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igepal ca360  (Thermo Fisher)


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    Structured Review

    Thermo Fisher igepal ca360
    Igepal Ca360, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/igepal+ca+630/IGEPAL%26mid%3Br+CA-630/10__1016_slash_j__apsb__2026__06__031-205-26-34
    Average 95 stars, based on 1 article reviews
    igepal ca360 - by Bioz Stars, 2026-10
    95/100 stars

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    Related Articles

    Protease Inhibitor:

    Article Title: LAMP1 and LAMP2A localise to axonal organelles with distinct motility dynamics and partially overlapping molecular signatures in human neurons
    Article Snippet: .. Cells were lysed in 50 mM Tris-HCl pH 7.5, 100 mM NaCl, 1% Igepal CA-630, 0.1% SDS and 0.5% sodium deoxycholate containing 1× Halt protease inhibitor cocktail with EDTA (Thermo Fisher Scientific) for 15 min at 4°C. ..

    Article Title: Pathogenic PTCD1 variants cause mitochondrial protein aggregation and cardiomyopathy
    Article Snippet: .. Each sample was resuspended in 0.5 mL of RIPA buffer containing 1% Igepal CA-630, 1.5% Triton X-100, 0.5% sodium deoxycholate, 0.1% SDS, 10 mM β-mercaptoethanol, 1 mM phenylmethylsulfonyl fluoride (PMSF), and 1× Ethylenediaminetetraacetic acid (EDTA) free protease inhibitor cocktail (Pierce) and incubated on ice for 45 min. ..

    Article Title: Intrinsically disordered regions stimulate concentration of small nucleolar ribonucleoproteins and formation of Cajal bodies and nucleoli
    Article Snippet: .. Briefly, cell pellets were resuspended in 1/20 culture volume of lysis buffer (50 mM Tris at pH 7.9, 100 mM KCl, 0.5% [w/v] Igepal CA-630, 0.2 mM EDTA, 10 mM imidazole, 1× EDTA-free Pierce protease inhibitor cocktail) and sonicated four times for 20 sec, and the lysate was cleared by sedimentation at 34,000 g for 20 min at 4°C and loaded onto a nickel-NTA resin column. ..

    Extraction:

    Article Title: Durable protection against SIV challenge by adeno-associated virus delivery of Env-specific antibodies
    Article Snippet: .. Upon thawing on ice, the adhered material was manually homogenized with the weck itself in the same tube with 0.3 ml of the freshly prepared ice-cold extraction buffer consisting of 1X PBS, 2 mM EDTA, 0.5% Igepal CA-630, 5 mg/ml BSA, 5 mM sodium azide and 1X protease inhibitors cocktail (ThermoFisher, cat. 87785) and incubated on ice for 15 min. ..

    Incubation:

    Article Title: Durable protection against SIV challenge by adeno-associated virus delivery of Env-specific antibodies
    Article Snippet: .. Upon thawing on ice, the adhered material was manually homogenized with the weck itself in the same tube with 0.3 ml of the freshly prepared ice-cold extraction buffer consisting of 1X PBS, 2 mM EDTA, 0.5% Igepal CA-630, 5 mg/ml BSA, 5 mM sodium azide and 1X protease inhibitors cocktail (ThermoFisher, cat. 87785) and incubated on ice for 15 min. ..

    Article Title: Pathogenic PTCD1 variants cause mitochondrial protein aggregation and cardiomyopathy
    Article Snippet: .. Each sample was resuspended in 0.5 mL of RIPA buffer containing 1% Igepal CA-630, 1.5% Triton X-100, 0.5% sodium deoxycholate, 0.1% SDS, 10 mM β-mercaptoethanol, 1 mM phenylmethylsulfonyl fluoride (PMSF), and 1× Ethylenediaminetetraacetic acid (EDTA) free protease inhibitor cocktail (Pierce) and incubated on ice for 45 min. ..

    Isolation:

    Article Title: Single-molecule dynamics of the TRiC chaperonin system in vivo.
    Article Snippet: .. Lysate was digested with 500 U per 1 mg RNase I (Lucigen) at 4 °C for 1 h. Ribosome pellets were isolated using a 25% sucrose cushion prepared in lysis buffer without IGEPAL CA-630 and supplemented with 20 U ml−1 SUPERase*In (Invitrogen). .. Samples were centrifuged at 55,000 rpm in a SW 55 Ti rotor (Beckman Coulter) for 1 h at 4 °C.

