e8200  (New England Biolabs)


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    Name:
    pMAL Protein Fusion and Purification System
    Description:
    pMAL Protein Fusion and Purification System
    Catalog Number:
    e8200s
    Price:
    677
    Category:
    E coli Protein Expression Kits
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    Structured Review

    New England Biolabs e8200
    pMAL Protein Fusion and Purification System
    pMAL Protein Fusion and Purification System
    https://www.bioz.com/result/e8200/product/New England Biolabs
    Average 99 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    e8200 - by Bioz Stars, 2020-07
    99/100 stars

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    Related Articles

    Affinity Chromatography:

    Article Title: The Coenzyme A Biosynthetic Enzyme Phosphopantetheine Adenylyltransferase Plays a Crucial Role in Plant Growth, Salt/Osmotic Stress Resistance, and Seed Lipid Storage 1The Coenzyme A Biosynthetic Enzyme Phosphopantetheine Adenylyltransferase Plays a Crucial Role in Plant Growth, Salt/Osmotic Stress Resistance, and Seed Lipid Storage 1 [W]
    Article Snippet: .. Expression of recombinant MBP-PPAT was induced with 1 m m isopropylthio- β -galactoside in Escherichia coli DH5a cells and the fusion protein was purified by amylose affinity chromatography according to the manufacturer's instructions (New England Biolabs). ..

    Article Title: Interaction of the putative tyrosine recombinases RipX (UU145), XerC (UU222), and CodV (UU529) of Ureaplasma parvum serovar 3 with specific DNA
    Article Snippet: .. The soluble fractions of cell lysates were loaded onto 5 mL amylose, and fusion proteins were purified as described by the manufacturer (NEB; pMAL™ Protein Fusion and Purification System (Expression and Purification of Proteins and Cloned Genes) Instruction Manual, #E8000S Version 5.3 11/07, Affinity Chromatography, Method I). .. Electrophoretic mobility shift assay Electrophoretic mobility shift assay (EMSA) analysis was carried out with the LightShift® Chemoluminescent EMSA Kit (PIERCE) according to the product manual.

    Purification:

    Article Title: The Coenzyme A Biosynthetic Enzyme Phosphopantetheine Adenylyltransferase Plays a Crucial Role in Plant Growth, Salt/Osmotic Stress Resistance, and Seed Lipid Storage 1The Coenzyme A Biosynthetic Enzyme Phosphopantetheine Adenylyltransferase Plays a Crucial Role in Plant Growth, Salt/Osmotic Stress Resistance, and Seed Lipid Storage 1 [W]
    Article Snippet: .. Expression of recombinant MBP-PPAT was induced with 1 m m isopropylthio- β -galactoside in Escherichia coli DH5a cells and the fusion protein was purified by amylose affinity chromatography according to the manufacturer's instructions (New England Biolabs). ..

    Article Title: Molecular and functional insights into a novel teleost malectin from big-belly seahorse Hippocampus abdominalis
    Article Snippet: .. 3.4 Overexpression and purification of rHaMLEC rHaMLEC was overexpressed in E. coli BL21(DE3) cells and purified using a pMAL protein fusion and purification system (New England Biolabs, USA). .. The following samples were analyzed by SDS-PAGE throughout the purification steps: total protein extract after sonication, supernatant after centrifugation, and purified protein ( ).

    Article Title: The Integrative Conjugative Element (ICE) of Mycoplasma agalactiae: Key Elements Involved in Horizontal Dissemination and Influence of Coresident ICEs
    Article Snippet: .. The anti-CDS14 lipoprotein rabbit serum was produced by animal immunization with a recombinant CDS14 protein (pMAL protein fusion and purification system; New England Biolabs). ..

    Article Title: Interaction of the putative tyrosine recombinases RipX (UU145), XerC (UU222), and CodV (UU529) of Ureaplasma parvum serovar 3 with specific DNA
    Article Snippet: .. The soluble fractions of cell lysates were loaded onto 5 mL amylose, and fusion proteins were purified as described by the manufacturer (NEB; pMAL™ Protein Fusion and Purification System (Expression and Purification of Proteins and Cloned Genes) Instruction Manual, #E8000S Version 5.3 11/07, Affinity Chromatography, Method I). .. Electrophoretic mobility shift assay Electrophoretic mobility shift assay (EMSA) analysis was carried out with the LightShift® Chemoluminescent EMSA Kit (PIERCE) according to the product manual.

