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full-length e. coli codon-optimized sequence of tbsti1  (GenScript corporation)

 
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    GenScript corporation full-length e. coli codon-optimized sequence of tbsti1
    TbHsp70 and TbHsp70.4 directly interact with <t>TbSTi1.</t> Interaction between the TbHsp70s, TbHsp70 and TbHsp70.4 and TbSTi1 was investigated using far western analysis. TbHsp70 (50 µg); control protein, BSA (50 µg) and TbSTi1 at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred onto a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( A ; top panel). A similar blot was then overlaid with TbHsp70 and it was probed using anti-TbHsp70 ( A ; bottom panel). ( B ) TbHsp70.4 protein (50 µg); control protein, BSA (50 µg) and TbSTi1 protein at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred to a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( B ; top panel). A similar blot was then overlaid with TbHsp70.4 (75 µg) and it was probed using anti-TbHsp70.4 ( B ; bottom panel). The blots are representative of independent replicates.
    Full Length E. Coli Codon Optimized Sequence Of Tbsti1, supplied by GenScript corporation, 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/full-length+e%2E+coli+codon-optimized+sequence+of+tbsti1/full+length+e++coli+codon+optimized+sequence+of+tbsti1/pmc08269394-194-7-18
    Average 90 stars, based on 1 article reviews
    full-length e. coli codon-optimized sequence of tbsti1 - by Bioz Stars, 2026-10
    90/100 stars

    Images

    1) Product Images from "Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue"

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms22136776

    TbHsp70 and TbHsp70.4 directly interact with TbSTi1. Interaction between the TbHsp70s, TbHsp70 and TbHsp70.4 and TbSTi1 was investigated using far western analysis. TbHsp70 (50 µg); control protein, BSA (50 µg) and TbSTi1 at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred onto a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( A ; top panel). A similar blot was then overlaid with TbHsp70 and it was probed using anti-TbHsp70 ( A ; bottom panel). ( B ) TbHsp70.4 protein (50 µg); control protein, BSA (50 µg) and TbSTi1 protein at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred to a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( B ; top panel). A similar blot was then overlaid with TbHsp70.4 (75 µg) and it was probed using anti-TbHsp70.4 ( B ; bottom panel). The blots are representative of independent replicates.
    Figure Legend Snippet: TbHsp70 and TbHsp70.4 directly interact with TbSTi1. Interaction between the TbHsp70s, TbHsp70 and TbHsp70.4 and TbSTi1 was investigated using far western analysis. TbHsp70 (50 µg); control protein, BSA (50 µg) and TbSTi1 at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred onto a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( A ; top panel). A similar blot was then overlaid with TbHsp70 and it was probed using anti-TbHsp70 ( A ; bottom panel). ( B ) TbHsp70.4 protein (50 µg); control protein, BSA (50 µg) and TbSTi1 protein at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred to a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( B ; top panel). A similar blot was then overlaid with TbHsp70.4 (75 µg) and it was probed using anti-TbHsp70.4 ( B ; bottom panel). The blots are representative of independent replicates.

    Techniques Used: Western Blot, Control, SDS Page

    TbSTi1 interacts with TbHsp70 but not with TbHsp70.c. Far western analysis was used to investigate the interactions between TbHsp70.c ( A ) and TbHsp70 ( B ) with TbSTi1. BSA (20 µg/mL) as negative control protein, TbSTi1 (20 µg/mL) as positive control protein, and TbHsp70 or TbHsp70.c proteins at various concentrations (2.5 µg/mL, 5 µg/mL, 10 µg/mL, and 20 µg/mL) were resolved by SDS-PAGE and transferred to the respective blots that were then probed using anti-HA antibody (top panel), an epitope of TbSTi1. Similarly transferred blots were overlaid with TbSTi1 then also probed with anti-HA antibody (bottom panel). The blots are representative of independent replicates.
    Figure Legend Snippet: TbSTi1 interacts with TbHsp70 but not with TbHsp70.c. Far western analysis was used to investigate the interactions between TbHsp70.c ( A ) and TbHsp70 ( B ) with TbSTi1. BSA (20 µg/mL) as negative control protein, TbSTi1 (20 µg/mL) as positive control protein, and TbHsp70 or TbHsp70.c proteins at various concentrations (2.5 µg/mL, 5 µg/mL, 10 µg/mL, and 20 µg/mL) were resolved by SDS-PAGE and transferred to the respective blots that were then probed using anti-HA antibody (top panel), an epitope of TbSTi1. Similarly transferred blots were overlaid with TbSTi1 then also probed with anti-HA antibody (bottom panel). The blots are representative of independent replicates.

    Techniques Used: Western Blot, Negative Control, Positive Control, SDS Page

    Related Articles

    Sequencing:

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue
    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.

    Synthesized:

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue
    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.

    Expressing:

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue
    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.

    Plasmid Preparation:

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue
    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.

    Western Blot:

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue
    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.

    Control:

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue
    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.

    SDS Page:

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue
    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.

    Negative Control:

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue
    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.

    Positive Control:

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue
    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.



