pmal c2 expression vector  (New England Biolabs)


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    Structured Review

    New England Biolabs pmal c2 expression vector
    Pmal C2 Expression Vector, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 88/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pmal c2 expression vector/product/New England Biolabs
    Average 88 stars, based on 15 article reviews
    Price from $9.99 to $1999.99
    pmal c2 expression vector - by Bioz Stars, 2020-05
    88/100 stars

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    Related Articles

    Transferring:

    Article Title: Aluminum-Dependent Terminal Differentiation of the Arabidopsis Root Tip Is Mediated through an ATR-, ALT2-, and SOG1-Regulated Transcriptional Response [OPEN]
    Article Snippet: .. After transferring into the pMAL-C2 expression vector with Xmn I and Xba I (New England Biolabs), the MBP-SOG1 construct was transformed into BL21(DE3)-competent Escherichia coli (New England Biolabs) after which protein was produced following induction for 3 h with 0.4 mM isopropyl β- d -1-thiogalactopyranoside. .. MBP-SOG1 was isolated by sonication followed by purification with amylose resin (New England Biolabs) and then elution with 50 mM maltose.

    Construct:

    Article Title: Aluminum-Dependent Terminal Differentiation of the Arabidopsis Root Tip Is Mediated through an ATR-, ALT2-, and SOG1-Regulated Transcriptional Response [OPEN]
    Article Snippet: .. After transferring into the pMAL-C2 expression vector with Xmn I and Xba I (New England Biolabs), the MBP-SOG1 construct was transformed into BL21(DE3)-competent Escherichia coli (New England Biolabs) after which protein was produced following induction for 3 h with 0.4 mM isopropyl β- d -1-thiogalactopyranoside. .. MBP-SOG1 was isolated by sonication followed by purification with amylose resin (New England Biolabs) and then elution with 50 mM maltose.

    Produced:

    Article Title: Aluminum-Dependent Terminal Differentiation of the Arabidopsis Root Tip Is Mediated through an ATR-, ALT2-, and SOG1-Regulated Transcriptional Response [OPEN]
    Article Snippet: .. After transferring into the pMAL-C2 expression vector with Xmn I and Xba I (New England Biolabs), the MBP-SOG1 construct was transformed into BL21(DE3)-competent Escherichia coli (New England Biolabs) after which protein was produced following induction for 3 h with 0.4 mM isopropyl β- d -1-thiogalactopyranoside. .. MBP-SOG1 was isolated by sonication followed by purification with amylose resin (New England Biolabs) and then elution with 50 mM maltose.

    Expressing:

    Article Title: egc-Encoded Superantigens from Staphylococcus aureus Are Neutralized by Human Sera Much Less Efficiently than Are Classical Staphylococcal Enterotoxins or Toxic Shock Syndrome Toxin
    Article Snippet: .. After digestion with these enzymes, the PCR products were ligated into the pMAL-c2 expression vector from New England Biolabs (Ozyme), which was restricted with the same enzymes. .. The resulting plasmids were transfected into Escherichia coli TG1.

    Article Title: Aluminum-Dependent Terminal Differentiation of the Arabidopsis Root Tip Is Mediated through an ATR-, ALT2-, and SOG1-Regulated Transcriptional Response [OPEN]
    Article Snippet: .. After transferring into the pMAL-C2 expression vector with Xmn I and Xba I (New England Biolabs), the MBP-SOG1 construct was transformed into BL21(DE3)-competent Escherichia coli (New England Biolabs) after which protein was produced following induction for 3 h with 0.4 mM isopropyl β- d -1-thiogalactopyranoside. .. MBP-SOG1 was isolated by sonication followed by purification with amylose resin (New England Biolabs) and then elution with 50 mM maltose.