    Article Title: Characterization of Mannitol-2-Dehydrogenase in Saccharina japonica: Evidence for a New Polyol-Specific Long-Chain Dehydrogenases/Reductase
    Article Snippet: .. Recombinant Expression and Purification of SjM2DH pMAL Protein Fusion & Purification System (NEB #E8200S) was applied to perform the prokaryotic expression of SjM2DH in E. coli . .. The restriction sites of SjM2DH sequence were analyzed with the on-line tool WatCut ( http://watcut.uwaterloo.ca/watcut/watcut/template.php ).

    Article Title: Structural and functional evaluation of de novo-designed, two-component nanoparticle carriers for HIV Env trimer immunogens
    Article Snippet: .. Assembly component expression and purification E coli expression system was used for assembly component production (T33_dn2B, T33_dn10B and I53_dn5A). .. BL21-DE3 cells (NEB) were transformed with pET28b (+) vector carrying the appropriate gene with a C-terminal His-tag.

    Produced:

    Article Title: The Integrative Conjugative Element (ICE) of Mycoplasma agalactiae: Key Elements Involved in Horizontal Dissemination and Influence of Coresident ICEs
    Article Snippet: .. The anti-CDS14 lipoprotein rabbit serum was produced by animal immunization with a recombinant CDS14 protein (pMAL protein fusion and purification system; New England Biolabs). ..

    Expressing:

    Article Title: The Coenzyme A Biosynthetic Enzyme Phosphopantetheine Adenylyltransferase Plays a Crucial Role in Plant Growth, Salt/Osmotic Stress Resistance, and Seed Lipid Storage 1The Coenzyme A Biosynthetic Enzyme Phosphopantetheine Adenylyltransferase Plays a Crucial Role in Plant Growth, Salt/Osmotic Stress Resistance, and Seed Lipid Storage 1 [W]
    Article Snippet: .. Expression of recombinant MBP-PPAT was induced with 1 m m isopropylthio- β -galactoside in Escherichia coli DH5a cells and the fusion protein was purified by amylose affinity chromatography according to the manufacturer's instructions (New England Biolabs). ..

    Article Title: Interaction of the putative tyrosine recombinases RipX (UU145), XerC (UU222), and CodV (UU529) of Ureaplasma parvum serovar 3 with specific DNA
    Article Snippet: .. The soluble fractions of cell lysates were loaded onto 5 mL amylose, and fusion proteins were purified as described by the manufacturer (NEB; pMAL™ Protein Fusion and Purification System (Expression and Purification of Proteins and Cloned Genes) Instruction Manual, #E8000S Version 5.3 11/07, Affinity Chromatography, Method I). .. Electrophoretic mobility shift assay Electrophoretic mobility shift assay (EMSA) analysis was carried out with the LightShift® Chemoluminescent EMSA Kit (PIERCE) according to the product manual.

    Article Title: Characterization of Mannitol-2-Dehydrogenase in Saccharina japonica: Evidence for a New Polyol-Specific Long-Chain Dehydrogenases/Reductase
    Article Snippet: .. Recombinant Expression and Purification of SjM2DH pMAL Protein Fusion & Purification System (NEB #E8200S) was applied to perform the prokaryotic expression of SjM2DH in E. coli . .. The restriction sites of SjM2DH sequence were analyzed with the on-line tool WatCut ( http://watcut.uwaterloo.ca/watcut/watcut/template.php ).

    Article Title: Structural and functional evaluation of de novo-designed, two-component nanoparticle carriers for HIV Env trimer immunogens
    Article Snippet: .. Assembly component expression and purification E coli expression system was used for assembly component production (T33_dn2B, T33_dn10B and I53_dn5A). .. BL21-DE3 cells (NEB) were transformed with pET28b (+) vector carrying the appropriate gene with a C-terminal His-tag.

