5-Alexa488 compared to the control. Data from 30 fibers from three independent experiments were analyzed. Shown error bars represent the standard deviation. p -value was obtained from a Student’s t test. h Human dermal fibroblast ECM was stained for Fn and incubated with FnBPA5-Alexa488 and the scrambled control peptide, respectively. Representative images show specific binding of FnBPA5-Alexa488 to Fn. Scale bar, 10 μm
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    Thermo Fisher biotinylated goat anti rabbit igg h l
    In vitro binding studies of the peptide <t>FnBPA5-Alexa-488</t> and the scrambled control (scraFnBPA5-Alexa-488) to soluble and fibrillar Fn. a Mechanosensitive binding of FnBPA5 was tested using relaxed (7% strain) and stretched (380% strain) fibers. Color-coded intensity ratio images of FnBPA5-Alexa488 divided by Fn-Cy5 of manually pulled Fn fibers of different mechanical state show higher binding to relaxed fibers than to stretched ones, leading to a higher FnBPA5/Fn ratio (representative images). Scale bar, 50 μm. b Normalized analysis of relaxed and stretched fibers showing a significant decrease in binding ratio of FnBPA5 from relaxed to stretched fibers. Data from 30 fibers from three independent experiments with error bars being standard deviations. p -value was obtained from a Student’s t test. c Schematic of manual fiber pulling, using a sharp pipette tip dipping into a Fn solution and pulling Fn fibers onto a flexible silicone sheet. d The binding of FnBPA5-Alexa-488 and scraFnBPA5-Alexa488 to soluble plasma Fn was determined using an anisotropy measurement (Methods). The results show a K d of 75 ± 8 nM for FnBPA5-Alexa488 and no specific binding for the scrambled control peptide. e Measurements of affinity of FnBPA5-Alexa488 to single relaxed Fn fibers showed a K d of 28 ± 6 nM. f Fluorescence images showing the binding of FnBPA5-Alexa488 and scraFnBPA5-Alexa488 to single relaxed Fn fibers (7% strain) using a previously described stretch assay 41 . For this experiment Cy5-labeled Fn was used (images on the left side). Scale bar, 50 μm. g The quantification of the fluorescence intensity showed a significant higher binding of FnBPA5-Alexa488 compared to the control. Data from 30 fibers from three independent experiments were analyzed. Shown error bars represent the standard deviation. p -value was obtained from a Student’s t test. h Human dermal fibroblast ECM was stained for Fn and incubated with FnBPA5-Alexa488 and the scrambled control peptide, respectively. Representative images show specific binding of FnBPA5-Alexa488 to Fn. Scale bar, 10 μm
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    Thermo Fisher goat anti rabbit igg h l poly hrp secondary antibody
    In vitro binding studies of the peptide <t>FnBPA5-Alexa-488</t> and the scrambled control (scraFnBPA5-Alexa-488) to soluble and fibrillar Fn. a Mechanosensitive binding of FnBPA5 was tested using relaxed (7% strain) and stretched (380% strain) fibers. Color-coded intensity ratio images of FnBPA5-Alexa488 divided by Fn-Cy5 of manually pulled Fn fibers of different mechanical state show higher binding to relaxed fibers than to stretched ones, leading to a higher FnBPA5/Fn ratio (representative images). Scale bar, 50 μm. b Normalized analysis of relaxed and stretched fibers showing a significant decrease in binding ratio of FnBPA5 from relaxed to stretched fibers. Data from 30 fibers from three independent experiments with error bars being standard deviations. p -value was obtained from a Student’s t test. c Schematic of manual fiber pulling, using a sharp pipette tip dipping into a Fn solution and pulling Fn fibers onto a flexible silicone sheet. d The binding of FnBPA5-Alexa-488 and scraFnBPA5-Alexa488 to soluble plasma Fn was determined using an anisotropy measurement (Methods). The results show a K d of 75 ± 8 nM for FnBPA5-Alexa488 and no specific binding for the scrambled control peptide. e Measurements of affinity of FnBPA5-Alexa488 to single relaxed Fn fibers showed a K d of 28 ± 6 nM. f Fluorescence images showing the binding of FnBPA5-Alexa488 and scraFnBPA5-Alexa488 to single relaxed Fn fibers (7% strain) using a previously described stretch assay 41 . For this experiment Cy5-labeled Fn was used (images on the left side). Scale bar, 50 μm. g The quantification of the fluorescence intensity showed a significant higher binding of FnBPA5-Alexa488 compared to the control. Data from 30 fibers from three independent experiments were analyzed. Shown error bars represent the standard deviation. p -value was obtained from a Student’s t test. h Human dermal fibroblast ECM was stained for Fn and incubated with FnBPA5-Alexa488 and the scrambled control peptide, respectively. Representative images show specific binding of FnBPA5-Alexa488 to Fn. Scale bar, 10 μm
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    Image Search Results


