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continuous–elution electrophoresis mini prep cell assembly system  (Bio-Rad)


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    Bio-Rad continuous–elution electrophoresis mini prep cell assembly system
    Continuous–Elution Electrophoresis Mini Prep Cell Assembly System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/continuous+elution+electrophoresis/Mini+Prep+Cell+Elution+Chamber+Top/pmc06368300-61-6-13
    Average 90 stars, based on 1 article reviews
    continuous–elution electrophoresis mini prep cell assembly system - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Purification:

    Article Title: Assessment of Virally Vectored Autoimmunity as a Biocontrol Strategy for Cane Toads
    Article Snippet: His 6 -tagged proteins were purified in the denatured state using Ni 2+ NTA agarose (Qiagen), washed via imidazole-containing steps (TBS+20, 30 or 40 mM imidazol) and eluted in TBS+500 mM imidazole. .. Size-based secondary purification was then achieved by continuous-elution electrophoresis (Model 491 Prep Cell, Bio-Rad). .. Globin proteins were dialysed against amphibian Ringers solution [4.89 g NaCl, 0.298 g KCl, 0.265 g CaCl 2 .2H 2 0, 0.197 g MgSO 4 .7H 2 0, 1.495 g NaHCO 3 , 0.127 g NaH 2 PO 4 .H 2 O and 1.982 g glucose per litre dH 2 O] overnight at 4°C and concentrations determined using the Bio-Rad Protein Assay.

    Article Title: Yersinia enterocolitica envelope proteins that are crossreactive with the thyrotropin receptor (TSHR) also have B-cell mitogenic activity.
    Article Snippet: Received 23 August 1995 Accepted 26 January 1996 Autoantibodies to the thyrotropin receptor (TSHR) have been shown to mediate the hyperthyroidism associated with Graves’ disease (GD).. A number of hypotheses have been proposed which link an infectious agent to the mechanism(s) involved in the induction of GD.. Several studies have suggested that the development of GD may be linked to infection with the enteric pathogen Yersinia enterocolitica.

    Article Title: Simian parvovirus infection: a potential zoonosis.
    Article Snippet: .. The fusion proteins were partially purified by continuous-elution electrophoresis (Model 491 Prep Cell; Bio-Rad) on an 8%-polyacrylamide separating gel. ..

    Electrophoresis:

    Article Title: Assessment of Virally Vectored Autoimmunity as a Biocontrol Strategy for Cane Toads
    Article Snippet: His 6 -tagged proteins were purified in the denatured state using Ni 2+ NTA agarose (Qiagen), washed via imidazole-containing steps (TBS+20, 30 or 40 mM imidazol) and eluted in TBS+500 mM imidazole. .. Size-based secondary purification was then achieved by continuous-elution electrophoresis (Model 491 Prep Cell, Bio-Rad). .. Globin proteins were dialysed against amphibian Ringers solution [4.89 g NaCl, 0.298 g KCl, 0.265 g CaCl 2 .2H 2 0, 0.197 g MgSO 4 .7H 2 0, 1.495 g NaHCO 3 , 0.127 g NaH 2 PO 4 .H 2 O and 1.982 g glucose per litre dH 2 O] overnight at 4°C and concentrations determined using the Bio-Rad Protein Assay.

    Article Title: Identification of Lactobacillus proteins with different recognition patterns between immune rabbit sera and nonimmune mice or human sera
    Article Snippet: .. Fig. 3 The SDS-PAGE profile of a separated proteins isolated from Lactobacillus johnsonii 151 in the presence of low molecular mass marker – 94, 67, 43, 30, 20.1, 14.4 kDa by continuous-elution electrophoresis (Prep-Cell apparatus Model 491 Bio-Rad). ..

    Article Title: Yersinia enterocolitica envelope proteins that are crossreactive with the thyrotropin receptor (TSHR) also have B-cell mitogenic activity.
    Article Snippet: Received 23 August 1995 Accepted 26 January 1996 Autoantibodies to the thyrotropin receptor (TSHR) have been shown to mediate the hyperthyroidism associated with Graves’ disease (GD).. A number of hypotheses have been proposed which link an infectious agent to the mechanism(s) involved in the induction of GD.. Several studies have suggested that the development of GD may be linked to infection with the enteric pathogen Yersinia enterocolitica.

