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kchip2 mab neuromabs  (Millipore)

 
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    Structured Review

    Millipore kchip2 mab neuromabs
    ( A ) – ( D ) Immunoblot images of rabbit and rat hearts (except (A), right lane, rat brain), probed with Abs marked on top. Kv1.4 was detected in whole tissue lysates (WTL), while the other three proteins were detected in membrane-enriched fraction (Memb). ( E ) Lengths, accession numbers and molecular sizes (in kDa) of rat and rabbit channel subunit orthologs currently available in the NCBI protein database. The Kv1.4 sizes are those of unglycosylated forms, which are smaller than the N-glycosylated forms shown in (A). Kv4.2 and Kv4.3 do not have N-glycosylation signals. The rabbit Kv4.3 we detected (∼60 kDa, panel (C), left lane) was likely the short isoform (62.4 kDa). <t>KChIP2</t> is a cytosolic protein, and thus is not glycosylated.
    Kchip2 Mab Neuromabs, supplied by Millipore, 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/result/kchip2 mab neuromabs/product/Millipore
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    kchip2 mab neuromabs - by Bioz Stars, 2024-12
    86/100 stars

    Images

    1) Product Images from "Long-Term Fish Oil Supplementation Induces Cardiac Electrical Remodeling by Changing Channel Protein Expression in the Rabbit Model"

    Article Title: Long-Term Fish Oil Supplementation Induces Cardiac Electrical Remodeling by Changing Channel Protein Expression in the Rabbit Model

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0010140

    ( A ) – ( D ) Immunoblot images of rabbit and rat hearts (except (A), right lane, rat brain), probed with Abs marked on top. Kv1.4 was detected in whole tissue lysates (WTL), while the other three proteins were detected in membrane-enriched fraction (Memb). ( E ) Lengths, accession numbers and molecular sizes (in kDa) of rat and rabbit channel subunit orthologs currently available in the NCBI protein database. The Kv1.4 sizes are those of unglycosylated forms, which are smaller than the N-glycosylated forms shown in (A). Kv4.2 and Kv4.3 do not have N-glycosylation signals. The rabbit Kv4.3 we detected (∼60 kDa, panel (C), left lane) was likely the short isoform (62.4 kDa). KChIP2 is a cytosolic protein, and thus is not glycosylated.
    Figure Legend Snippet: ( A ) – ( D ) Immunoblot images of rabbit and rat hearts (except (A), right lane, rat brain), probed with Abs marked on top. Kv1.4 was detected in whole tissue lysates (WTL), while the other three proteins were detected in membrane-enriched fraction (Memb). ( E ) Lengths, accession numbers and molecular sizes (in kDa) of rat and rabbit channel subunit orthologs currently available in the NCBI protein database. The Kv1.4 sizes are those of unglycosylated forms, which are smaller than the N-glycosylated forms shown in (A). Kv4.2 and Kv4.3 do not have N-glycosylation signals. The rabbit Kv4.3 we detected (∼60 kDa, panel (C), left lane) was likely the short isoform (62.4 kDa). KChIP2 is a cytosolic protein, and thus is not glycosylated.

    Techniques Used: Western Blot

    ( A ) Immunoblot images of Kv4.2, Kv4.3, and KChIP2 (∼80 ug/lane). ( B ) Immunoblot images of Kv1.4 (∼160 ug/lane). Size marker bands (in kDa) are listed on the left. Sizes for proteins of interest are marked on the right. Note that for panel (A) here and , each channel subunit immunoblot was corrected by its own α-actin immunoblot for loading variations, although only one representative α-actin immunoblot is shown. Loading variation in Fig. 6B was further checked by coomassie blue (CB) stain. ( C ) Data summary: background-subtracted band intensities were divided by corresponding α-actin band intensity, and then normalized by the mean value of control lanes.
    Figure Legend Snippet: ( A ) Immunoblot images of Kv4.2, Kv4.3, and KChIP2 (∼80 ug/lane). ( B ) Immunoblot images of Kv1.4 (∼160 ug/lane). Size marker bands (in kDa) are listed on the left. Sizes for proteins of interest are marked on the right. Note that for panel (A) here and , each channel subunit immunoblot was corrected by its own α-actin immunoblot for loading variations, although only one representative α-actin immunoblot is shown. Loading variation in Fig. 6B was further checked by coomassie blue (CB) stain. ( C ) Data summary: background-subtracted band intensities were divided by corresponding α-actin band intensity, and then normalized by the mean value of control lanes.