    Lysis:

    Article Title: Single-molecule dynamics of the TRiC chaperonin system in vivo.
    Article Snippet: .. Lysate was digested with 500 U per 1 mg RNase I (Lucigen) at 4 °C for 1 h. Ribosome pellets were isolated using a 25% sucrose cushion prepared in lysis buffer without IGEPAL CA-630 and supplemented with 20 U ml−1 SUPERase*In (Invitrogen). .. Samples were centrifuged at 55,000 rpm in a SW 55 Ti rotor (Beckman Coulter) for 1 h at 4 °C.

    Article Title: Substitution of the SEMA3A basic domain with the VEGF 165 heparin-binding domain enhances anti-angiogenic potency in ovo.
    Article Snippet: .. After the last washing step, the beads were resuspended into 4x Laemmli buffer and protein complexes were denatured by heating samples at 95°C for 5 min. For whole-cell extract (WCE) preparation, transfected cells were lysed in RIPA lysis buffer (50 mM TrisHCl (pH 7.5), 150 mM NaCl, 1% Igepal CA-630, 0.5% sodium deoxycholate, 0.1% SDS) supplemented with the Halt Protease and Phosphatase Inhibitor Cocktail (Thermo Fisher Scientific Inc. cat. No. 78440) and centrifuged 40 min at 12.000 × g at 4°C. ..

    Article Title: Intrinsically disordered regions stimulate concentration of small nucleolar ribonucleoproteins and formation of Cajal bodies and nucleoli
    Article Snippet: .. Briefly, cell pellets were resuspended in 1/20 culture volume of lysis buffer (50 mM Tris at pH 7.9, 100 mM KCl, 0.5% [w/v] Igepal CA-630, 0.2 mM EDTA, 10 mM imidazole, 1× EDTA-free Pierce protease inhibitor cocktail) and sonicated four times for 20 sec, and the lysate was cleared by sedimentation at 34,000 g for 20 min at 4°C and loaded onto a nickel-NTA resin column. ..

    Transfection:

    Article Title: Substitution of the SEMA3A basic domain with the VEGF 165 heparin-binding domain enhances anti-angiogenic potency in ovo.
    Article Snippet: .. After the last washing step, the beads were resuspended into 4x Laemmli buffer and protein complexes were denatured by heating samples at 95°C for 5 min. For whole-cell extract (WCE) preparation, transfected cells were lysed in RIPA lysis buffer (50 mM TrisHCl (pH 7.5), 150 mM NaCl, 1% Igepal CA-630, 0.5% sodium deoxycholate, 0.1% SDS) supplemented with the Halt Protease and Phosphatase Inhibitor Cocktail (Thermo Fisher Scientific Inc. cat. No. 78440) and centrifuged 40 min at 12.000 × g at 4°C. ..

    Sonication:

    Article Title: Intrinsically disordered regions stimulate concentration of small nucleolar ribonucleoproteins and formation of Cajal bodies and nucleoli
    Article Snippet: .. Briefly, cell pellets were resuspended in 1/20 culture volume of lysis buffer (50 mM Tris at pH 7.9, 100 mM KCl, 0.5% [w/v] Igepal CA-630, 0.2 mM EDTA, 10 mM imidazole, 1× EDTA-free Pierce protease inhibitor cocktail) and sonicated four times for 20 sec, and the lysate was cleared by sedimentation at 34,000 g for 20 min at 4°C and loaded onto a nickel-NTA resin column. ..

    Sedimentation:

    Article Title: Intrinsically disordered regions stimulate concentration of small nucleolar ribonucleoproteins and formation of Cajal bodies and nucleoli
    Article Snippet: .. Briefly, cell pellets were resuspended in 1/20 culture volume of lysis buffer (50 mM Tris at pH 7.9, 100 mM KCl, 0.5% [w/v] Igepal CA-630, 0.2 mM EDTA, 10 mM imidazole, 1× EDTA-free Pierce protease inhibitor cocktail) and sonicated four times for 20 sec, and the lysate was cleared by sedimentation at 34,000 g for 20 min at 4°C and loaded onto a nickel-NTA resin column. ..