    Polymerase Chain Reaction:

    Article Title: egc-Encoded Superantigens from Staphylococcus aureus Are Neutralized by Human Sera Much Less Efficiently than Are Classical Staphylococcal Enterotoxins or Toxic Shock Syndrome Toxin
    Article Snippet: .. After digestion with these enzymes, the PCR products were ligated into the pMAL-c2 expression vector from New England Biolabs (Ozyme), which was restricted with the same enzymes. .. The resulting plasmids were transfected into Escherichia coli TG1.

    Transformation Assay:

    Article Title: Aluminum-Dependent Terminal Differentiation of the Arabidopsis Root Tip Is Mediated through an ATR-, ALT2-, and SOG1-Regulated Transcriptional Response [OPEN]
    Article Snippet: .. After transferring into the pMAL-C2 expression vector with Xmn I and Xba I (New England Biolabs), the MBP-SOG1 construct was transformed into BL21(DE3)-competent Escherichia coli (New England Biolabs) after which protein was produced following induction for 3 h with 0.4 mM isopropyl β- d -1-thiogalactopyranoside. .. MBP-SOG1 was isolated by sonication followed by purification with amylose resin (New England Biolabs) and then elution with 50 mM maltose.

    Plasmid Preparation:

    Article Title: egc-Encoded Superantigens from Staphylococcus aureus Are Neutralized by Human Sera Much Less Efficiently than Are Classical Staphylococcal Enterotoxins or Toxic Shock Syndrome Toxin
    Article Snippet: .. After digestion with these enzymes, the PCR products were ligated into the pMAL-c2 expression vector from New England Biolabs (Ozyme), which was restricted with the same enzymes. .. The resulting plasmids were transfected into Escherichia coli TG1.

    Article Title: Aluminum-Dependent Terminal Differentiation of the Arabidopsis Root Tip Is Mediated through an ATR-, ALT2-, and SOG1-Regulated Transcriptional Response [OPEN]
    Article Snippet: .. After transferring into the pMAL-C2 expression vector with Xmn I and Xba I (New England Biolabs), the MBP-SOG1 construct was transformed into BL21(DE3)-competent Escherichia coli (New England Biolabs) after which protein was produced following induction for 3 h with 0.4 mM isopropyl β- d -1-thiogalactopyranoside. .. MBP-SOG1 was isolated by sonication followed by purification with amylose resin (New England Biolabs) and then elution with 50 mM maltose.

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    New England Biolabs expression vector pmal c2
    Protein Gel Blot Analysis of the MBP-AtIpk2β Fusion Protein. E. coli cells were transformed with either the empty vector <t>pMAL-c2</t> (lane C) or plasmid pMAL-c2–AtIpk2β (lanes 1 and 2). Protein extracts were obtained from noninduced (−) or IPTG-induced (+) cells. Proteins (45 μg per lane) were detected using an antiserum that recognizes the MBP portion of the proteins. The positions of MBP (42 kD) and the MBP-AtIpk2β fusion protein (75 kD) are indicated by arrows.
    Expression Vector Pmal C2, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 88/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/expression vector pmal c2/product/New England Biolabs
    Average 88 stars, based on 19 article reviews
    Price from $9.99 to $1999.99
    expression vector pmal c2 - by Bioz Stars, 2020-05
    88/100 stars
      Buy from Supplier

    85
    New England Biolabs mbp fusion expression vector pmal c2
    The maltose-binding protein <t>(MBP)-amyloid</t> precursor protein intracellular domain (AICD) fusion protein was expressed, purified and detected in vitro . (A) Whole-cell extracts from E. coli BL21 transformed with <t>AICD/pMAL-c2</t> plasmids either noninduced (lane I) or induced by isopropyl-β-D-thiogalactoside (lane II), purified MBP-AICD (lane III) and MBP (lane IV) were separated on 10% sodium dodecyl sulfate-polyacrylamide electrophoresis gels and stained with Coomassie brilliant blue. (B) MBP-AICD (lane I, corresponding to lane III in Figure 1A ) but not MBP (lane II, corresponding to lane IV in Figure 1A ) was recognized by a specific antibody against AICD in western blot analysis.
    Mbp Fusion Expression Vector Pmal C2, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mbp fusion expression vector pmal c2/product/New England Biolabs
    Average 85 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    mbp fusion expression vector pmal c2 - by Bioz Stars, 2020-05
    85/100 stars
      Buy from Supplier