    Similar Products

    full-length e. coli codon-optimized sequence of tbsti1  (GenScript corporation)
    90
    GenScript corporation full-length e. coli codon-optimized sequence of tbsti1
    TbHsp70 and TbHsp70.4 directly interact with <t>TbSTi1.</t> Interaction between the TbHsp70s, TbHsp70 and TbHsp70.4 and TbSTi1 was investigated using far western analysis. TbHsp70 (50 µg); control protein, BSA (50 µg) and TbSTi1 at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred onto a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( A ; top panel). A similar blot was then overlaid with TbHsp70 and it was probed using anti-TbHsp70 ( A ; bottom panel). ( B ) TbHsp70.4 protein (50 µg); control protein, BSA (50 µg) and TbSTi1 protein at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred to a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( B ; top panel). A similar blot was then overlaid with TbHsp70.4 (75 µg) and it was probed using anti-TbHsp70.4 ( B ; bottom panel). The blots are representative of independent replicates.
    Full Length E. Coli Codon Optimized Sequence Of Tbsti1, supplied by GenScript corporation, 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/full-length+e%2E+coli+codon-optimized+sequence+of+tbsti1/full+length+e++coli+codon+optimized+sequence+of+tbsti1/pmc08269394-194-7-18
    Average 90 stars, based on 1 article reviews
    full-length e. coli codon-optimized sequence of tbsti1 - by Bioz Stars, 2026-10
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    TbHsp70 and TbHsp70.4 directly interact with TbSTi1. Interaction between the TbHsp70s, TbHsp70 and TbHsp70.4 and TbSTi1 was investigated using far western analysis. TbHsp70 (50 µg); control protein, BSA (50 µg) and TbSTi1 at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred onto a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( A ; top panel). A similar blot was then overlaid with TbHsp70 and it was probed using anti-TbHsp70 ( A ; bottom panel). ( B ) TbHsp70.4 protein (50 µg); control protein, BSA (50 µg) and TbSTi1 protein at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred to a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( B ; top panel). A similar blot was then overlaid with TbHsp70.4 (75 µg) and it was probed using anti-TbHsp70.4 ( B ; bottom panel). The blots are representative of independent replicates.

    Journal: International Journal of Molecular Sciences

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue

    doi: 10.3390/ijms22136776

    Figure Lengend Snippet: TbHsp70 and TbHsp70.4 directly interact with TbSTi1. Interaction between the TbHsp70s, TbHsp70 and TbHsp70.4 and TbSTi1 was investigated using far western analysis. TbHsp70 (50 µg); control protein, BSA (50 µg) and TbSTi1 at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred onto a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( A ; top panel). A similar blot was then overlaid with TbHsp70 and it was probed using anti-TbHsp70 ( A ; bottom panel). ( B ) TbHsp70.4 protein (50 µg); control protein, BSA (50 µg) and TbSTi1 protein at various concentrations (25 µg, 50 µg, 75 µg, 100 µg) were resolved by SDS-PAGE and transferred to a blot and the blot was probed using rabbit polyclonal anti-TbHsp70.4 ( B ; top panel). A similar blot was then overlaid with TbHsp70.4 (75 µg) and it was probed using anti-TbHsp70.4 ( B ; bottom panel). The blots are representative of independent replicates.

    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.

    Techniques: Western Blot, Control, SDS Page

    TbSTi1 interacts with TbHsp70 but not with TbHsp70.c. Far western analysis was used to investigate the interactions between TbHsp70.c ( A ) and TbHsp70 ( B ) with TbSTi1. BSA (20 µg/mL) as negative control protein, TbSTi1 (20 µg/mL) as positive control protein, and TbHsp70 or TbHsp70.c proteins at various concentrations (2.5 µg/mL, 5 µg/mL, 10 µg/mL, and 20 µg/mL) were resolved by SDS-PAGE and transferred to the respective blots that were then probed using anti-HA antibody (top panel), an epitope of TbSTi1. Similarly transferred blots were overlaid with TbSTi1 then also probed with anti-HA antibody (bottom panel). The blots are representative of independent replicates.

    Journal: International Journal of Molecular Sciences

    Article Title: Characterization of an Atypical Trypanosoma brucei Hsp70 Demonstrates Its Cytosolic-Nuclear Localization and Modulation by Quercetin and Methylene Blue

    doi: 10.3390/ijms22136776

    Figure Lengend Snippet: TbSTi1 interacts with TbHsp70 but not with TbHsp70.c. Far western analysis was used to investigate the interactions between TbHsp70.c ( A ) and TbHsp70 ( B ) with TbSTi1. BSA (20 µg/mL) as negative control protein, TbSTi1 (20 µg/mL) as positive control protein, and TbHsp70 or TbHsp70.c proteins at various concentrations (2.5 µg/mL, 5 µg/mL, 10 µg/mL, and 20 µg/mL) were resolved by SDS-PAGE and transferred to the respective blots that were then probed using anti-HA antibody (top panel), an epitope of TbSTi1. Similarly transferred blots were overlaid with TbSTi1 then also probed with anti-HA antibody (bottom panel). The blots are representative of independent replicates.

    Article Snippet: The full-length E. coli codon-optimized sequence of TBSTI1 (TriTrypDB accession number: Tb927.5.2190) was synthesized and supplied by the GenScript Corporation (Piscataway, NJ, USA) and inserted into the pQE60 (Qiagen, Germantown, MD, USA) between the Bam HI and Hind III restriction sites to generate the pQE60-TbSTi expression plasmid with an N-terminal HA epitope.

    Techniques: Western Blot, Negative Control, Positive Control, SDS Page