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kpna1  (Proteintech)


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    Structured Review

    Proteintech kpna1
    (A) CV-1 cells transfected with the indicated siRNA were infected with SV40 and the resulting whole cell extracts were subjected to SDS-PAGE followed by immunoblotting. The extent of depletion by the <t>KPNA1,</t> KPNA2, and KPNA4 siRNA is shown in the Western blots below. Data were normalized to the Scr control. (B) The T-Ag band intensity in A was quantified by the FIJI software. Data were normalized to the Scr control. (C) CV-1 cells transfected with the indicated siRNA were infected with SV40 and the resulting whole cell extracts were subjected to SDS-PAGE and immunoblotting. (D) The T-Ag band intensity in C was quantified by the FIJI software. Data were normalized to the Scr control. (E) CV-1 cells were fixed and stained for Nesprin-2 (red) and either one of the KPNA1, KPNA2, or KPNA4 protein (green) and counterstained with DAPI (blue). Scale bar: 10 µm. (F) Pearson’s coefficient was used to quantify colocalization between KPNA1, KPNA2, or KPNA4 with Nesprin-2. Each data point represents one field of view with at least 10 cells. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001
    Kpna1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/kpna1/importin+%CE%B15+Antibody/bio_rxiv__64898__2026__03__15__711898-197-78-79
    Average 93 stars, based on 31 article reviews
    kpna1 - by Bioz Stars, 2026-09
    93/100 stars

    Images

    1) Product Images from "SV40 exploits the Nesprin-2-SUN1-KPNA4 axis for stepwise targeting and entry into the host nucleus to promote infection"

    Article Title: SV40 exploits the Nesprin-2-SUN1-KPNA4 axis for stepwise targeting and entry into the host nucleus to promote infection

    Journal: bioRxiv

    doi: 10.64898/2026.03.15.711898

    (A) CV-1 cells transfected with the indicated siRNA were infected with SV40 and the resulting whole cell extracts were subjected to SDS-PAGE followed by immunoblotting. The extent of depletion by the KPNA1, KPNA2, and KPNA4 siRNA is shown in the Western blots below. Data were normalized to the Scr control. (B) The T-Ag band intensity in A was quantified by the FIJI software. Data were normalized to the Scr control. (C) CV-1 cells transfected with the indicated siRNA were infected with SV40 and the resulting whole cell extracts were subjected to SDS-PAGE and immunoblotting. (D) The T-Ag band intensity in C was quantified by the FIJI software. Data were normalized to the Scr control. (E) CV-1 cells were fixed and stained for Nesprin-2 (red) and either one of the KPNA1, KPNA2, or KPNA4 protein (green) and counterstained with DAPI (blue). Scale bar: 10 µm. (F) Pearson’s coefficient was used to quantify colocalization between KPNA1, KPNA2, or KPNA4 with Nesprin-2. Each data point represents one field of view with at least 10 cells. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001
    Figure Legend Snippet: (A) CV-1 cells transfected with the indicated siRNA were infected with SV40 and the resulting whole cell extracts were subjected to SDS-PAGE followed by immunoblotting. The extent of depletion by the KPNA1, KPNA2, and KPNA4 siRNA is shown in the Western blots below. Data were normalized to the Scr control. (B) The T-Ag band intensity in A was quantified by the FIJI software. Data were normalized to the Scr control. (C) CV-1 cells transfected with the indicated siRNA were infected with SV40 and the resulting whole cell extracts were subjected to SDS-PAGE and immunoblotting. (D) The T-Ag band intensity in C was quantified by the FIJI software. Data were normalized to the Scr control. (E) CV-1 cells were fixed and stained for Nesprin-2 (red) and either one of the KPNA1, KPNA2, or KPNA4 protein (green) and counterstained with DAPI (blue). Scale bar: 10 µm. (F) Pearson’s coefficient was used to quantify colocalization between KPNA1, KPNA2, or KPNA4 with Nesprin-2. Each data point represents one field of view with at least 10 cells. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001

    Techniques Used: Transfection, Infection, SDS Page, Western Blot, Control, Software, Staining

    Related Articles

    Membrane:

    Article Title: Respiratory syncytial virus NS1 inhibits anti-viral Interferon-α-induced JAK/STAT signaling, by limiting the nuclear translocation of STAT1.
    Article Snippet: .. The PVDF membrane was incubated with primary antibody (pSTAT1, 9167, Cell Signalling Technology; pSTAT2 88410, Cell Signalling Technology; STAT1, 9172S, Cell Signalling Technology; STAT2, SC-476, Santa Cruz Biotechnologies; RSV-NS1, a kind gift from Prof. Mike Teng USF, USA (32); KPNA1, 18137–1-AP, Proteintech; b-actin, A5441-.2ML, Sigma-Aldrich) overnight at 4C. .. The membranes were incubated in the appropriate secondary antibody (anti-Rabbit, 11859140, Fisher Scientific or anti-Mouse, 10158113, Fisher Scientific) for 1h before imaging (Bio-Rad Imager). densitometry for each band was carried out using BioRad Image Lab software (Bio-Rad, USA).