    Reactivity of anti-hdsg3 Abs with cells expressing mdsg3. The 293 cells were transfected with pSR α neo vector containing full-length mdsg3 cDNA, and stable cell lines were established (293 mdsg3). Cells were analysed by flow cytometry for the expression of mdsg3 by staining with rabbit anti-hdsg3 antibody (1 : 100), followed by FITC- conjugated goat antirabbit IgG (1 : 100). Propidium iodide was used to distinguish live from dead cells. — , 293 cells; ···, 293 mdsg3 cells.

    Journal: Clinical and Experimental Immunology

    Article Title: Relevance of differential immunogenicity of human and mouse recombinant desmoglein-3 for the induction of Acantholytic autoantibodies in mice

    doi: 10.1046/j.1365-2249.2003.02135.x

    Figure Lengend Snippet: Reactivity of anti-hdsg3 Abs with cells expressing mdsg3. The 293 cells were transfected with pSR α neo vector containing full-length mdsg3 cDNA, and stable cell lines were established (293 mdsg3). Cells were analysed by flow cytometry for the expression of mdsg3 by staining with rabbit anti-hdsg3 antibody (1 : 100), followed by FITC- conjugated goat antirabbit IgG (1 : 100). Propidium iodide was used to distinguish live from dead cells. — , 293 cells; ···, 293 mdsg3 cells.

    Article Snippet: Blots were treated for 1 h with a blocking buffer (5% non-fat dry milk in 200 m m NaCl with 0·1% Tween-20), and then incubated for 1 h each with the following reagents in succession with washing between each step: 1 : 2000 diluted rabbit anti-hdsg3 antibody [ ], and 1 : 3000 diluted HRP-conjugated goat antirabbit IgG (Caltag Laboratories, San Francisco, CA, USA).

    Techniques: Expressing, Transfection, Plasmid Preparation, Stable Transfection, Flow Cytometry, Cytometry, Staining

    Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. Alexa fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.

    Journal: PLoS ONE

    Article Title: RNF185, a Novel Mitochondrial Ubiquitin E3 Ligase, Regulates Autophagy through Interaction with BNIP1

    doi: 10.1371/journal.pone.0024367

    Figure Lengend Snippet: Mitochondrial localization of exogenously expressed and endogenous RNF185. ( A ) schematic presentation of GFP tagged full-length RNF185 and its mutants. RNF185-WT, wild type RNF185; RNF185-RM, RING domain mutated; RNF185-TM, two TM domains deleted; RNF185-TM1, the first TM domain mutated; RNF185-TM2, the second TM domain deleted. ( B ) RNF185's predicted TM domains mediated its localization to mitochondria. GFP tagged wild type or mutated RNF185 was transfected into HeLa cells and MitoTracker Red was used to stain mitochondria at 24 h post transfection. ( C ) GFP-RNF185 colocalized with DsRed2-Mito. Plasmid encoding GFP tagged wild type RNF185 (GFP-RNF185) and pDsRed2-Mito were co-transfected into HeLa cells and confocal microscopic analysis was taken at 24 h post transfection. ( D ) Endogenous RNF185 localized at mitochondria. HeLa cells were subjected to immunocytochemistry-based confocal microscopic analysis with Rabbit IgG or affinity chromatography purified polyclonal antibody (pAb) raised against RNF185. Alexa fluor 488-conjugated goat anti Rabbit IgG(H+L) (Green) served as the secondary antibody. Mitochondria were stained with MitoTracker Red (Red) and DNA was stained with Hoechst 33258 (Blue). White bar, 10 µm.