    Image Search Results


    Protein Gel Blot Analysis of the MBP-AtIpk2β Fusion Protein. E. coli cells were transformed with either the empty vector pMAL-c2 (lane C) or plasmid pMAL-c2–AtIpk2β (lanes 1 and 2). Protein extracts were obtained from noninduced (−) or IPTG-induced (+) cells. Proteins (45 μg per lane) were detected using an antiserum that recognizes the MBP portion of the proteins. The positions of MBP (42 kD) and the MBP-AtIpk2β fusion protein (75 kD) are indicated by arrows.

    Journal: The Plant Cell

    Article Title: Arabidopsis Inositol Polyphosphate 6-/3-Kinase Is a Nuclear Protein That Complements a Yeast Mutant Lacking a Functional ArgR-Mcm1 Transcription Complex

    doi: 10.1105/tpc.006676

    Figure Lengend Snippet: Protein Gel Blot Analysis of the MBP-AtIpk2β Fusion Protein. E. coli cells were transformed with either the empty vector pMAL-c2 (lane C) or plasmid pMAL-c2–AtIpk2β (lanes 1 and 2). Protein extracts were obtained from noninduced (−) or IPTG-induced (+) cells. Proteins (45 μg per lane) were detected using an antiserum that recognizes the MBP portion of the proteins. The positions of MBP (42 kD) and the MBP-AtIpk2β fusion protein (75 kD) are indicated by arrows.

    Article Snippet: The AtIpk2 β coding sequence was excised from plasmid pCR-K-2 using EcoRI-XhoI restriction enzymes and subcloned into the expression vector pMAL-c2 (New England Biolabs, Schwalbach, Germany), which had been cut previously with EcoRI and SalI.

    Techniques: Western Blot, Transformation Assay, Plasmid Preparation

    Enzyme activity assay of Nor-1c–MBP and Nor-1c proteins. All reactions were conducted at 37°C in the dark. The reaction products were resolved by TLC with benzene-ethyl acetate (7:3) as the developing system. The photograph was taken under white light. The reaction components for each lane are as follows. Lane 1, NA (0.9 mM); lane 2, AVN (0.9 mM); lane 3, NA (0.9 mM) plus NADPH (2.3 mM); lane 4, NA (0.9 mM) plus NADPH (2.3 mM) plus crude cell extract (35 μg) from E. coli DH5α; lane 5, NA (0.9 mM) plus NADPH (2.3 mM) plus crude cell extract (70 μg) from E. coli DH5α containing pMAL-c2; lane 6, NA (0.9 mM) plus NADPH (2.3 mM) plus crude cell extract (70 μg) from E. coli DH5α containing pMN1; lane 7, NA (0.9 mM) plus crude cell extract from (70 μg) E. coli DH5α containing pMN1; lane 8, NA (0.9 mM) plus NADPH (2.3 mM) plus crude cell extract (35 μg) from E. coli DH5α plus purified Nor-1c (35 μg); lane 9, NA (0.9 mM) plus crude cell extract (35 μg) from E. coli DH5α plus purified Nor-1c (35 μg). All crude cell extracts are the 10,000 × g supernatant fraction.