    Article Title: Respiratory syncytial virus NS1 inhibits anti-viral Interferon-α-induced JAK/STAT signaling, by limiting the nuclear translocation of STAT1
    Article Snippet: .. The PVDF membrane was incubated with primary antibody (pSTAT1, 9167, Cell Signalling Technology; pSTAT2 88410, Cell Signalling Technology; STAT1, 9172S, Cell Signalling Technology; STAT2, SC-476, Santa Cruz Biotechnologies; RSV-NS1, a kind gift from Prof. Mike Teng USF, USA ( ); KPNA1, 18137–1-AP, Proteintech; β-actin, A5441-.2ML, Sigma-Aldrich) overnight at 4C. .. The membranes were incubated in the appropriate secondary antibody (anti-Rabbit, 11859140, Fisher Scientific or anti-Mouse, 10158113, Fisher Scientific) for 1h before imaging (Bio-Rad Imager). densitometry for each band was carried out using Bio-Rad Image Lab software (Bio-Rad, USA).

    Incubation:

    Article Title: Respiratory syncytial virus NS1 inhibits anti-viral Interferon-α-induced JAK/STAT signaling, by limiting the nuclear translocation of STAT1.
    Article Snippet: .. The PVDF membrane was incubated with primary antibody (pSTAT1, 9167, Cell Signalling Technology; pSTAT2 88410, Cell Signalling Technology; STAT1, 9172S, Cell Signalling Technology; STAT2, SC-476, Santa Cruz Biotechnologies; RSV-NS1, a kind gift from Prof. Mike Teng USF, USA (32); KPNA1, 18137–1-AP, Proteintech; b-actin, A5441-.2ML, Sigma-Aldrich) overnight at 4C. .. The membranes were incubated in the appropriate secondary antibody (anti-Rabbit, 11859140, Fisher Scientific or anti-Mouse, 10158113, Fisher Scientific) for 1h before imaging (Bio-Rad Imager). densitometry for each band was carried out using BioRad Image Lab software (Bio-Rad, USA).

    Article Title: Respiratory syncytial virus NS1 inhibits anti-viral Interferon-α-induced JAK/STAT signaling, by limiting the nuclear translocation of STAT1
    Article Snippet: .. The PVDF membrane was incubated with primary antibody (pSTAT1, 9167, Cell Signalling Technology; pSTAT2 88410, Cell Signalling Technology; STAT1, 9172S, Cell Signalling Technology; STAT2, SC-476, Santa Cruz Biotechnologies; RSV-NS1, a kind gift from Prof. Mike Teng USF, USA ( ); KPNA1, 18137–1-AP, Proteintech; β-actin, A5441-.2ML, Sigma-Aldrich) overnight at 4C. .. The membranes were incubated in the appropriate secondary antibody (anti-Rabbit, 11859140, Fisher Scientific or anti-Mouse, 10158113, Fisher Scientific) for 1h before imaging (Bio-Rad Imager). densitometry for each band was carried out using Bio-Rad Image Lab software (Bio-Rad, USA).

    Western Blot:

    Article Title: SV40 exploits the Nesprin-2-SUN1-KPNA4 axis for stepwise targeting and entry into the host nucleus to promote infection
    Article Snippet: .. Antibodies, along with the companies that were purchase from and the corresponding catalog numbers, are indicated: SUN1 (Invitrogen, MA5-47231), SUN2 (Proteintech, 27556-1-AP), β actin (Cell Signaling, 4967S), SV40 large T-antigen (Western blot: Santa Cruz Biotechnology, SC-53448; Immunofluorescence: Santa Cruz Biotechnology, SC-147), Nesprin-2 (IP and Immunofluorescence: Invitrogen, MA5-18075; Western blot: Bethyl, A305-393A), SV40 VP1 (Abcam, ab53977), SV40 VP2/3 (Abcam, ab53983), Bap31 (Invitrogen, MA 3002), Hsp90 (Santa Cruz Biotechnology, sc-13119), M2 FLAG (Millipore, F3165-1MG), FLAG (Millipore, F7425), BicD2 (Abcam, ab117818), KPNA1 (Proteintech, 18137-1-AP), KPNA2 (Invitrogen, 108191AP150UL), KPNA4 (Invitrogen, PA518239), Mab414 (Abcam, ab24609). ..