    Article Snippet: Secondary antibodies used were: Alexa Fluor 488 goat anti-rabbit IgG(H+L) (Invitrogen), TRITC goat anti-mouse IgG(H+L) (Zymed Laboratories), horseradish peroxidase (HRP) conjugated goat anti-rabbit/mouse IgG(H+L) (Sigma), HRP conjugated goat anti-mouse Fc fragment (Thermo Scientific) and HRP conjugated goat anti-rabbit Fc fragment (Jackson ImmunoResearch Laboratories).

    Techniques: Transfection, Staining, Plasmid Preparation, Immunocytochemistry, Affinity Chromatography, Purification

    Analysis of toll-like receptor 3 (TLR3) expression in porcine intestinal epithelial (PIE) cells . (A) Flow cytometric analysis of TLR3 in PIE cells. Histograms show flow cytometric analysis for TLR3 staining as follows: intracellular (open histogram), cell surface (broken lines) and isotype-matched controls (shaded histograms). The analysis of intracellular and cell surface expression of TLR3 is presented as the log of mean fluorescence intensity (MFI). The results represent three independent experiments. (B) Confocal microscopic analysis of the subcellular localization of TLR3 in PIE cells. Fixed and permeabilized cells were stained with anti-mouse TLR3(unlabeled) rabbit-IgG and goat anti-rabbit IgG (H+L) Alexa Fluor488 and Early Endosomes-RFP BacMam. The merged color (yellow) is indicative of co-localization. Bar, 2 um. PIE cells stained with rabbit IgG-Alexa Fluor488 Isotype were used as controls.

    Journal: Veterinary Research

    Article Title: Immunobiotic lactic acid bacteria beneficially regulate immune response triggered by poly(I:C) in porcine intestinal epithelial cells

    doi: 10.1186/1297-9716-42-111

    Figure Lengend Snippet: Analysis of toll-like receptor 3 (TLR3) expression in porcine intestinal epithelial (PIE) cells . (A) Flow cytometric analysis of TLR3 in PIE cells. Histograms show flow cytometric analysis for TLR3 staining as follows: intracellular (open histogram), cell surface (broken lines) and isotype-matched controls (shaded histograms). The analysis of intracellular and cell surface expression of TLR3 is presented as the log of mean fluorescence intensity (MFI). The results represent three independent experiments. (B) Confocal microscopic analysis of the subcellular localization of TLR3 in PIE cells. Fixed and permeabilized cells were stained with anti-mouse TLR3(unlabeled) rabbit-IgG and goat anti-rabbit IgG (H+L) Alexa Fluor488 and Early Endosomes-RFP BacMam. The merged color (yellow) is indicative of co-localization. Bar, 2 um. PIE cells stained with rabbit IgG-Alexa Fluor488 Isotype were used as controls.

    Article Snippet: In addition the following secondary antibodies were used: goat anti-rabbit IgG (H+L) Alexa Fluor488 (A-11008, Invitrogen, Tokyo, Japan), goat anti-mouse IgG2a-PE (sc-3765, Santa Cruz Biotechnology), goat anti-mouse IgG1-PerCP/Cy5.5 (sc-45103, Santa Cruz Biotechnology) and streptavidin(PE) (12-4317-87, eBioscience, CA, USA).