    Article Title: Identification, purification, and characterization of a secretory serine protease in an Indian strain of Leishmania donovani.
    Article Snippet: An aprotinin sensitive serine protease was identified in the culture supernatant of the Indian strain of Leishmania donovani (MHOM/IN/1983/AG83).. The protease was subsequently purified and characterized.. The apparent molecular mass of the enzyme was 115 kDa in SDS-PAGE under non-reducing condition, while on reduction it showed a 56 kDa protein band indicating that the protease is a dimeric protein.

    Article Title: Preparative electrophoresis with on-column optical fiber monitoring and direct elution into a minimized volume.
    Article Snippet: A ‘‘column-format’’ preparative electrophoresis device which obviates the need for gel extraction or secondary electro-elution steps is described.. Separated biomolecules are continuously detected and eluted directly into a minimal volume of free solution for subsequent use.. An optical fiber allows the species of interest to be detected just prior to elution from the gel column, and a small collection volume is created by addition of an ion-exchange membrane near the end of the column.

    Article Title: Simian parvovirus infection: a potential zoonosis.
    Article Snippet: .. The fusion proteins were partially purified by continuous-elution electrophoresis (Model 491 Prep Cell; Bio-Rad) on an 8%-polyacrylamide separating gel. ..

    SDS Page:

    Article Title: Identification of Lactobacillus proteins with different recognition patterns between immune rabbit sera and nonimmune mice or human sera
    Article Snippet: .. Fig. 3 The SDS-PAGE profile of a separated proteins isolated from Lactobacillus johnsonii 151 in the presence of low molecular mass marker – 94, 67, 43, 30, 20.1, 14.4 kDa by continuous-elution electrophoresis (Prep-Cell apparatus Model 491 Bio-Rad). ..

    Isolation:

    Article Title: Identification of Lactobacillus proteins with different recognition patterns between immune rabbit sera and nonimmune mice or human sera
    Article Snippet: .. Fig. 3 The SDS-PAGE profile of a separated proteins isolated from Lactobacillus johnsonii 151 in the presence of low molecular mass marker – 94, 67, 43, 30, 20.1, 14.4 kDa by continuous-elution electrophoresis (Prep-Cell apparatus Model 491 Bio-Rad). ..

    Marker:

    Article Title: Identification of Lactobacillus proteins with different recognition patterns between immune rabbit sera and nonimmune mice or human sera
    Article Snippet: .. Fig. 3 The SDS-PAGE profile of a separated proteins isolated from Lactobacillus johnsonii 151 in the presence of low molecular mass marker – 94, 67, 43, 30, 20.1, 14.4 kDa by continuous-elution electrophoresis (Prep-Cell apparatus Model 491 Bio-Rad). ..

    Activity Assay:

    Article Title: Identification, purification, and characterization of a secretory serine protease in an Indian strain of Leishmania donovani.
    Article Snippet: An aprotinin sensitive serine protease was identified in the culture supernatant of the Indian strain of Leishmania donovani (MHOM/IN/1983/AG83).. The protease was subsequently purified and characterized.. The apparent molecular mass of the enzyme was 115 kDa in SDS-PAGE under non-reducing condition, while on reduction it showed a 56 kDa protein band indicating that the protease is a dimeric protein.

    Membrane:

    Article Title: Identification, purification, and characterization of a secretory serine protease in an Indian strain of Leishmania donovani.
    Article Snippet: An aprotinin sensitive serine protease was identified in the culture supernatant of the Indian strain of Leishmania donovani (MHOM/IN/1983/AG83).. The protease was subsequently purified and characterized.. The apparent molecular mass of the enzyme was 115 kDa in SDS-PAGE under non-reducing condition, while on reduction it showed a 56 kDa protein band indicating that the protease is a dimeric protein.

    Article Title: Preparative electrophoresis with on-column optical fiber monitoring and direct elution into a minimized volume.
    Article Snippet: A ‘‘column-format’’ preparative electrophoresis device which obviates the need for gel extraction or secondary electro-elution steps is described.. Separated biomolecules are continuously detected and eluted directly into a minimal volume of free solution for subsequent use.. An optical fiber allows the species of interest to be detected just prior to elution from the gel column, and a small collection volume is created by addition of an ion-exchange membrane near the end of the column.