    Article Title: Nuclear-capture of endosomes depletes nuclear G-actin to promote SRF/MRTF activation and cancer cell invasion
    Article Snippet: .. 3 n atu re p o rtfo lio | rep o rtin g su m m ary M a rch 2021 Materials & experimental systems n/a Involved in the study Antibodies Eukaryotic cell lines Palaeontology and archaeology Animals and other organisms Human research participants Clinical data Dual use research of concern Methods n/a Involved in the study ChIP-seq Flow cytometry MRI-based neuroimaging Antibodies Antibodies used Validation Eukaryotic cell lines Policy information about cell lines Cell line source(s) Authentication Mycoplasma contamination Commonly misidentified lines (See ICLAC register) For Western blotting and immunofluorescence, antibodies were from the following sources: goat anti-LaminA/C (Santa Cruz, sc-6215), mouse anti-EphA2 (Millipore, 05-480), mouse anti-EphA2 (Santa Cruz, sc-398832), rabbit anti-EphA2 phospho-Ser897 (Cell Signaling, #6347), rabbit anti-EphA2 phospho-Tyr588 (Cell Signaling, #12677), mouse anti-GFP (Immunoprecipitations, Abcam, ab1218), mouse anti-GFP (Western Blot, Santa Cruz, sc-9996), rabbit anti-GFP (Abcam, ab6556), rabbit anti-importin-!5 (KPNA1, Proteintech, 18137-1-AP), mouse anti-importin-"1 (KPNB1, Cell Signaling, #60769), mouse anti-actin (Sigma, A1978), mouse antiRhoG (Millipore, 04-486), mouse anti-Rab17 (Abnova, H00064284-MO1), mouse anti-importin-!7 (Proteintech, 12366-2-AP), rabbit anti-TNPO3 (Abcam, ab109386), mouse anti-CHC (TD1, gift from F. Brodsky), rabbit anti-HistoneH2a (Abcam, ab16563) and rabbit anti-XPO6 (Proteintech, 11408-1-AP), mouse anti-cofilin (Proteintech, 66057-1-Ig) and rabbit anti-cofilin phospho-Ser3 (Santa Cruz, sc-12912-R). .. For immunoprecipitation, mouse antibodies were coupled to magnetic beads conjugated to anti-mouse IgG (Invitrogen; Dynabeads Sheep anti-mouse IgG; catalogue number 11031).

    Article Title: Respiratory syncytial virus NS1 inhibits anti-viral Interferon-α-induced JAK/STAT signaling, by limiting the nuclear translocation of STAT1.
    Article Snippet: .. Lysates were immunoprecipitated with STAT1 (9172S, Cell Signalling Technology) and protein A/G agarose beads (Santa Cruz Biotechnologies) before immunoblotting for STAT1 (9172S, Cell Signalling Technology), RSV-NS1 (a gift from Prof Michael Teng, USF), KPNA1 (18137–1-AP, Proteintech), and bactin (A5441, Sigma-Aldrich). ..

    Article Title: Respiratory syncytial virus NS1 inhibits anti-viral Interferon-α-induced JAK/STAT signaling, by limiting the nuclear translocation of STAT1
    Article Snippet: .. Lysates were immunoprecipitated with STAT1 (9172S, Cell Signalling Technology) and protein A/G agarose beads (Santa Cruz Biotechnologies) before immunoblotting for STAT1 (9172S, Cell Signalling Technology), RSV-NS1 (a gift from Prof Michael Teng, USF), KPNA1 (18137–1-AP, Proteintech), and β-actin (A5441, Sigma-Aldrich). ..

    Immunofluorescence:

    Article Title: SV40 exploits the Nesprin-2-SUN1-KPNA4 axis for stepwise targeting and entry into the host nucleus to promote infection
    Article Snippet: .. Antibodies, along with the companies that were purchase from and the corresponding catalog numbers, are indicated: SUN1 (Invitrogen, MA5-47231), SUN2 (Proteintech, 27556-1-AP), β actin (Cell Signaling, 4967S), SV40 large T-antigen (Western blot: Santa Cruz Biotechnology, SC-53448; Immunofluorescence: Santa Cruz Biotechnology, SC-147), Nesprin-2 (IP and Immunofluorescence: Invitrogen, MA5-18075; Western blot: Bethyl, A305-393A), SV40 VP1 (Abcam, ab53977), SV40 VP2/3 (Abcam, ab53983), Bap31 (Invitrogen, MA 3002), Hsp90 (Santa Cruz Biotechnology, sc-13119), M2 FLAG (Millipore, F3165-1MG), FLAG (Millipore, F7425), BicD2 (Abcam, ab117818), KPNA1 (Proteintech, 18137-1-AP), KPNA2 (Invitrogen, 108191AP150UL), KPNA4 (Invitrogen, PA518239), Mab414 (Abcam, ab24609). ..

    Article Title: Nuclear-capture of endosomes depletes nuclear G-actin to promote SRF/MRTF activation and cancer cell invasion
    Article Snippet: .. 3 n atu re p o rtfo lio | rep o rtin g su m m ary M a rch 2021 Materials & experimental systems n/a Involved in the study Antibodies Eukaryotic cell lines Palaeontology and archaeology Animals and other organisms Human research participants Clinical data Dual use research of concern Methods n/a Involved in the study ChIP-seq Flow cytometry MRI-based neuroimaging Antibodies Antibodies used Validation Eukaryotic cell lines Policy information about cell lines Cell line source(s) Authentication Mycoplasma contamination Commonly misidentified lines (See ICLAC register) For Western blotting and immunofluorescence, antibodies were from the following sources: goat anti-LaminA/C (Santa Cruz, sc-6215), mouse anti-EphA2 (Millipore, 05-480), mouse anti-EphA2 (Santa Cruz, sc-398832), rabbit anti-EphA2 phospho-Ser897 (Cell Signaling, #6347), rabbit anti-EphA2 phospho-Tyr588 (Cell Signaling, #12677), mouse anti-GFP (Immunoprecipitations, Abcam, ab1218), mouse anti-GFP (Western Blot, Santa Cruz, sc-9996), rabbit anti-GFP (Abcam, ab6556), rabbit anti-importin-!5 (KPNA1, Proteintech, 18137-1-AP), mouse anti-importin-"1 (KPNB1, Cell Signaling, #60769), mouse anti-actin (Sigma, A1978), mouse antiRhoG (Millipore, 04-486), mouse anti-Rab17 (Abnova, H00064284-MO1), mouse anti-importin-!7 (Proteintech, 12366-2-AP), rabbit anti-TNPO3 (Abcam, ab109386), mouse anti-CHC (TD1, gift from F. Brodsky), rabbit anti-HistoneH2a (Abcam, ab16563) and rabbit anti-XPO6 (Proteintech, 11408-1-AP), mouse anti-cofilin (Proteintech, 66057-1-Ig) and rabbit anti-cofilin phospho-Ser3 (Santa Cruz, sc-12912-R). .. For immunoprecipitation, mouse antibodies were coupled to magnetic beads conjugated to anti-mouse IgG (Invitrogen; Dynabeads Sheep anti-mouse IgG; catalogue number 11031).