    Techniques Used: Western Blot, Marker, Staining



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    ( A ) – ( D ) Immunoblot images of rabbit and rat hearts (except (A), right lane, rat brain), probed with Abs marked on top. Kv1.4 was detected in whole tissue lysates (WTL), while the other three proteins were detected in membrane-enriched fraction (Memb). ( E ) Lengths, accession numbers and molecular sizes (in kDa) of rat and rabbit channel subunit orthologs currently available in the NCBI protein database. The Kv1.4 sizes are those of unglycosylated forms, which are smaller than the N-glycosylated forms shown in (A). Kv4.2 and Kv4.3 do not have N-glycosylation signals. The rabbit Kv4.3 we detected (∼60 kDa, panel (C), left lane) was likely the short isoform (62.4 kDa). <t>KChIP2</t> is a cytosolic protein, and thus is not glycosylated.
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    kchip2 mab neuromabs  (Millipore)
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    ( A ) – ( D ) Immunoblot images of rabbit and rat hearts (except (A), right lane, rat brain), probed with Abs marked on top. Kv1.4 was detected in whole tissue lysates (WTL), while the other three proteins were detected in membrane-enriched fraction (Memb). ( E ) Lengths, accession numbers and molecular sizes (in kDa) of rat and rabbit channel subunit orthologs currently available in the NCBI protein database. The Kv1.4 sizes are those of unglycosylated forms, which are smaller than the N-glycosylated forms shown in (A). Kv4.2 and Kv4.3 do not have N-glycosylation signals. The rabbit Kv4.3 we detected (∼60 kDa, panel (C), left lane) was likely the short isoform (62.4 kDa). <t>KChIP2</t> is a cytosolic protein, and thus is not glycosylated.
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    neuromab monoclonal anti kchip2 antibody  (NeuroMab)
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    ( A ) – ( D ) Immunoblot images of rabbit and rat hearts (except (A), right lane, rat brain), probed with Abs marked on top. Kv1.4 was detected in whole tissue lysates (WTL), while the other three proteins were detected in membrane-enriched fraction (Memb). ( E ) Lengths, accession numbers and molecular sizes (in kDa) of rat and rabbit channel subunit orthologs currently available in the NCBI protein database. The Kv1.4 sizes are those of unglycosylated forms, which are smaller than the N-glycosylated forms shown in (A). Kv4.2 and Kv4.3 do not have N-glycosylation signals. The rabbit Kv4.3 we detected (∼60 kDa, panel (C), left lane) was likely the short isoform (62.4 kDa). <t>KChIP2</t> is a cytosolic protein, and thus is not glycosylated.
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    https://www.bioz.com/result/neuromab monoclonal anti kchip2 antibody/product/NeuroMab
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    Image Search Results


    ( A ) – ( D ) Immunoblot images of rabbit and rat hearts (except (A), right lane, rat brain), probed with Abs marked on top. Kv1.4 was detected in whole tissue lysates (WTL), while the other three proteins were detected in membrane-enriched fraction (Memb). ( E ) Lengths, accession numbers and molecular sizes (in kDa) of rat and rabbit channel subunit orthologs currently available in the NCBI protein database. The Kv1.4 sizes are those of unglycosylated forms, which are smaller than the N-glycosylated forms shown in (A). Kv4.2 and Kv4.3 do not have N-glycosylation signals. The rabbit Kv4.3 we detected (∼60 kDa, panel (C), left lane) was likely the short isoform (62.4 kDa). KChIP2 is a cytosolic protein, and thus is not glycosylated.