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    Schistosoma mansoni venom allergen-like 9 (SmVAL9) undergoes transcriptional regulation throughout schistosome development, is maximally expressed in miracidia and is post-translationally modified in eggs. (A) DNA microarray analysis of SmVAL9 expression throughout 15 lifecycle stages. Histogram represents normalised mean fluorescent intensities + S.D. ( n = 3 replicates/lifecycle stage except adult female where n = 2) of SmVAL9 transcript abundance derived from oligonucleotide CD111828 as described previously . Dashed box encloses schistosome lifecycle stages where SmVAL9 is maximally expressed. Inset drawing represents SmVAL9 (Smp_176180) gene organisation (five exons – black boxes; four introns – black lines) and localisation of oligonucleotide CD111828 to exon 5 (SchistoGeneDB v5.1). (B) Expression and purification of recombinant SmVAL9 (rSmVAL9) in Escherichia coli cells. The majority of rSmVAL9 is found in insoluble inclusion bodies after induction, allowing preparatory cell <t>electrophoresis</t> (Prep. Cell) to concentrate and purify large amounts of the protein for murine immunisations and other downstream studies. (C) Anti-rSmVAL9 recognises the 19.3 kDa rSmVAL9 immunogen and a ∼25 kDa post-translationally modified, native SmVAL9 (nSmVAL9) from soluble egg antigen. Pre-bleed normal mouse serum does not recognise either protein or the BSA control.
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    Schistosoma mansoni venom allergen-like 9 (SmVAL9) undergoes transcriptional regulation throughout schistosome development, is maximally expressed in miracidia and is post-translationally modified in eggs. (A) DNA microarray analysis of SmVAL9 expression throughout 15 lifecycle stages. Histogram represents normalised mean fluorescent intensities + S.D. ( n = 3 replicates/lifecycle stage except adult female where n = 2) of SmVAL9 transcript abundance derived from oligonucleotide CD111828 as described previously . Dashed box encloses schistosome lifecycle stages where SmVAL9 is maximally expressed. Inset drawing represents SmVAL9 (Smp_176180) gene organisation (five exons – black boxes; four introns – black lines) and localisation of oligonucleotide CD111828 to exon 5 (SchistoGeneDB v5.1). (B) Expression and purification of recombinant SmVAL9 (rSmVAL9) in Escherichia coli cells. The majority of rSmVAL9 is found in insoluble inclusion bodies after induction, allowing preparatory cell <t>electrophoresis</t> (Prep. Cell) to concentrate and purify large amounts of the protein for murine immunisations and other downstream studies. (C) Anti-rSmVAL9 recognises the 19.3 kDa rSmVAL9 immunogen and a ∼25 kDa post-translationally modified, native SmVAL9 (nSmVAL9) from soluble egg antigen. Pre-bleed normal mouse serum does not recognise either protein or the BSA control.
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    Schistosoma mansoni venom allergen-like 9 (SmVAL9) undergoes transcriptional regulation throughout schistosome development, is maximally expressed in miracidia and is post-translationally modified in eggs. (A) DNA microarray analysis of SmVAL9 expression throughout 15 lifecycle stages. Histogram represents normalised mean fluorescent intensities + S.D. ( n = 3 replicates/lifecycle stage except adult female where n = 2) of SmVAL9 transcript abundance derived from oligonucleotide CD111828 as described previously . Dashed box encloses schistosome lifecycle stages where SmVAL9 is maximally expressed. Inset drawing represents SmVAL9 (Smp_176180) gene organisation (five exons – black boxes; four introns – black lines) and localisation of oligonucleotide CD111828 to exon 5 (SchistoGeneDB v5.1). (B) Expression and purification of recombinant SmVAL9 (rSmVAL9) in Escherichia coli cells. The majority of rSmVAL9 is found in insoluble inclusion bodies after induction, allowing preparatory cell <t>electrophoresis</t> (Prep. Cell) to concentrate and purify large amounts of the protein for murine immunisations and other downstream studies. (C) Anti-rSmVAL9 recognises the 19.3 kDa rSmVAL9 immunogen and a ∼25 kDa post-translationally modified, native SmVAL9 (nSmVAL9) from soluble egg antigen. Pre-bleed normal mouse serum does not recognise either protein or the BSA control.
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    Schistosoma mansoni venom allergen-like 9 (SmVAL9) undergoes transcriptional regulation throughout schistosome development, is maximally expressed in miracidia and is post-translationally modified in eggs. (A) DNA microarray analysis of SmVAL9 expression throughout 15 lifecycle stages. Histogram represents normalised mean fluorescent intensities + S.D. ( n = 3 replicates/lifecycle stage except adult female where n = 2) of SmVAL9 transcript abundance derived from oligonucleotide CD111828 as described previously . Dashed box encloses schistosome lifecycle stages where SmVAL9 is maximally expressed. Inset drawing represents SmVAL9 (Smp_176180) gene organisation (five exons – black boxes; four introns – black lines) and localisation of oligonucleotide CD111828 to exon 5 (SchistoGeneDB v5.1). (B) Expression and purification of recombinant SmVAL9 (rSmVAL9) in Escherichia coli cells. The majority of rSmVAL9 is found in insoluble inclusion bodies after induction, allowing preparatory cell <t>electrophoresis</t> (Prep. Cell) to concentrate and purify large amounts of the protein for murine immunisations and other downstream studies. (C) Anti-rSmVAL9 recognises the 19.3 kDa rSmVAL9 immunogen and a ∼25 kDa post-translationally modified, native SmVAL9 (nSmVAL9) from soluble egg antigen. Pre-bleed normal mouse serum does not recognise either protein or the BSA control.
    Preparative Continuous Elution Electrophoresis System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/continuous+elution+electrophoresis/Model+491+Prep+Cell/pm17289043-60-18-25
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    Schistosoma mansoni venom allergen-like 9 (SmVAL9) undergoes transcriptional regulation throughout schistosome development, is maximally expressed in miracidia and is post-translationally modified in eggs. (A) DNA microarray analysis of SmVAL9 expression throughout 15 lifecycle stages. Histogram represents normalised mean fluorescent intensities + S.D. ( n = 3 replicates/lifecycle stage except adult female where n = 2) of SmVAL9 transcript abundance derived from oligonucleotide CD111828 as described previously . Dashed box encloses schistosome lifecycle stages where SmVAL9 is maximally expressed. Inset drawing represents SmVAL9 (Smp_176180) gene organisation (five exons – black boxes; four introns – black lines) and localisation of oligonucleotide CD111828 to exon 5 (SchistoGeneDB v5.1). (B) Expression and purification of recombinant SmVAL9 (rSmVAL9) in Escherichia coli cells. The majority of rSmVAL9 is found in insoluble inclusion bodies after induction, allowing preparatory cell electrophoresis (Prep. Cell) to concentrate and purify large amounts of the protein for murine immunisations and other downstream studies. (C) Anti-rSmVAL9 recognises the 19.3 kDa rSmVAL9 immunogen and a ∼25 kDa post-translationally modified, native SmVAL9 (nSmVAL9) from soluble egg antigen. Pre-bleed normal mouse serum does not recognise either protein or the BSA control.