    Chromatin Immunoprecipitation:

    Article Title: Nuclear-capture of endosomes depletes nuclear G-actin to promote SRF/MRTF activation and cancer cell invasion
    Article Snippet: .. 3 n atu re p o rtfo lio | rep o rtin g su m m ary M a rch 2021 Materials & experimental systems n/a Involved in the study Antibodies Eukaryotic cell lines Palaeontology and archaeology Animals and other organisms Human research participants Clinical data Dual use research of concern Methods n/a Involved in the study ChIP-seq Flow cytometry MRI-based neuroimaging Antibodies Antibodies used Validation Eukaryotic cell lines Policy information about cell lines Cell line source(s) Authentication Mycoplasma contamination Commonly misidentified lines (See ICLAC register) For Western blotting and immunofluorescence, antibodies were from the following sources: goat anti-LaminA/C (Santa Cruz, sc-6215), mouse anti-EphA2 (Millipore, 05-480), mouse anti-EphA2 (Santa Cruz, sc-398832), rabbit anti-EphA2 phospho-Ser897 (Cell Signaling, #6347), rabbit anti-EphA2 phospho-Tyr588 (Cell Signaling, #12677), mouse anti-GFP (Immunoprecipitations, Abcam, ab1218), mouse anti-GFP (Western Blot, Santa Cruz, sc-9996), rabbit anti-GFP (Abcam, ab6556), rabbit anti-importin-!5 (KPNA1, Proteintech, 18137-1-AP), mouse anti-importin-"1 (KPNB1, Cell Signaling, #60769), mouse anti-actin (Sigma, A1978), mouse antiRhoG (Millipore, 04-486), mouse anti-Rab17 (Abnova, H00064284-MO1), mouse anti-importin-!7 (Proteintech, 12366-2-AP), rabbit anti-TNPO3 (Abcam, ab109386), mouse anti-CHC (TD1, gift from F. Brodsky), rabbit anti-HistoneH2a (Abcam, ab16563) and rabbit anti-XPO6 (Proteintech, 11408-1-AP), mouse anti-cofilin (Proteintech, 66057-1-Ig) and rabbit anti-cofilin phospho-Ser3 (Santa Cruz, sc-12912-R). .. For immunoprecipitation, mouse antibodies were coupled to magnetic beads conjugated to anti-mouse IgG (Invitrogen; Dynabeads Sheep anti-mouse IgG; catalogue number 11031).

    Flow Cytometry:

    Article Title: Nuclear-capture of endosomes depletes nuclear G-actin to promote SRF/MRTF activation and cancer cell invasion
    Article Snippet: .. 3 n atu re p o rtfo lio | rep o rtin g su m m ary M a rch 2021 Materials & experimental systems n/a Involved in the study Antibodies Eukaryotic cell lines Palaeontology and archaeology Animals and other organisms Human research participants Clinical data Dual use research of concern Methods n/a Involved in the study ChIP-seq Flow cytometry MRI-based neuroimaging Antibodies Antibodies used Validation Eukaryotic cell lines Policy information about cell lines Cell line source(s) Authentication Mycoplasma contamination Commonly misidentified lines (See ICLAC register) For Western blotting and immunofluorescence, antibodies were from the following sources: goat anti-LaminA/C (Santa Cruz, sc-6215), mouse anti-EphA2 (Millipore, 05-480), mouse anti-EphA2 (Santa Cruz, sc-398832), rabbit anti-EphA2 phospho-Ser897 (Cell Signaling, #6347), rabbit anti-EphA2 phospho-Tyr588 (Cell Signaling, #12677), mouse anti-GFP (Immunoprecipitations, Abcam, ab1218), mouse anti-GFP (Western Blot, Santa Cruz, sc-9996), rabbit anti-GFP (Abcam, ab6556), rabbit anti-importin-!5 (KPNA1, Proteintech, 18137-1-AP), mouse anti-importin-"1 (KPNB1, Cell Signaling, #60769), mouse anti-actin (Sigma, A1978), mouse antiRhoG (Millipore, 04-486), mouse anti-Rab17 (Abnova, H00064284-MO1), mouse anti-importin-!7 (Proteintech, 12366-2-AP), rabbit anti-TNPO3 (Abcam, ab109386), mouse anti-CHC (TD1, gift from F. Brodsky), rabbit anti-HistoneH2a (Abcam, ab16563) and rabbit anti-XPO6 (Proteintech, 11408-1-AP), mouse anti-cofilin (Proteintech, 66057-1-Ig) and rabbit anti-cofilin phospho-Ser3 (Santa Cruz, sc-12912-R). .. For immunoprecipitation, mouse antibodies were coupled to magnetic beads conjugated to anti-mouse IgG (Invitrogen; Dynabeads Sheep anti-mouse IgG; catalogue number 11031).