    Journal: PLoS ONE

    Article Title: Long-Term Fish Oil Supplementation Induces Cardiac Electrical Remodeling by Changing Channel Protein Expression in the Rabbit Model

    doi: 10.1371/journal.pone.0010140

    Figure Lengend Snippet: ( A ) – ( D ) Immunoblot images of rabbit and rat hearts (except (A), right lane, rat brain), probed with Abs marked on top. Kv1.4 was detected in whole tissue lysates (WTL), while the other three proteins were detected in membrane-enriched fraction (Memb). ( E ) Lengths, accession numbers and molecular sizes (in kDa) of rat and rabbit channel subunit orthologs currently available in the NCBI protein database. The Kv1.4 sizes are those of unglycosylated forms, which are smaller than the N-glycosylated forms shown in (A). Kv4.2 and Kv4.3 do not have N-glycosylation signals. The rabbit Kv4.3 we detected (∼60 kDa, panel (C), left lane) was likely the short isoform (62.4 kDa). KChIP2 is a cytosolic protein, and thus is not glycosylated.

    Article Snippet: After fractionation, the proteins were blotted to PVDF membranes (Amersham), and probed with the following antibodies: Cav1.2 mAb (NeuroMabs), Cav1.1 mAb (Abcam), Kv4.2 pAb (Sigma), Kv4.3 pAb (Alomone), KChIP2 mAb (NeuroMabs), Kv1.4 mAb (NeuroMabs) and hERG pAb (Alomone).

    Techniques: Western Blot

    ( A ) Immunoblot images of Kv4.2, Kv4.3, and KChIP2 (∼80 ug/lane). ( B ) Immunoblot images of Kv1.4 (∼160 ug/lane). Size marker bands (in kDa) are listed on the left. Sizes for proteins of interest are marked on the right. Note that for panel (A) here and , each channel subunit immunoblot was corrected by its own α-actin immunoblot for loading variations, although only one representative α-actin immunoblot is shown. Loading variation in Fig. 6B was further checked by coomassie blue (CB) stain. ( C ) Data summary: background-subtracted band intensities were divided by corresponding α-actin band intensity, and then normalized by the mean value of control lanes.

    Journal: PLoS ONE

    Article Title: Long-Term Fish Oil Supplementation Induces Cardiac Electrical Remodeling by Changing Channel Protein Expression in the Rabbit Model

    doi: 10.1371/journal.pone.0010140

    Figure Lengend Snippet: ( A ) Immunoblot images of Kv4.2, Kv4.3, and KChIP2 (∼80 ug/lane). ( B ) Immunoblot images of Kv1.4 (∼160 ug/lane). Size marker bands (in kDa) are listed on the left. Sizes for proteins of interest are marked on the right. Note that for panel (A) here and , each channel subunit immunoblot was corrected by its own α-actin immunoblot for loading variations, although only one representative α-actin immunoblot is shown. Loading variation in Fig. 6B was further checked by coomassie blue (CB) stain. ( C ) Data summary: background-subtracted band intensities were divided by corresponding α-actin band intensity, and then normalized by the mean value of control lanes.

    Article Snippet: After fractionation, the proteins were blotted to PVDF membranes (Amersham), and probed with the following antibodies: Cav1.2 mAb (NeuroMabs), Cav1.1 mAb (Abcam), Kv4.2 pAb (Sigma), Kv4.3 pAb (Alomone), KChIP2 mAb (NeuroMabs), Kv1.4 mAb (NeuroMabs) and hERG pAb (Alomone).