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    <t>Cryo-EM</t> structure of raiA motif RNA from Nocardioides sp. Iso805N ( Ns-raiA ) at 3.0 Å resolution. ( A ) Cryo-EM density map of Ns-raiA shown in three different views. Individual stem–loops are color-coded as indicated. Pyramid diagrams indicate the orientation of Ns-raiA structure. ( B ) Overlaid cryo-EM densities and models of P1c, P3a, PK1, P5, P6, and P8.
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    <t>Cryo-EM</t> structure of raiA motif RNA from Nocardioides sp. Iso805N ( Ns-raiA ) at 3.0 Å resolution. ( A ) Cryo-EM density map of Ns-raiA shown in three different views. Individual stem–loops are color-coded as indicated. Pyramid diagrams indicate the orientation of Ns-raiA structure. ( B ) Overlaid cryo-EM densities and models of P1c, P3a, PK1, P5, P6, and P8.
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    Image Search Results


    Cryo-EM structure of raiA motif RNA from Nocardioides sp. Iso805N ( Ns-raiA ) at 3.0 Å resolution. ( A ) Cryo-EM density map of Ns-raiA shown in three different views. Individual stem–loops are color-coded as indicated. Pyramid diagrams indicate the orientation of Ns-raiA structure. ( B ) Overlaid cryo-EM densities and models of P1c, P3a, PK1, P5, P6, and P8.

    Journal: Nucleic Acids Research

    Article Title: Cryo-EM structures reveal a conserved architecture for raiA noncoding RNA

    doi: 10.1093/nar/gkag185

    Figure Lengend Snippet: Cryo-EM structure of raiA motif RNA from Nocardioides sp. Iso805N ( Ns-raiA ) at 3.0 Å resolution. ( A ) Cryo-EM density map of Ns-raiA shown in three different views. Individual stem–loops are color-coded as indicated. Pyramid diagrams indicate the orientation of Ns-raiA structure. ( B ) Overlaid cryo-EM densities and models of P1c, P3a, PK1, P5, P6, and P8.

    Article Snippet: RNA samples were diluted to ∼30 μM in EM buffer (20 mM HEPES–HCl, pH 7.5, 50 mM KCl, 10 mM MgCl 2 , 0.05% Igepal CA-630) before preparing cryo-EM samples.

    Techniques: Cryo-EM Sample Prep

    Tertiary and secondary structures of Ns-raiA . ( A ) Atomic model of Ns-raiA shown in three different views. Individual stem–loops are color-coded as indicated. Nucleotides in the conserved UU AGAC GUAA linker connecting PK1 and P6 not resolved in the cryo-EM map are shown as a dotted line. Secondary structures of Ns-raiA are shown in the canonical layout ( B ) as proposed in or in a layout that more closely reflects the tertiary structure ( C ). The nucleotides are colored as in the structure in panel (A). Black arrowheads indicate the backbone direction. Non-Watson–Crick base pairs are indicated with Leontis–Westhof nomenclature symbols (inset) .

    Journal: Nucleic Acids Research

    Article Title: Cryo-EM structures reveal a conserved architecture for raiA noncoding RNA

    doi: 10.1093/nar/gkag185

    Figure Lengend Snippet: Tertiary and secondary structures of Ns-raiA . ( A ) Atomic model of Ns-raiA shown in three different views. Individual stem–loops are color-coded as indicated. Nucleotides in the conserved UU AGAC GUAA linker connecting PK1 and P6 not resolved in the cryo-EM map are shown as a dotted line. Secondary structures of Ns-raiA are shown in the canonical layout ( B ) as proposed in or in a layout that more closely reflects the tertiary structure ( C ). The nucleotides are colored as in the structure in panel (A). Black arrowheads indicate the backbone direction. Non-Watson–Crick base pairs are indicated with Leontis–Westhof nomenclature symbols (inset) .

    Article Snippet: RNA samples were diluted to ∼30 μM in EM buffer (20 mM HEPES–HCl, pH 7.5, 50 mM KCl, 10 mM MgCl 2 , 0.05% Igepal CA-630) before preparing cryo-EM samples.

    Techniques: Cryo-EM Sample Prep

    Structural comparison of raiA motif RNAs from Nocardioides sp. Iso805N ( Ns-raiA ) , Clostridium acetobutylicum ( Ca-raiA ), and Mogibacterium pumilum ( Mp-raiA ). Cryo-EM density map (left) and atomic model (right) of Ns-raiA ( A ), Ca-raiA ( B ), and Mp-raiA ( C ). The absence of P2 and distal P7 in Ca-raiA and Mp-raiA , and the absence of P8 in Mp-raiA are indicated by dashed lines. Sequence and secondary structure of Ca-raiA ( D ), and Mp-raiA ( E ). Black arrowheads indicate the backbone direction. Non-Watson–Crick base pairs are labeled as indicated. Insets show the schematics of J1 regions. Zoom-in views of the P1c-P2-P3a junction in Ns-raiA ( F ), and the P1c-P3a junctions in Ca-raiA ( G ) and Mp-raiA ( H ), highlighting the GAA(A) tetraloop fold, shown in the same orientation. Zoom-in views of the interface of P8 and PK1 stems in Ns-raiA ( I ) and Ca-raiA ( J ), and the PK1 stem in Mp-raiA ( K ), shown in the same orientation.