    Magnetic Resonance Imaging:

    Article Title: Nuclear-capture of endosomes depletes nuclear G-actin to promote SRF/MRTF activation and cancer cell invasion
    Article Snippet: .. 3 n atu re p o rtfo lio | rep o rtin g su m m ary M a rch 2021 Materials & experimental systems n/a Involved in the study Antibodies Eukaryotic cell lines Palaeontology and archaeology Animals and other organisms Human research participants Clinical data Dual use research of concern Methods n/a Involved in the study ChIP-seq Flow cytometry MRI-based neuroimaging Antibodies Antibodies used Validation Eukaryotic cell lines Policy information about cell lines Cell line source(s) Authentication Mycoplasma contamination Commonly misidentified lines (See ICLAC register) For Western blotting and immunofluorescence, antibodies were from the following sources: goat anti-LaminA/C (Santa Cruz, sc-6215), mouse anti-EphA2 (Millipore, 05-480), mouse anti-EphA2 (Santa Cruz, sc-398832), rabbit anti-EphA2 phospho-Ser897 (Cell Signaling, #6347), rabbit anti-EphA2 phospho-Tyr588 (Cell Signaling, #12677), mouse anti-GFP (Immunoprecipitations, Abcam, ab1218), mouse anti-GFP (Western Blot, Santa Cruz, sc-9996), rabbit anti-GFP (Abcam, ab6556), rabbit anti-importin-!5 (KPNA1, Proteintech, 18137-1-AP), mouse anti-importin-"1 (KPNB1, Cell Signaling, #60769), mouse anti-actin (Sigma, A1978), mouse antiRhoG (Millipore, 04-486), mouse anti-Rab17 (Abnova, H00064284-MO1), mouse anti-importin-!7 (Proteintech, 12366-2-AP), rabbit anti-TNPO3 (Abcam, ab109386), mouse anti-CHC (TD1, gift from F. Brodsky), rabbit anti-HistoneH2a (Abcam, ab16563) and rabbit anti-XPO6 (Proteintech, 11408-1-AP), mouse anti-cofilin (Proteintech, 66057-1-Ig) and rabbit anti-cofilin phospho-Ser3 (Santa Cruz, sc-12912-R). .. For immunoprecipitation, mouse antibodies were coupled to magnetic beads conjugated to anti-mouse IgG (Invitrogen; Dynabeads Sheep anti-mouse IgG; catalogue number 11031).

    Biomarker Discovery:

    Article Title: Nuclear-capture of endosomes depletes nuclear G-actin to promote SRF/MRTF activation and cancer cell invasion
    Article Snippet: .. 3 n atu re p o rtfo lio | rep o rtin g su m m ary M a rch 2021 Materials & experimental systems n/a Involved in the study Antibodies Eukaryotic cell lines Palaeontology and archaeology Animals and other organisms Human research participants Clinical data Dual use research of concern Methods n/a Involved in the study ChIP-seq Flow cytometry MRI-based neuroimaging Antibodies Antibodies used Validation Eukaryotic cell lines Policy information about cell lines Cell line source(s) Authentication Mycoplasma contamination Commonly misidentified lines (See ICLAC register) For Western blotting and immunofluorescence, antibodies were from the following sources: goat anti-LaminA/C (Santa Cruz, sc-6215), mouse anti-EphA2 (Millipore, 05-480), mouse anti-EphA2 (Santa Cruz, sc-398832), rabbit anti-EphA2 phospho-Ser897 (Cell Signaling, #6347), rabbit anti-EphA2 phospho-Tyr588 (Cell Signaling, #12677), mouse anti-GFP (Immunoprecipitations, Abcam, ab1218), mouse anti-GFP (Western Blot, Santa Cruz, sc-9996), rabbit anti-GFP (Abcam, ab6556), rabbit anti-importin-!5 (KPNA1, Proteintech, 18137-1-AP), mouse anti-importin-"1 (KPNB1, Cell Signaling, #60769), mouse anti-actin (Sigma, A1978), mouse antiRhoG (Millipore, 04-486), mouse anti-Rab17 (Abnova, H00064284-MO1), mouse anti-importin-!7 (Proteintech, 12366-2-AP), rabbit anti-TNPO3 (Abcam, ab109386), mouse anti-CHC (TD1, gift from F. Brodsky), rabbit anti-HistoneH2a (Abcam, ab16563) and rabbit anti-XPO6 (Proteintech, 11408-1-AP), mouse anti-cofilin (Proteintech, 66057-1-Ig) and rabbit anti-cofilin phospho-Ser3 (Santa Cruz, sc-12912-R). .. For immunoprecipitation, mouse antibodies were coupled to magnetic beads conjugated to anti-mouse IgG (Invitrogen; Dynabeads Sheep anti-mouse IgG; catalogue number 11031).