    Techniques: Western Blot, Marker, Staining

    ( A ) – ( D ) Immunoblot images of rabbit and rat hearts (except (A), right lane, rat brain), probed with Abs marked on top. Kv1.4 was detected in whole tissue lysates (WTL), while the other three proteins were detected in membrane-enriched fraction (Memb). ( E ) Lengths, accession numbers and molecular sizes (in kDa) of rat and rabbit channel subunit orthologs currently available in the NCBI protein database. The Kv1.4 sizes are those of unglycosylated forms, which are smaller than the N-glycosylated forms shown in (A). Kv4.2 and Kv4.3 do not have N-glycosylation signals. The rabbit Kv4.3 we detected (∼60 kDa, panel (C), left lane) was likely the short isoform (62.4 kDa). KChIP2 is a cytosolic protein, and thus is not glycosylated.

    Journal: PLoS ONE

    Article Title: Long-Term Fish Oil Supplementation Induces Cardiac Electrical Remodeling by Changing Channel Protein Expression in the Rabbit Model

    doi: 10.1371/journal.pone.0010140

    Figure Lengend Snippet: ( A ) – ( D ) Immunoblot images of rabbit and rat hearts (except (A), right lane, rat brain), probed with Abs marked on top. Kv1.4 was detected in whole tissue lysates (WTL), while the other three proteins were detected in membrane-enriched fraction (Memb). ( E ) Lengths, accession numbers and molecular sizes (in kDa) of rat and rabbit channel subunit orthologs currently available in the NCBI protein database. The Kv1.4 sizes are those of unglycosylated forms, which are smaller than the N-glycosylated forms shown in (A). Kv4.2 and Kv4.3 do not have N-glycosylation signals. The rabbit Kv4.3 we detected (∼60 kDa, panel (C), left lane) was likely the short isoform (62.4 kDa). KChIP2 is a cytosolic protein, and thus is not glycosylated.

    Article Snippet: After fractionation, the proteins were blotted to PVDF membranes (Amersham), and probed with the following antibodies: Cav1.2 mAb (NeuroMabs), Cav1.1 mAb (Abcam), Kv4.2 pAb (Sigma), Kv4.3 pAb (Alomone), KChIP2 mAb (NeuroMabs), Kv1.4 mAb (NeuroMabs) and hERG pAb (Alomone).

    Techniques: Western Blot

    ( A ) Immunoblot images of Kv4.2, Kv4.3, and KChIP2 (∼80 ug/lane). ( B ) Immunoblot images of Kv1.4 (∼160 ug/lane). Size marker bands (in kDa) are listed on the left. Sizes for proteins of interest are marked on the right. Note that for panel (A) here and , each channel subunit immunoblot was corrected by its own α-actin immunoblot for loading variations, although only one representative α-actin immunoblot is shown. Loading variation in Fig. 6B was further checked by coomassie blue (CB) stain. ( C ) Data summary: background-subtracted band intensities were divided by corresponding α-actin band intensity, and then normalized by the mean value of control lanes.

    Journal: PLoS ONE

    Article Title: Long-Term Fish Oil Supplementation Induces Cardiac Electrical Remodeling by Changing Channel Protein Expression in the Rabbit Model

    doi: 10.1371/journal.pone.0010140

    Figure Lengend Snippet: ( A ) Immunoblot images of Kv4.2, Kv4.3, and KChIP2 (∼80 ug/lane). ( B ) Immunoblot images of Kv1.4 (∼160 ug/lane). Size marker bands (in kDa) are listed on the left. Sizes for proteins of interest are marked on the right. Note that for panel (A) here and , each channel subunit immunoblot was corrected by its own α-actin immunoblot for loading variations, although only one representative α-actin immunoblot is shown. Loading variation in Fig. 6B was further checked by coomassie blue (CB) stain. ( C ) Data summary: background-subtracted band intensities were divided by corresponding α-actin band intensity, and then normalized by the mean value of control lanes.

    Article Snippet: After fractionation, the proteins were blotted to PVDF membranes (Amersham), and probed with the following antibodies: Cav1.2 mAb (NeuroMabs), Cav1.1 mAb (Abcam), Kv4.2 pAb (Sigma), Kv4.3 pAb (Alomone), KChIP2 mAb (NeuroMabs), Kv1.4 mAb (NeuroMabs) and hERG pAb (Alomone).

    Techniques: Western Blot, Marker, Staining