mbp fusion expression vector pmal c2 (New England Biolabs)
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mbp fusion expression vector pmal c2
Mbp Fusion Expression Vector Pmal C2, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mbp+expression+vector+pmal+c2/pmc04350115-59-56-61
Average 86 stars, based on 1 article reviews
Mbp Fusion Expression Vector Pmal C2, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mbp+expression+vector+pmal+c2/pmc04350115-59-56-61
Average 86 stars, based on 1 article reviews
mbp fusion expression vector pmal c2 - by Bioz Stars,
2026-10
86/100 stars
Images
1) Product Images from "Two memory associated genes regulated by amyloid precursor protein intracellular domain"
Article Title: Two memory associated genes regulated by amyloid precursor protein intracellular domain
Journal: Neural Regeneration Research
doi: 10.3969/j.issn.1673-5374.2012.05.003
Figure Legend 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 ) but not MBP (lane II, corresponding to lane IV in ) was recognized by a specific antibody against AICD in western blot analysis.
Techniques Used: Binding Assay, Purification, In Vitro, Transformation Assay, Electrophoresis, Staining, Western Blot
Related Articles
Expressing:Article Title: Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner Article Snippet: .. MBP was obtained from an E. coli strain that carries the Article Title: The Combination of MBP and BCG-Induced Dendritic Cell Maturation through TLR2/TLR4 Promotes Th1 Activation In Vitro and Vivo Article Snippet: .. MBP was produced from an E. coli strain that carries the Article Title: Immunolocalization of the electrogenic Na+- HCO 3 − cotransporter in mammalian and amphibian kidney Article Snippet: .. The purified PCR product was digested with EcoR I and Xba I, repurified, and ligated into the Article Title: Synergistic antitumor effects of Escherichia coli maltose binding protein and Bacillus Calmette-Guerin in a mouse lung carcinoma model. Article Snippet: Maltose binding protein (MBP) is a component of the maltose transport system in the periplasm of Escherichia coli.. It is commonly believed that MBP has minimal effects on the bioactivity, thus, it is widely used in the purification of recombinant proteins.. Here, we found that the combined immunization with MBP and Bacillus Calmette–Guerin (BCG) significantly inhibited tumor growth compared with MBP or Article Title: TLR9 played a more important role than TLR2 in the combination of maltose-binding protein and BCG-induced Th1 activation. Article Snippet: Our previous study demonstrated that maltose-binding protein (MBP) combined with BCG induced synergistic mouse Th1 activation in vivo.. Here, to explore the mechanism of MBP combined with BCG on Th1 activation, mouse purified CD4+ T cells were stimulated with MBP and BCG in vitro.. The results showed that MBP combined with BCG synergistically increased IFNproduction, accompanied with the upregulation of TLR2/9 expressions, suggesting that TLR2/9 were involved in the combination-induced Th1 activation. Article Title: Antibody which binds human blue-light photoreceptor hCRY2 Article Snippet: .. A maltose binding protein (MBP) fusion construct was made by inserting the Bgl II/Hind III fragment carrying the entire photolyase homolog coding region into the H I/Hind III site of the Article Title: Putative human blue-light photoreceptors hCRY1 and hCRY2 are flavoproteins. Article Snippet: Recently, a human cDNA clone with high sequence homology to the photolyase/blue-light photoreceptor family was identified.. The putative protein encoded by this gene exhibited a strikingly high (48% identity) degree of homology to the Drosophila melanogaster (6-4) photolyase [Todo et al. (1996) Science 272, 109-112].. We have now identified a second human gene whose amino acid sequence displays 73% identity to the first one and have named the two genes CRY1 and CRY2, respectively. Produced:Article Title: The Combination of MBP and BCG-Induced Dendritic Cell Maturation through TLR2/TLR4 Promotes Th1 Activation In Vitro and Vivo Article Snippet: .. MBP was produced from an E. coli strain that carries the Purification:Article Title: Immunolocalization of the electrogenic Na+- HCO 3 − cotransporter in mammalian and amphibian kidney Article Snippet: .. The purified PCR product was digested with EcoR I and Xba I, repurified, and ligated into the Polymerase Chain Reaction:Article Title: Immunolocalization of the electrogenic Na+- HCO 3 − cotransporter in mammalian and amphibian kidney Article Snippet: .. The purified PCR product was digested with EcoR I and Xba I, repurified, and ligated into the Activity Assay:Article Title: Synergistic antitumor effects of Escherichia coli maltose binding protein and Bacillus Calmette-Guerin in a mouse lung carcinoma model. Article Snippet: Maltose binding protein (MBP) is a component of the maltose transport system in the periplasm of Escherichia coli.. It is commonly believed that MBP has minimal effects on the bioactivity, thus, it is widely used in the purification of recombinant proteins.. Here, we found that the combined immunization with MBP and Bacillus Calmette–Guerin (BCG) significantly inhibited tumor growth compared with MBP or Phospho-proteomics:Article Title: Escherichia coli maltose-binding protein (MBP) directly induces mouse Th1 activation through upregulating TLR2 and downregulating TLR4 expressions. Article Snippet: Maltose-binding protein (MBP), a component of the maltose transport system of Escherichia coli, has been commonly thought to have minimal bioactivity.. Our previous studies demonstrated that MBP could significantly enhance Bacillus Calmette–Guerin (BCG)-induced T helper 1 (Th1) cell activation in mice.. In the present study, we analyzed the effect of MBP on mouse T cells and found that MBP promoted the proliferation and IFNproduction of CD4+ T cells, suggesting that MBP directly induces Th1 activation. Binding Assay:Article Title: Antibody which binds human blue-light photoreceptor hCRY2 Article Snippet: .. A maltose binding protein (MBP) fusion construct was made by inserting the Bgl II/Hind III fragment carrying the entire photolyase homolog coding region into the H I/Hind III site of the Construct:Article Title: Antibody which binds human blue-light photoreceptor hCRY2 Article Snippet: .. A maltose binding protein (MBP) fusion construct was made by inserting the Bgl II/Hind III fragment carrying the entire photolyase homolog coding region into the H I/Hind III site of the Article Title: Putative human blue-light photoreceptors hCRY1 and hCRY2 are flavoproteins. Article Snippet: Recently, a human cDNA clone with high sequence homology to the photolyase/blue-light photoreceptor family was identified.. The putative protein encoded by this gene exhibited a strikingly high (48% identity) degree of homology to the Drosophila melanogaster (6-4) photolyase [Todo et al. (1996) Science 272, 109-112].. We have now identified a second human gene whose amino acid sequence displays 73% identity to the first one and have named the two genes CRY1 and CRY2, respectively. Plasmid Preparation:Article Title: Putative human blue-light photoreceptors hCRY1 and hCRY2 are flavoproteins. Article Snippet: Recently, a human cDNA clone with high sequence homology to the photolyase/blue-light photoreceptor family was identified.. The putative protein encoded by this gene exhibited a strikingly high (48% identity) degree of homology to the Drosophila melanogaster (6-4) photolyase [Todo et al. (1996) Science 272, 109-112].. We have now identified a second human gene whose amino acid sequence displays 73% identity to the first one and have named the two genes CRY1 and CRY2, respectively. |