    Immunoprecipitation:

    Article Title: Respiratory syncytial virus NS1 inhibits anti-viral Interferon-α-induced JAK/STAT signaling, by limiting the nuclear translocation of STAT1.
    Article Snippet: .. Lysates were immunoprecipitated with STAT1 (9172S, Cell Signalling Technology) and protein A/G agarose beads (Santa Cruz Biotechnologies) before immunoblotting for STAT1 (9172S, Cell Signalling Technology), RSV-NS1 (a gift from Prof Michael Teng, USF), KPNA1 (18137–1-AP, Proteintech), and bactin (A5441, Sigma-Aldrich). ..

    Article Title: Respiratory syncytial virus NS1 inhibits anti-viral Interferon-α-induced JAK/STAT signaling, by limiting the nuclear translocation of STAT1
    Article Snippet: .. Lysates were immunoprecipitated with STAT1 (9172S, Cell Signalling Technology) and protein A/G agarose beads (Santa Cruz Biotechnologies) before immunoblotting for STAT1 (9172S, Cell Signalling Technology), RSV-NS1 (a gift from Prof Michael Teng, USF), KPNA1 (18137–1-AP, Proteintech), and β-actin (A5441, Sigma-Aldrich). ..

    other:

    Article Title: Ivermectin Inhibits HBV Entry into the Nucleus by Suppressing KPNA2
    Article Snippet: KPNA1 , Proteintech , 18137-1-AP , Rabbit , 1:1000.



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    Proteintech anti importin alpha 5 kpna1
    Structural analysis of KPNA binding to TDP-43-NLS. Computational CABS-DOCK analysis reveals TDP-43 nuclear localisation signal (NLS, blue) and KPNA binding (left) together with corresponding molecular contact maps (right) for (A) <t>KPNA1</t> (PDB: 6WX9, green), (B) KPNA4 (PDB: 5XZX, chartreuse) and (C) KPNA6 (PDB: 4UAD, cyan). The corresponding 2D contact map shows the intermolecular interaction between the minor and major binding site of the NLS (squares) and the active residues of the KPNA proteins (coloured spheres) which is mediated via conserved Tryptophan (W) residues. Interaction types are, electrostatic and salt-bridge (orange), hydrogen bonds (green), hydrophobic contact (pink). Note, all models generated reveal the bipartite binding pattern, with the N-terminal P1´- P5´ residues (KRKMD) interfacing with the minor groove residues (ARM6-8) of the KPNA protein, and the C-terminal P1’ – P5’ residues (VKRAV) dovetailing with the major groove (ARM2-4). (D–F) Comparison between CABS-DOCK (blue peptide) and HPEP-DOCK (red peptide) computational models reveals correspondences for binding prediction between TDP-43-NLS and (D) KPNA1, (E) KPNA4 or (F) KPNA6.
    Anti Importin Alpha 5 Kpna1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti importin alpha 5  (Proteintech)
    96
    Proteintech anti importin alpha 5
    Structural analysis of KPNA binding to TDP-43-NLS. Computational CABS-DOCK analysis reveals TDP-43 nuclear localisation signal (NLS, blue) and KPNA binding (left) together with corresponding molecular contact maps (right) for (A) <t>KPNA1</t> (PDB: 6WX9, green), (B) KPNA4 (PDB: 5XZX, chartreuse) and (C) KPNA6 (PDB: 4UAD, cyan). The corresponding 2D contact map shows the intermolecular interaction between the minor and major binding site of the NLS (squares) and the active residues of the KPNA proteins (coloured spheres) which is mediated via conserved Tryptophan (W) residues. Interaction types are, electrostatic and salt-bridge (orange), hydrogen bonds (green), hydrophobic contact (pink). Note, all models generated reveal the bipartite binding pattern, with the N-terminal P1´- P5´ residues (KRKMD) interfacing with the minor groove residues (ARM6-8) of the KPNA protein, and the C-terminal P1’ – P5’ residues (VKRAV) dovetailing with the major groove (ARM2-4). (D–F) Comparison between CABS-DOCK (blue peptide) and HPEP-DOCK (red peptide) computational models reveals correspondences for binding prediction between TDP-43-NLS and (D) KPNA1, (E) KPNA4 or (F) KPNA6.
    Anti Importin Alpha 5, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti-kpna1 antibody  (Thermo Fisher)
    90
    Thermo Fisher anti-kpna1 antibody
    Structural analysis of KPNA binding to TDP-43-NLS. Computational CABS-DOCK analysis reveals TDP-43 nuclear localisation signal (NLS, blue) and KPNA binding (left) together with corresponding molecular contact maps (right) for (A) <t>KPNA1</t> (PDB: 6WX9, green), (B) KPNA4 (PDB: 5XZX, chartreuse) and (C) KPNA6 (PDB: 4UAD, cyan). The corresponding 2D contact map shows the intermolecular interaction between the minor and major binding site of the NLS (squares) and the active residues of the KPNA proteins (coloured spheres) which is mediated via conserved Tryptophan (W) residues. Interaction types are, electrostatic and salt-bridge (orange), hydrogen bonds (green), hydrophobic contact (pink). Note, all models generated reveal the bipartite binding pattern, with the N-terminal P1´- P5´ residues (KRKMD) interfacing with the minor groove residues (ARM6-8) of the KPNA protein, and the C-terminal P1’ – P5’ residues (VKRAV) dovetailing with the major groove (ARM2-4). (D–F) Comparison between CABS-DOCK (blue peptide) and HPEP-DOCK (red peptide) computational models reveals correspondences for binding prediction between TDP-43-NLS and (D) KPNA1, (E) KPNA4 or (F) KPNA6.
    Anti Kpna1 Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti kpna1  (Proteintech)
    93
    Proteintech anti kpna1
    Structural analysis of KPNA binding to TDP-43-NLS. Computational CABS-DOCK analysis reveals TDP-43 nuclear localisation signal (NLS, blue) and KPNA binding (left) together with corresponding molecular contact maps (right) for (A) <t>KPNA1</t> (PDB: 6WX9, green), (B) KPNA4 (PDB: 5XZX, chartreuse) and (C) KPNA6 (PDB: 4UAD, cyan). The corresponding 2D contact map shows the intermolecular interaction between the minor and major binding site of the NLS (squares) and the active residues of the KPNA proteins (coloured spheres) which is mediated via conserved Tryptophan (W) residues. Interaction types are, electrostatic and salt-bridge (orange), hydrogen bonds (green), hydrophobic contact (pink). Note, all models generated reveal the bipartite binding pattern, with the N-terminal P1´- P5´ residues (KRKMD) interfacing with the minor groove residues (ARM6-8) of the KPNA protein, and the C-terminal P1’ – P5’ residues (VKRAV) dovetailing with the major groove (ARM2-4). (D–F) Comparison between CABS-DOCK (blue peptide) and HPEP-DOCK (red peptide) computational models reveals correspondences for binding prediction between TDP-43-NLS and (D) KPNA1, (E) KPNA4 or (F) KPNA6.
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    anti-kpna1 antibody  (Abnova)
    90
    Abnova anti-kpna1 antibody
    Structural analysis of KPNA binding to TDP-43-NLS. Computational CABS-DOCK analysis reveals TDP-43 nuclear localisation signal (NLS, blue) and KPNA binding (left) together with corresponding molecular contact maps (right) for (A) <t>KPNA1</t> (PDB: 6WX9, green), (B) KPNA4 (PDB: 5XZX, chartreuse) and (C) KPNA6 (PDB: 4UAD, cyan). The corresponding 2D contact map shows the intermolecular interaction between the minor and major binding site of the NLS (squares) and the active residues of the KPNA proteins (coloured spheres) which is mediated via conserved Tryptophan (W) residues. Interaction types are, electrostatic and salt-bridge (orange), hydrogen bonds (green), hydrophobic contact (pink). Note, all models generated reveal the bipartite binding pattern, with the N-terminal P1´- P5´ residues (KRKMD) interfacing with the minor groove residues (ARM6-8) of the KPNA protein, and the C-terminal P1’ – P5’ residues (VKRAV) dovetailing with the major groove (ARM2-4). (D–F) Comparison between CABS-DOCK (blue peptide) and HPEP-DOCK (red peptide) computational models reveals correspondences for binding prediction between TDP-43-NLS and (D) KPNA1, (E) KPNA4 or (F) KPNA6.
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    Image Search Results