    Techniques: Expressing, Flow Cytometry, Staining, Fluorescence

    Sub-cellular localization of target proteins. NC stained with negative serum was no green fluorescence, and TaSP was observed with green fluorescence on membrane of T. annulata shizonts as positive control (yellow arrow). TaCyp1 was mainly distributed around membrane of T. annulata shizonts (white arrow). Cell cytoskeleton stained with Alexa Fluor TM 594 Phalloidin and DNA stained with Hoechst 33342 were observed with red fluorescence and blue fluorescence, respectively, and target proteins stained with purified sera and Alexa Fluor 488 were observed with green fluorescence. The merge were fused images under the above three conditions.

    Journal: Frontiers in Microbiology

    Article Title: Theileria annulata Cyclophilin1 (TaCyp1) Interacts With Host Cell MED21

    doi: 10.3389/fmicb.2018.02973

    Figure Lengend Snippet: Sub-cellular localization of target proteins. NC stained with negative serum was no green fluorescence, and TaSP was observed with green fluorescence on membrane of T. annulata shizonts as positive control (yellow arrow). TaCyp1 was mainly distributed around membrane of T. annulata shizonts (white arrow). Cell cytoskeleton stained with Alexa Fluor TM 594 Phalloidin and DNA stained with Hoechst 33342 were observed with red fluorescence and blue fluorescence, respectively, and target proteins stained with purified sera and Alexa Fluor 488 were observed with green fluorescence. The merge were fused images under the above three conditions.

    Article Snippet: After washing in PBS, the coverslips were stained with Hoechst 33342 (1/2000, Invitrogen, United States) and goat anti-rabbit IgG (H+L) secondary antibody Alexa Fluor 488 (1/1000, Invitrogen, United States) in PBS 1% BSA for 1 h at 37°C.

    Techniques: Staining, Fluorescence, Positive Control, Purification

    Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by Alexa Fluor 647 goat anti rabbit

    Journal: Biochimica et biophysica acta

    Article Title: Specific inhibition of pathogenic receptor tyrosine kinase activation by its transmembrane domain

    doi: 10.1016/j.bbamem.2010.08.007

    Figure Lengend Snippet: Immunofluorescent staining of the TM domains in HEK 293 cells. (A). FGFR3 TM domain. B. FGFR3/A391E TM domain. (C). Neu TM domain. (D). Neu/V664E TM domain. Intact cells were stained with anti-VSV-G antibodies, followed by Alexa Fluor 647 goat anti rabbit

    Article Snippet: The secondary antibody used was Alexa Fluor 647 goat anti rabbit IgG (H+L) (Invitrogen, CA).

    Techniques: Staining

    In vitro binding studies of the peptide FnBPA5-Alexa-488 and the scrambled control (scraFnBPA5-Alexa-488) to soluble and fibrillar Fn. a Mechanosensitive binding of FnBPA5 was tested using relaxed (7% strain) and stretched (380% strain) fibers. Color-coded intensity ratio images of FnBPA5-Alexa488 divided by Fn-Cy5 of manually pulled Fn fibers of different mechanical state show higher binding to relaxed fibers than to stretched ones, leading to a higher FnBPA5/Fn ratio (representative images). Scale bar, 50 μm. b Normalized analysis of relaxed and stretched fibers showing a significant decrease in binding ratio of FnBPA5 from relaxed to stretched fibers. Data from 30 fibers from three independent experiments with error bars being standard deviations. p -value was obtained from a Student’s t test. c Schematic of manual fiber pulling, using a sharp pipette tip dipping into a Fn solution and pulling Fn fibers onto a flexible silicone sheet. d The binding of FnBPA5-Alexa-488 and scraFnBPA5-Alexa488 to soluble plasma Fn was determined using an anisotropy measurement (Methods). The results show a K d of 75 ± 8 nM for FnBPA5-Alexa488 and no specific binding for the scrambled control peptide. e Measurements of affinity of FnBPA5-Alexa488 to single relaxed Fn fibers showed a K d of 28 ± 6 nM. f Fluorescence images showing the binding of FnBPA5-Alexa488 and scraFnBPA5-Alexa488 to single relaxed Fn fibers (7% strain) using a previously described stretch assay 41 . For this experiment Cy5-labeled Fn was used (images on the left side). Scale bar, 50 μm. g The quantification of the fluorescence intensity showed a significant higher binding of FnBPA5-Alexa488 compared to the control. Data from 30 fibers from three independent experiments were analyzed. Shown error bars represent the standard deviation. p -value was obtained from a Student’s t test. h Human dermal fibroblast ECM was stained for Fn and incubated with FnBPA5-Alexa488 and the scrambled control peptide, respectively. Representative images show specific binding of FnBPA5-Alexa488 to Fn. Scale bar, 10 μm