    Recombinant:

    Article Title: The Coenzyme A Biosynthetic Enzyme Phosphopantetheine Adenylyltransferase Plays a Crucial Role in Plant Growth, Salt/Osmotic Stress Resistance, and Seed Lipid Storage 1The Coenzyme A Biosynthetic Enzyme Phosphopantetheine Adenylyltransferase Plays a Crucial Role in Plant Growth, Salt/Osmotic Stress Resistance, and Seed Lipid Storage 1 [W]
    Article Snippet: .. Expression of recombinant MBP-PPAT was induced with 1 m m isopropylthio- β -galactoside in Escherichia coli DH5a cells and the fusion protein was purified by amylose affinity chromatography according to the manufacturer's instructions (New England Biolabs). ..

    Article Title: The Integrative Conjugative Element (ICE) of Mycoplasma agalactiae: Key Elements Involved in Horizontal Dissemination and Influence of Coresident ICEs
    Article Snippet: .. The anti-CDS14 lipoprotein rabbit serum was produced by animal immunization with a recombinant CDS14 protein (pMAL protein fusion and purification system; New England Biolabs). ..

    Article Title: Characterization of Mannitol-2-Dehydrogenase in Saccharina japonica: Evidence for a New Polyol-Specific Long-Chain Dehydrogenases/Reductase
    Article Snippet: .. Recombinant Expression and Purification of SjM2DH pMAL Protein Fusion & Purification System (NEB #E8200S) was applied to perform the prokaryotic expression of SjM2DH in E. coli . .. The restriction sites of SjM2DH sequence were analyzed with the on-line tool WatCut ( http://watcut.uwaterloo.ca/watcut/watcut/template.php ).

    Over Expression:

    Article Title: Molecular and functional insights into a novel teleost malectin from big-belly seahorse Hippocampus abdominalis
    Article Snippet: .. 3.4 Overexpression and purification of rHaMLEC rHaMLEC was overexpressed in E. coli BL21(DE3) cells and purified using a pMAL protein fusion and purification system (New England Biolabs, USA). .. The following samples were analyzed by SDS-PAGE throughout the purification steps: total protein extract after sonication, supernatant after centrifugation, and purified protein ( ).

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  • 99
    New England Biolabs pmal protein fusion
    SDS-PAGE validation of purified <t>rHaMLEC</t> fusion protein. Lane 1 = protein size marker (Enzynomics-Korea); Lane 2 = supernatant from E. coli BL21 (DE3) transfected with <t>rHaMLEC-pMAL-c5X;</t> Lane 3 = total extract from IPTG-induced E. coli BL21 (DE3) cells transfected with rHaMLEC-pMAL-c5X; Lane 4 = supernatant of IPTG-induced E. coli BL21 (DE3) cells transfected with rHaMLEC-pMAL-c5X; Lane 5 = purified rHaMLEC-MBP fusion protein.
    Pmal Protein Fusion, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pmal protein fusion/product/New England Biolabs
    Average 99 stars, based on 45 article reviews
    Price from $9.99 to $1999.99
    pmal protein fusion - by Bioz Stars, 2020-07
    99/100 stars
      Buy from Supplier

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    SDS-PAGE validation of purified rHaMLEC fusion protein. Lane 1 = protein size marker (Enzynomics-Korea); Lane 2 = supernatant from E. coli BL21 (DE3) transfected with rHaMLEC-pMAL-c5X; Lane 3 = total extract from IPTG-induced E. coli BL21 (DE3) cells transfected with rHaMLEC-pMAL-c5X; Lane 4 = supernatant of IPTG-induced E. coli BL21 (DE3) cells transfected with rHaMLEC-pMAL-c5X; Lane 5 = purified rHaMLEC-MBP fusion protein.