    (A) CV-1 cells transfected with the indicated siRNA were infected with SV40 and the resulting whole cell extracts were subjected to SDS-PAGE followed by immunoblotting. The extent of depletion by the KPNA1, KPNA2, and KPNA4 siRNA is shown in the Western blots below. Data were normalized to the Scr control. (B) The T-Ag band intensity in A was quantified by the FIJI software. Data were normalized to the Scr control. (C) CV-1 cells transfected with the indicated siRNA were infected with SV40 and the resulting whole cell extracts were subjected to SDS-PAGE and immunoblotting. (D) The T-Ag band intensity in C was quantified by the FIJI software. Data were normalized to the Scr control. (E) CV-1 cells were fixed and stained for Nesprin-2 (red) and either one of the KPNA1, KPNA2, or KPNA4 protein (green) and counterstained with DAPI (blue). Scale bar: 10 µm. (F) Pearson’s coefficient was used to quantify colocalization between KPNA1, KPNA2, or KPNA4 with Nesprin-2. Each data point represents one field of view with at least 10 cells. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001

    Journal: bioRxiv

    Article Title: SV40 exploits the Nesprin-2-SUN1-KPNA4 axis for stepwise targeting and entry into the host nucleus to promote infection

    doi: 10.64898/2026.03.15.711898

    Figure Lengend Snippet: (A) CV-1 cells transfected with the indicated siRNA were infected with SV40 and the resulting whole cell extracts were subjected to SDS-PAGE followed by immunoblotting. The extent of depletion by the KPNA1, KPNA2, and KPNA4 siRNA is shown in the Western blots below. Data were normalized to the Scr control. (B) The T-Ag band intensity in A was quantified by the FIJI software. Data were normalized to the Scr control. (C) CV-1 cells transfected with the indicated siRNA were infected with SV40 and the resulting whole cell extracts were subjected to SDS-PAGE and immunoblotting. (D) The T-Ag band intensity in C was quantified by the FIJI software. Data were normalized to the Scr control. (E) CV-1 cells were fixed and stained for Nesprin-2 (red) and either one of the KPNA1, KPNA2, or KPNA4 protein (green) and counterstained with DAPI (blue). Scale bar: 10 µm. (F) Pearson’s coefficient was used to quantify colocalization between KPNA1, KPNA2, or KPNA4 with Nesprin-2. Each data point represents one field of view with at least 10 cells. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001