    Journal: Nature Communications

    Article Title: Novel peptide probes to assess the tensional state of fibronectin fibers in cancer

    doi: 10.1038/s41467-017-01846-0

    Figure Lengend Snippet: In vitro binding studies of the peptide FnBPA5-Alexa-488 and the scrambled control (scraFnBPA5-Alexa-488) to soluble and fibrillar Fn. a Mechanosensitive binding of FnBPA5 was tested using relaxed (7% strain) and stretched (380% strain) fibers. Color-coded intensity ratio images of FnBPA5-Alexa488 divided by Fn-Cy5 of manually pulled Fn fibers of different mechanical state show higher binding to relaxed fibers than to stretched ones, leading to a higher FnBPA5/Fn ratio (representative images). Scale bar, 50 μm. b Normalized analysis of relaxed and stretched fibers showing a significant decrease in binding ratio of FnBPA5 from relaxed to stretched fibers. Data from 30 fibers from three independent experiments with error bars being standard deviations. p -value was obtained from a Student’s t test. c Schematic of manual fiber pulling, using a sharp pipette tip dipping into a Fn solution and pulling Fn fibers onto a flexible silicone sheet. d The binding of FnBPA5-Alexa-488 and scraFnBPA5-Alexa488 to soluble plasma Fn was determined using an anisotropy measurement (Methods). The results show a K d of 75 ± 8 nM for FnBPA5-Alexa488 and no specific binding for the scrambled control peptide. e Measurements of affinity of FnBPA5-Alexa488 to single relaxed Fn fibers showed a K d of 28 ± 6 nM. f Fluorescence images showing the binding of FnBPA5-Alexa488 and scraFnBPA5-Alexa488 to single relaxed Fn fibers (7% strain) using a previously described stretch assay 41 . For this experiment Cy5-labeled Fn was used (images on the left side). Scale bar, 50 μm. g The quantification of the fluorescence intensity showed a significant higher binding of FnBPA5-Alexa488 compared to the control. Data from 30 fibers from three independent experiments were analyzed. Shown error bars represent the standard deviation. p -value was obtained from a Student’s t test. h Human dermal fibroblast ECM was stained for Fn and incubated with FnBPA5-Alexa488 and the scrambled control peptide, respectively. Representative images show specific binding of FnBPA5-Alexa488 to Fn. Scale bar, 10 μm

    Article Snippet: Primary antibody solution was removed and samples were washed before incubation with secondary goat anti-rabbit Alexa-633 (A-21070, Invitrogen, 1:100 dilution) or goat anti rat Alexa 546 (A-11081, Invitrogen, 1:100 dilution) or goat anti-rabbit Alexa-488 (A-11034, Invitrogen, 1:100 dilution) antibody solution for 45 min. After another washing step, samples were mounted using Prolong Antifade Gold with or without DAPI (Invitrogen).