    Journal: Fish & Shellfish Immunology

    Article Title: Molecular and functional insights into a novel teleost malectin from big-belly seahorse Hippocampus abdominalis

    doi: 10.1016/j.fsi.2020.02.044

    Figure Lengend Snippet: SDS-PAGE validation of purified rHaMLEC fusion protein. Lane 1 = protein size marker (Enzynomics-Korea); Lane 2 = supernatant from E. coli BL21 (DE3) transfected with rHaMLEC-pMAL-c5X; Lane 3 = total extract from IPTG-induced E. coli BL21 (DE3) cells transfected with rHaMLEC-pMAL-c5X; Lane 4 = supernatant of IPTG-induced E. coli BL21 (DE3) cells transfected with rHaMLEC-pMAL-c5X; Lane 5 = purified rHaMLEC-MBP fusion protein.

    Article Snippet: 3.4 Overexpression and purification of rHaMLEC rHaMLEC was overexpressed in E. coli BL21(DE3) cells and purified using a pMAL protein fusion and purification system (New England Biolabs, USA).

    Techniques: SDS Page, Purification, Marker, Transfection

    Overview of conjugative ICE transfer in M. agalactiae ). Under normal conditions, ICEA copies are found integrated into the host chromosome and most ICEA genes are not expressed. Among the few proteins expressed by chromosomal ICEAs is the CDS14 lipoprotein, which is surface exposed and plays a critical role in initiating the conjugative process (step 1). When ICEA gene expression is induced, under specific cellular conditions or stochastically, the cis -acting DDE transposase is produced and one of the three ICEA copies excises from the chromosome and forms a circular double-stranded DNA (dsDNA) molecule (step 2). ICEA circularization induces the expression of the conjugative module, whose products assemble into the mating pore, a simplified form of type IV secretion system (T4SS) found in more-complex bacteria (step 3). A protein complex known as a relaxosome recognizes the origin of transfer ( oriT ) on the circular ICEA, and a relaxase generates a linear single-stranded DNA (ssDNA) by nicking the ICEA DNA (step 4). Finally, the relaxosome complex interacts with the TraG-like (VirD4 homologue) energetic component found at the inner side of the membrane that facilitates the transfer of the ssDNA bound to the relaxase through the mating channel (step 5). Once in the recipient strain, the ICEA recircularizes, becomes doubly stranded, and integrates randomly into the host chromosome. The minimal functional ICEA encompasses 80% of the coding sequence and includes a gene cluster ( cds5 to cds19 , encoding proteins with transmembrane domains) that most likely represents a module associated with the conjugative channel. Additional essential ICEA determinants included the CDS14 surface lipoprotein, the CDSG putative partitioning protein, and the DDE transposase (CDS22), together with several proteins of unknown function (CDS1, CDSA, CDSC, and CDS30).

    Journal: mBio

    Article Title: The Integrative Conjugative Element (ICE) of Mycoplasma agalactiae: Key Elements Involved in Horizontal Dissemination and Influence of Coresident ICEs

    doi: 10.1128/mBio.00873-18

    Figure Lengend Snippet: Overview of conjugative ICE transfer in M. agalactiae ). Under normal conditions, ICEA copies are found integrated into the host chromosome and most ICEA genes are not expressed. Among the few proteins expressed by chromosomal ICEAs is the CDS14 lipoprotein, which is surface exposed and plays a critical role in initiating the conjugative process (step 1). When ICEA gene expression is induced, under specific cellular conditions or stochastically, the cis -acting DDE transposase is produced and one of the three ICEA copies excises from the chromosome and forms a circular double-stranded DNA (dsDNA) molecule (step 2). ICEA circularization induces the expression of the conjugative module, whose products assemble into the mating pore, a simplified form of type IV secretion system (T4SS) found in more-complex bacteria (step 3). A protein complex known as a relaxosome recognizes the origin of transfer ( oriT ) on the circular ICEA, and a relaxase generates a linear single-stranded DNA (ssDNA) by nicking the ICEA DNA (step 4). Finally, the relaxosome complex interacts with the TraG-like (VirD4 homologue) energetic component found at the inner side of the membrane that facilitates the transfer of the ssDNA bound to the relaxase through the mating channel (step 5). Once in the recipient strain, the ICEA recircularizes, becomes doubly stranded, and integrates randomly into the host chromosome. The minimal functional ICEA encompasses 80% of the coding sequence and includes a gene cluster ( cds5 to cds19 , encoding proteins with transmembrane domains) that most likely represents a module associated with the conjugative channel. Additional essential ICEA determinants included the CDS14 surface lipoprotein, the CDSG putative partitioning protein, and the DDE transposase (CDS22), together with several proteins of unknown function (CDS1, CDSA, CDSC, and CDS30).