    Journal: Applied and Environmental Microbiology

    Article Title: Enzymatic Function of the Nor-1 Protein in Aflatoxin Biosynthesis in Aspergillus parasiticus

    doi:

    Figure Lengend Snippet: Enzyme activity assay of Nor-1c–MBP and Nor-1c proteins. All reactions were conducted at 37°C in the dark. The reaction products were resolved by TLC with benzene-ethyl acetate (7:3) as the developing system. The photograph was taken under white light. The reaction components for each lane are as follows. Lane 1, NA (0.9 mM); lane 2, AVN (0.9 mM); lane 3, NA (0.9 mM) plus NADPH (2.3 mM); lane 4, NA (0.9 mM) plus NADPH (2.3 mM) plus crude cell extract (35 μg) from E. coli DH5α; lane 5, NA (0.9 mM) plus NADPH (2.3 mM) plus crude cell extract (70 μg) from E. coli DH5α containing pMAL-c2; lane 6, NA (0.9 mM) plus NADPH (2.3 mM) plus crude cell extract (70 μg) from E. coli DH5α containing pMN1; lane 7, NA (0.9 mM) plus crude cell extract from (70 μg) E. coli DH5α containing pMN1; lane 8, NA (0.9 mM) plus NADPH (2.3 mM) plus crude cell extract (35 μg) from E. coli DH5α plus purified Nor-1c (35 μg); lane 9, NA (0.9 mM) plus crude cell extract (35 μg) from E. coli DH5α plus purified Nor-1c (35 μg). All crude cell extracts are the 10,000 × g supernatant fraction.

    Article Snippet: The nor-1 cDNA was excised from pQE31 with Eco RI and Sal I and cloned into the Eco RI/ Sal I sites of the expression vector pMAL-c2 (New England Biolabs, Inc., Beverly, Mass.).

    Techniques: Enzyme Activity Assay, Thin Layer Chromatography, Purification

    The maltose-binding protein (MBP)-amyloid precursor protein intracellular domain (AICD) fusion protein was expressed, purified and detected in vitro . (A) Whole-cell extracts from E. coli BL21 transformed with AICD/pMAL-c2 plasmids either noninduced (lane I) or induced by isopropyl-β-D-thiogalactoside (lane II), purified MBP-AICD (lane III) and MBP (lane IV) were separated on 10% sodium dodecyl sulfate-polyacrylamide electrophoresis gels and stained with Coomassie brilliant blue. (B) MBP-AICD (lane I, corresponding to lane III in Figure 1A ) but not MBP (lane II, corresponding to lane IV in Figure 1A ) was recognized by a specific antibody against AICD in western blot analysis.

    Journal: Neural Regeneration Research

    Article Title: Two memory associated genes regulated by amyloid precursor protein intracellular domain

    doi: 10.3969/j.issn.1673-5374.2012.05.003

    Figure Lengend Snippet: The maltose-binding protein (MBP)-amyloid precursor protein intracellular domain (AICD) fusion protein was expressed, purified and detected in vitro . (A) Whole-cell extracts from E. coli BL21 transformed with AICD/pMAL-c2 plasmids either noninduced (lane I) or induced by isopropyl-β-D-thiogalactoside (lane II), purified MBP-AICD (lane III) and MBP (lane IV) were separated on 10% sodium dodecyl sulfate-polyacrylamide electrophoresis gels and stained with Coomassie brilliant blue. (B) MBP-AICD (lane I, corresponding to lane III in Figure 1A ) but not MBP (lane II, corresponding to lane IV in Figure 1A ) was recognized by a specific antibody against AICD in western blot analysis.

    Article Snippet: Expression of MBP-AICD fusion protein and its identification by western blot analysis The DNA fragment encoding AICD59, modified by the addition of a Bam HI (New England Biolabs (Beijing) Ltd., Beijing, China) site at the 5′ terminus and a Hind III (New England Biolabs (Beijing) Ltd.) site at the 3′ terminus, was amplified via PCR from full-length APP695 (New England Biolabs (Beijing) Ltd.) and then cloned into the MBP fusion expression vector pMAL-c2 (New England Biolabs (Beijing) Ltd.).

    Techniques: Binding Assay, Purification, In Vitro, Transformation Assay, Electrophoresis, Staining, Western Blot