    Article Snippet: Antibodies, along with the companies that were purchase from and the corresponding catalog numbers, are indicated: SUN1 (Invitrogen, MA5-47231), SUN2 (Proteintech, 27556-1-AP), β actin (Cell Signaling, 4967S), SV40 large T-antigen (Western blot: Santa Cruz Biotechnology, SC-53448; Immunofluorescence: Santa Cruz Biotechnology, SC-147), Nesprin-2 (IP and Immunofluorescence: Invitrogen, MA5-18075; Western blot: Bethyl, A305-393A), SV40 VP1 (Abcam, ab53977), SV40 VP2/3 (Abcam, ab53983), Bap31 (Invitrogen, MA 3002), Hsp90 (Santa Cruz Biotechnology, sc-13119), M2 FLAG (Millipore, F3165-1MG), FLAG (Millipore, F7425), BicD2 (Abcam, ab117818), KPNA1 (Proteintech, 18137-1-AP), KPNA2 (Invitrogen, 108191AP150UL), KPNA4 (Invitrogen, PA518239), Mab414 (Abcam, ab24609).

    Techniques: Transfection, Infection, SDS Page, Western Blot, Control, Software, Staining

    Structural analysis of KPNA binding to TDP-43-NLS. Computational CABS-DOCK analysis reveals TDP-43 nuclear localisation signal (NLS, blue) and KPNA binding (left) together with corresponding molecular contact maps (right) for (A) KPNA1 (PDB: 6WX9, green), (B) KPNA4 (PDB: 5XZX, chartreuse) and (C) KPNA6 (PDB: 4UAD, cyan). The corresponding 2D contact map shows the intermolecular interaction between the minor and major binding site of the NLS (squares) and the active residues of the KPNA proteins (coloured spheres) which is mediated via conserved Tryptophan (W) residues. Interaction types are, electrostatic and salt-bridge (orange), hydrogen bonds (green), hydrophobic contact (pink). Note, all models generated reveal the bipartite binding pattern, with the N-terminal P1´- P5´ residues (KRKMD) interfacing with the minor groove residues (ARM6-8) of the KPNA protein, and the C-terminal P1’ – P5’ residues (VKRAV) dovetailing with the major groove (ARM2-4). (D–F) Comparison between CABS-DOCK (blue peptide) and HPEP-DOCK (red peptide) computational models reveals correspondences for binding prediction between TDP-43-NLS and (D) KPNA1, (E) KPNA4 or (F) KPNA6.

    Journal: Frontiers in Neuroscience

    Article Title: Accumulation of TDP-43 causes karyopherin-α4 pathology that characterises amyotrophic lateral sclerosis

    doi: 10.3389/fnins.2025.1558227

    Figure Lengend Snippet: Structural analysis of KPNA binding to TDP-43-NLS. Computational CABS-DOCK analysis reveals TDP-43 nuclear localisation signal (NLS, blue) and KPNA binding (left) together with corresponding molecular contact maps (right) for (A) KPNA1 (PDB: 6WX9, green), (B) KPNA4 (PDB: 5XZX, chartreuse) and (C) KPNA6 (PDB: 4UAD, cyan). The corresponding 2D contact map shows the intermolecular interaction between the minor and major binding site of the NLS (squares) and the active residues of the KPNA proteins (coloured spheres) which is mediated via conserved Tryptophan (W) residues. Interaction types are, electrostatic and salt-bridge (orange), hydrogen bonds (green), hydrophobic contact (pink). Note, all models generated reveal the bipartite binding pattern, with the N-terminal P1´- P5´ residues (KRKMD) interfacing with the minor groove residues (ARM6-8) of the KPNA protein, and the C-terminal P1’ – P5’ residues (VKRAV) dovetailing with the major groove (ARM2-4). (D–F) Comparison between CABS-DOCK (blue peptide) and HPEP-DOCK (red peptide) computational models reveals correspondences for binding prediction between TDP-43-NLS and (D) KPNA1, (E) KPNA4 or (F) KPNA6.

    Article Snippet: Primary antibodies used were: KPNA1 (mouse, Santa Cruz Biotechnology, sc-101292, 1:750), KPNA3 (mouse, Santa Cruz Biotechnology, sc-514101, 1:750), KPNA4 (rabbit, Proteintech, 12,463-AP, 1:750), KPNA6 (mouse, Santa Cruz Biotechnology, sc-390055, 1:750), KPNA7 (rabbit, GeneTex, GTX31991, 1:1,000), TDP-43 (goat, Abcam, ab80608, 1:100) KPNA4 (mouse, SCBT, sc-390535, 1:50), Myc (rabbit, Proteintech, 60,003-2-Ig, 1:250) and Streptavidine-Atto488 (Rockland laboratories, S000-52).

    Techniques: Binding Assay, Generated, Comparison