    Article Snippet: The anti-CDS14 lipoprotein rabbit serum was produced by animal immunization with a recombinant CDS14 protein (pMAL protein fusion and purification system; New England Biolabs).

    Techniques: Expressing, Produced, Functional Assay, Sequencing

    Protein expression of PG2-ICEA mutants. (A) Immunostaining of M. agalactiae colonies showing CDS14 lipoprotein expression at the surface of 5632 cells. Colony blotting was carried out by using a specific serum (anti-CDS14), and ICEA-negative PG2 cells (PG2) were used as a negative control. (B) Western blot analysis of CDS14 lipoprotein expression in 5632 and PG2 ICEA cells. CDS14 lipoprotein expression in strain 5632 containing three chromosomal ICEA copies (lane 1) was not abrogated in a 5632 mutant harboring a cds14 knockout ICEA copy (lane 2). CDS14 lipoprotein expression was detectable in PG2 transconjugants that had acquired a mutant ICEA harboring an mTn inserted in ncr19 / E (lane 4) but not in strain PG2 (lane 3) or in PG2 transconjugants harboring a cds14 knockout ICEA (lane 5). Transformation of PG2 transconjugants harboring a cds14 knockout ICEA with a plasmid expressing CDS14 restored the expression of the lipoprotein (lane 6). A specific serum raised against lipoprotein P80 was used as a control (P80). (C) Schematic illustrating the protein expression profiles of selected mutant ICEAs in PG2 cells. Mutant ICEAs are identified according to Table S2 , and ICEA products detected by proteomics ( Table S4 ) are indicated (closed arrows).

    Journal: mBio

    Article Title: The Integrative Conjugative Element (ICE) of Mycoplasma agalactiae: Key Elements Involved in Horizontal Dissemination and Influence of Coresident ICEs

    doi: 10.1128/mBio.00873-18

    Figure Lengend Snippet: Protein expression of PG2-ICEA mutants. (A) Immunostaining of M. agalactiae colonies showing CDS14 lipoprotein expression at the surface of 5632 cells. Colony blotting was carried out by using a specific serum (anti-CDS14), and ICEA-negative PG2 cells (PG2) were used as a negative control. (B) Western blot analysis of CDS14 lipoprotein expression in 5632 and PG2 ICEA cells. CDS14 lipoprotein expression in strain 5632 containing three chromosomal ICEA copies (lane 1) was not abrogated in a 5632 mutant harboring a cds14 knockout ICEA copy (lane 2). CDS14 lipoprotein expression was detectable in PG2 transconjugants that had acquired a mutant ICEA harboring an mTn inserted in ncr19 / E (lane 4) but not in strain PG2 (lane 3) or in PG2 transconjugants harboring a cds14 knockout ICEA (lane 5). Transformation of PG2 transconjugants harboring a cds14 knockout ICEA with a plasmid expressing CDS14 restored the expression of the lipoprotein (lane 6). A specific serum raised against lipoprotein P80 was used as a control (P80). (C) Schematic illustrating the protein expression profiles of selected mutant ICEAs in PG2 cells. Mutant ICEAs are identified according to Table S2 , and ICEA products detected by proteomics ( Table S4 ) are indicated (closed arrows).

    Article Snippet: The anti-CDS14 lipoprotein rabbit serum was produced by animal immunization with a recombinant CDS14 protein (pMAL protein fusion and purification system; New England Biolabs).