    Journal: Nucleic Acids Research

    Article Title: Cryo-EM structures reveal a conserved architecture for raiA noncoding RNA

    doi: 10.1093/nar/gkag185

    Figure Lengend Snippet: Structural comparison of raiA motif RNAs from Nocardioides sp. Iso805N ( Ns-raiA ) , Clostridium acetobutylicum ( Ca-raiA ), and Mogibacterium pumilum ( Mp-raiA ). Cryo-EM density map (left) and atomic model (right) of Ns-raiA ( A ), Ca-raiA ( B ), and Mp-raiA ( C ). The absence of P2 and distal P7 in Ca-raiA and Mp-raiA , and the absence of P8 in Mp-raiA are indicated by dashed lines. Sequence and secondary structure of Ca-raiA ( D ), and Mp-raiA ( E ). Black arrowheads indicate the backbone direction. Non-Watson–Crick base pairs are labeled as indicated. Insets show the schematics of J1 regions. Zoom-in views of the P1c-P2-P3a junction in Ns-raiA ( F ), and the P1c-P3a junctions in Ca-raiA ( G ) and Mp-raiA ( H ), highlighting the GAA(A) tetraloop fold, shown in the same orientation. Zoom-in views of the interface of P8 and PK1 stems in Ns-raiA ( I ) and Ca-raiA ( J ), and the PK1 stem in Mp-raiA ( K ), shown in the same orientation.

    Article Snippet: RNA samples were diluted to ∼30 μM in EM buffer (20 mM HEPES–HCl, pH 7.5, 50 mM KCl, 10 mM MgCl 2 , 0.05% Igepal CA-630) before preparing cryo-EM samples.

    Techniques: Comparison, Cryo-EM Sample Prep, Sequencing, Labeling

    Structural details of P1 and its interactions with the core. ( A ) Overall view of P1 (shown as colored ribbon for backbone and filled bases and sugars) and its position relative to the core (colored ribbon) in the structure of Ns-raiA . Other stems are shown as white ribbons. ( B ) Close-up view of the interface between P1 and the core, in dashed box region in panel (A). The two insert panels highlight the long-range A81-G240-G10 stacking and the G10-G14-C242 base triple, respectively. ( C ) Secondary structure representation of the region shown in panel (B). Long-range stacking interactions are indicated by gray dashed lines, while base triple interactions are marked with green lines. ( D ) Representative 2D class averages of To-raiA (left) and enlargement with structure features labeled (right). ( E ) Cryo-EM density map and ribbon model of To-raiA . ( F ) Sequence conservation of raiA motif RNA mapped onto the Ns-raiA structure. View on left highlights conservation of P1 and on right conservation of the core. Conservation scores were calculated using the ConSurf server .

    Journal: Nucleic Acids Research

    Article Title: Cryo-EM structures reveal a conserved architecture for raiA noncoding RNA

    doi: 10.1093/nar/gkag185

    Figure Lengend Snippet: Structural details of P1 and its interactions with the core. ( A ) Overall view of P1 (shown as colored ribbon for backbone and filled bases and sugars) and its position relative to the core (colored ribbon) in the structure of Ns-raiA . Other stems are shown as white ribbons. ( B ) Close-up view of the interface between P1 and the core, in dashed box region in panel (A). The two insert panels highlight the long-range A81-G240-G10 stacking and the G10-G14-C242 base triple, respectively. ( C ) Secondary structure representation of the region shown in panel (B). Long-range stacking interactions are indicated by gray dashed lines, while base triple interactions are marked with green lines. ( D ) Representative 2D class averages of To-raiA (left) and enlargement with structure features labeled (right). ( E ) Cryo-EM density map and ribbon model of To-raiA . ( F ) Sequence conservation of raiA motif RNA mapped onto the Ns-raiA structure. View on left highlights conservation of P1 and on right conservation of the core. Conservation scores were calculated using the ConSurf server .

    Article Snippet: RNA samples were diluted to ∼30 μM in EM buffer (20 mM HEPES–HCl, pH 7.5, 50 mM KCl, 10 mM MgCl 2 , 0.05% Igepal CA-630) before preparing cryo-EM samples.

    Techniques: Labeling, Cryo-EM Sample Prep, Sequencing