    Techniques: In Vitro, Binding Assay, Transferring, Fluorescence, Labeling, Standard Deviation, Staining, Incubation

    Post mortem tumor cryosection from prostate cancer (PC-3) xenografts. a Overview mosaic image of a whole PC-3 tumor tissue section co-stained with the peptide FnBPA5 Alexa-488 (red), together with polyclonal antibodies against Fn (green) and endothelial cell marker CD-31 (PECAM-1) (blue). Scale bar, 1 mm b Zoomed-in high-resolution z-projection images of different indicated regions showing superpositions of the stains FnBPA5 (red), fibronectin (green), and CD-31 (blue), as well as the mature collagen fibers in the same regions as visualized by SHG (cyan). Analysis of neighboring pixels (indicated by the small box showing the 5 × 5 pixel matrix surrounding each analyzed pixel) between antibody-stained Fn, FnBPA5 peptide and collagen bundles (SHG) showed a clear spatial proximity of FnBPA5 with Fn (99.9% of all FnBPA5 pixels have at least one neighboring Fn pixel). A total of 87% of pixels from mature collagen bundles were found to be in close proximity (within the 5 × 5 matrix of neighboring pixels) of FnBPA5-positive pixels (19 images analyzed). Scale bar, 20 μm. c Representative z-projection images of PC-3 tumor tissue sections stained for α-SMA and FnBPA5 and merged with nuclei stainings using DAPI. Analysis of neighboring pixels (indicated by the small box showing the 5 × 5 pixel matrix surrounding each analyzed pixel) reveals that 94% of the α-SMA-positive pixels are in close proximity (within the 5 × 5 matrix of neighboring pixels) to FnBPA5-positive regions (60 images analyzed). Lower thresholds were set based on individual channels to exclude unspecific pixels from the analysis, and a 5 × 5 matrix was used for the spatial proximity analysis of each pixel in 60 images, respectively, with each of the analyzed pixels being in the center (Methods section for more details). Scale bar, 20 μm

    Journal: Nature Communications

    Article Title: Novel peptide probes to assess the tensional state of fibronectin fibers in cancer

    doi: 10.1038/s41467-017-01846-0

    Figure Lengend Snippet: Post mortem tumor cryosection from prostate cancer (PC-3) xenografts. a Overview mosaic image of a whole PC-3 tumor tissue section co-stained with the peptide FnBPA5 Alexa-488 (red), together with polyclonal antibodies against Fn (green) and endothelial cell marker CD-31 (PECAM-1) (blue). Scale bar, 1 mm b Zoomed-in high-resolution z-projection images of different indicated regions showing superpositions of the stains FnBPA5 (red), fibronectin (green), and CD-31 (blue), as well as the mature collagen fibers in the same regions as visualized by SHG (cyan). Analysis of neighboring pixels (indicated by the small box showing the 5 × 5 pixel matrix surrounding each analyzed pixel) between antibody-stained Fn, FnBPA5 peptide and collagen bundles (SHG) showed a clear spatial proximity of FnBPA5 with Fn (99.9% of all FnBPA5 pixels have at least one neighboring Fn pixel). A total of 87% of pixels from mature collagen bundles were found to be in close proximity (within the 5 × 5 matrix of neighboring pixels) of FnBPA5-positive pixels (19 images analyzed). Scale bar, 20 μm. c Representative z-projection images of PC-3 tumor tissue sections stained for α-SMA and FnBPA5 and merged with nuclei stainings using DAPI. Analysis of neighboring pixels (indicated by the small box showing the 5 × 5 pixel matrix surrounding each analyzed pixel) reveals that 94% of the α-SMA-positive pixels are in close proximity (within the 5 × 5 matrix of neighboring pixels) to FnBPA5-positive regions (60 images analyzed). Lower thresholds were set based on individual channels to exclude unspecific pixels from the analysis, and a 5 × 5 matrix was used for the spatial proximity analysis of each pixel in 60 images, respectively, with each of the analyzed pixels being in the center (Methods section for more details). Scale bar, 20 μm

    Article Snippet: Primary antibody solution was removed and samples were washed before incubation with secondary goat anti-rabbit Alexa-633 (A-21070, Invitrogen, 1:100 dilution) or goat anti rat Alexa 546 (A-11081, Invitrogen, 1:100 dilution) or goat anti-rabbit Alexa-488 (A-11034, Invitrogen, 1:100 dilution) antibody solution for 45 min. After another washing step, samples were mounted using Prolong Antifade Gold with or without DAPI (Invitrogen).

    Techniques: Staining, Marker