    Techniques: Expressing, Immunostaining, Negative Control, Western Blot, Mutagenesis, Knock-Out, Transformation Assay, Plasmid Preparation

    Overview of conjugative ICE transfer in M. agalactiae . This schematic illustrates the 5 key steps in ICEA transfer based on current knowledge in other bacteria ( 1 , 18 ). Under normal conditions, ICEA copies are found integrated into the host chromosome and most ICEA genes are not expressed. Among the few proteins expressed by chromosomal ICEAs is the CDS14 lipoprotein, which is surface exposed and plays a critical role in initiating the conjugative process (step 1). When ICEA gene expression is induced, under specific cellular conditions or stochastically, the cis -acting DDE transposase is produced and one of the three ICEA copies excises from the chromosome and forms a circular double-stranded DNA (dsDNA) molecule (step 2). ICEA circularization induces the expression of the conjugative module, whose products assemble into the mating pore, a simplified form of type IV secretion system (T4SS) found in more-complex bacteria (step 3). A protein complex known as a relaxosome recognizes the origin of transfer ( oriT ) on the circular ICEA, and a relaxase generates a linear single-stranded DNA (ssDNA) by nicking the ICEA DNA (step 4). Finally, the relaxosome complex interacts with the TraG-like (VirD4 homologue) energetic component found at the inner side of the membrane that facilitates the transfer of the ssDNA bound to the relaxase through the mating channel (step 5). Once in the recipient strain, the ICEA recircularizes, becomes doubly stranded, and integrates randomly into the host chromosome. The minimal functional ICEA encompasses 80% of the coding sequence and includes a gene cluster ( cds5 to cds19 , encoding proteins with transmembrane domains) that most likely represents a module associated with the conjugative channel. Additional essential ICEA determinants included the CDS14 surface lipoprotein, the CDSG putative partitioning protein, and the DDE transposase (CDS22), together with several proteins of unknown function (CDS1, CDSA, CDSC, and CDS30).

    Journal: mBio

    Article Title: The Integrative Conjugative Element (ICE) of Mycoplasma agalactiae: Key Elements Involved in Horizontal Dissemination and Influence of Coresident ICEs

    doi: 10.1128/mBio.00873-18

    Figure Lengend Snippet: Overview of conjugative ICE transfer in M. agalactiae . This schematic illustrates the 5 key steps in ICEA transfer based on current knowledge in other bacteria ( 1 , 18 ). Under normal conditions, ICEA copies are found integrated into the host chromosome and most ICEA genes are not expressed. Among the few proteins expressed by chromosomal ICEAs is the CDS14 lipoprotein, which is surface exposed and plays a critical role in initiating the conjugative process (step 1). When ICEA gene expression is induced, under specific cellular conditions or stochastically, the cis -acting DDE transposase is produced and one of the three ICEA copies excises from the chromosome and forms a circular double-stranded DNA (dsDNA) molecule (step 2). ICEA circularization induces the expression of the conjugative module, whose products assemble into the mating pore, a simplified form of type IV secretion system (T4SS) found in more-complex bacteria (step 3). A protein complex known as a relaxosome recognizes the origin of transfer ( oriT ) on the circular ICEA, and a relaxase generates a linear single-stranded DNA (ssDNA) by nicking the ICEA DNA (step 4). Finally, the relaxosome complex interacts with the TraG-like (VirD4 homologue) energetic component found at the inner side of the membrane that facilitates the transfer of the ssDNA bound to the relaxase through the mating channel (step 5). Once in the recipient strain, the ICEA recircularizes, becomes doubly stranded, and integrates randomly into the host chromosome. The minimal functional ICEA encompasses 80% of the coding sequence and includes a gene cluster ( cds5 to cds19 , encoding proteins with transmembrane domains) that most likely represents a module associated with the conjugative channel. Additional essential ICEA determinants included the CDS14 surface lipoprotein, the CDSG putative partitioning protein, and the DDE transposase (CDS22), together with several proteins of unknown function (CDS1, CDSA, CDSC, and CDS30).

    Article Snippet: The anti-CDS14 lipoprotein rabbit serum was produced by animal immunization with a recombinant CDS14 protein (pMAL protein fusion and purification system; New England Biolabs).

    Techniques: Expressing, Produced, Functional Assay, Sequencing