    Journal: International Journal for Parasitology

    Article Title: Excreted/secreted Schistosoma mansoni venom allergen-like 9 (SmVAL9) modulates host extracellular matrix remodelling gene expression

    doi: 10.1016/j.ijpara.2014.04.002

    Figure Lengend Snippet: Schistosoma mansoni venom allergen-like 9 (SmVAL9) undergoes transcriptional regulation throughout schistosome development, is maximally expressed in miracidia and is post-translationally modified in eggs. (A) DNA microarray analysis of SmVAL9 expression throughout 15 lifecycle stages. Histogram represents normalised mean fluorescent intensities + S.D. ( n = 3 replicates/lifecycle stage except adult female where n = 2) of SmVAL9 transcript abundance derived from oligonucleotide CD111828 as described previously . Dashed box encloses schistosome lifecycle stages where SmVAL9 is maximally expressed. Inset drawing represents SmVAL9 (Smp_176180) gene organisation (five exons – black boxes; four introns – black lines) and localisation of oligonucleotide CD111828 to exon 5 (SchistoGeneDB v5.1). (B) Expression and purification of recombinant SmVAL9 (rSmVAL9) in Escherichia coli cells. The majority of rSmVAL9 is found in insoluble inclusion bodies after induction, allowing preparatory cell electrophoresis (Prep. Cell) to concentrate and purify large amounts of the protein for murine immunisations and other downstream studies. (C) Anti-rSmVAL9 recognises the 19.3 kDa rSmVAL9 immunogen and a ∼25 kDa post-translationally modified, native SmVAL9 (nSmVAL9) from soluble egg antigen. Pre-bleed normal mouse serum does not recognise either protein or the BSA control.

    Article Snippet: Purification of rSmVAL9 was carried out by size fractionation using a continuous elution electrophoresis apparatus (Model 491 Prep Cell; Bio-Rad, UK), following the manufacturer’s instructions.

    Techniques: Modification, Microarray, Expressing, Derivative Assay, Purification, Recombinant, Electrophoresis, Control