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rabbit α twa1  (Novus Biologicals)


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    Structured Review

    Novus Biologicals rabbit α twa1
    (A) Schematic representation of the stability profiling experiment, in which the Ultimate ORFeome GPS expression library was used to identify proteins exhibiting increased stability in MAEA KO and <t>TWA1</t> KO cells. (B-C) Identification of AAMP, AEN and NATD1 as CTLH substrates. Screen profiles are depicted in (B) , while individual validation experiments by flow cytometry in the presence and absence of Torin-1 (dotted lines) are shown in (C) . See also . (D) Schematic representation of the proteomic experiment, in which TMT mass spectrometry was used to identify proteins more abundant in cells lacking the CTLH subunits TWA1 and Muskelin. Cells expressing GPS-ZMYND19 were used to allow purification of populations of cells in which TWA1 and Muskelin had been successfully ablated by FACS. See also . (E-F) AAMP is more abundant in cells lacking CTLH subunits. The scatterplot in (E) represents the mean fold change of each protein quantified in both TWA1 KO and Muskelin KO cells, with proteins showing a >1.2-fold increase in abundance in both conditions highlighted in red; the performance of AAMP compared to the known substrate HMGCS1 is depicted in (F) . Exogenous expression of ZMYND19 precludes assessment of the true magnitude of the stabilization of the endogenous ZMYND19 protein in this experiment.
    Rabbit α Twa1, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+twa1/TWA1+Antibody/bio_rxiv__64898__2026__01__14__698769-206-8-10
    Average 94 stars, based on 4 article reviews
    rabbit α twa1 - by Bioz Stars, 2026-10
    94/100 stars

    Images

    1) Product Images from "Proteome-wide C-degron activity profiling connects conditional regulation of the CTLH E3 ligase complex to ribosome biogenesis"

    Article Title: Proteome-wide C-degron activity profiling connects conditional regulation of the CTLH E3 ligase complex to ribosome biogenesis

    Journal: bioRxiv

    doi: 10.64898/2026.01.14.698769

    (A) Schematic representation of the stability profiling experiment, in which the Ultimate ORFeome GPS expression library was used to identify proteins exhibiting increased stability in MAEA KO and TWA1 KO cells. (B-C) Identification of AAMP, AEN and NATD1 as CTLH substrates. Screen profiles are depicted in (B) , while individual validation experiments by flow cytometry in the presence and absence of Torin-1 (dotted lines) are shown in (C) . See also . (D) Schematic representation of the proteomic experiment, in which TMT mass spectrometry was used to identify proteins more abundant in cells lacking the CTLH subunits TWA1 and Muskelin. Cells expressing GPS-ZMYND19 were used to allow purification of populations of cells in which TWA1 and Muskelin had been successfully ablated by FACS. See also . (E-F) AAMP is more abundant in cells lacking CTLH subunits. The scatterplot in (E) represents the mean fold change of each protein quantified in both TWA1 KO and Muskelin KO cells, with proteins showing a >1.2-fold increase in abundance in both conditions highlighted in red; the performance of AAMP compared to the known substrate HMGCS1 is depicted in (F) . Exogenous expression of ZMYND19 precludes assessment of the true magnitude of the stabilization of the endogenous ZMYND19 protein in this experiment.
    Figure Legend Snippet: (A) Schematic representation of the stability profiling experiment, in which the Ultimate ORFeome GPS expression library was used to identify proteins exhibiting increased stability in MAEA KO and TWA1 KO cells. (B-C) Identification of AAMP, AEN and NATD1 as CTLH substrates. Screen profiles are depicted in (B) , while individual validation experiments by flow cytometry in the presence and absence of Torin-1 (dotted lines) are shown in (C) . See also . (D) Schematic representation of the proteomic experiment, in which TMT mass spectrometry was used to identify proteins more abundant in cells lacking the CTLH subunits TWA1 and Muskelin. Cells expressing GPS-ZMYND19 were used to allow purification of populations of cells in which TWA1 and Muskelin had been successfully ablated by FACS. See also . (E-F) AAMP is more abundant in cells lacking CTLH subunits. The scatterplot in (E) represents the mean fold change of each protein quantified in both TWA1 KO and Muskelin KO cells, with proteins showing a >1.2-fold increase in abundance in both conditions highlighted in red; the performance of AAMP compared to the known substrate HMGCS1 is depicted in (F) . Exogenous expression of ZMYND19 precludes assessment of the true magnitude of the stabilization of the endogenous ZMYND19 protein in this experiment.

    Techniques Used: Expressing, Biomarker Discovery, Flow Cytometry, Mass Spectrometry, Purification

    Related Articles

    other:

    Article Title: Distinct nuclear and cytoplasmic assemblies and interactomes of the mammalian CTLH E3 ligase complex.
    Article Snippet: Gels were transferred onto polyvinylidene fluoride membranes, blocked in 5% milk and hybridized with the following primary antibodies: anti-ARMC8 (1:500; E-1, sc-365307, Santa Cruz Biotechnology); anti-MAEA (1:200; AF7288, R&D Systems); anti-muskelin (1:500; C-12, sc-398956, Santa Cruz Biotechnology); anti-RanBPM (1:4000; 5 M, 71-001, Bioacademia); anti-TWA1 (1:200; NBP1-32596, Novus Biologicals); anti-vinculin (1:10,000; E1E9V, Cell Signaling Technology); anti-WDR26 (1:4000; ab85962, Abcam – this antibody also gives rise to non-specific products as shown in Fig. S1); anti-RMND5A (1:2000; custom-made antibody from Yenzym Antibodies); anti-SAP62 (1:1000; A-3, sc-390444, Santa Cruz Biotechnology); tankyrase-1/2 (1:1000; E-10, sc-365897, Santa Cruz Biotechnology); anti-HDAC2 (1:500; 5113, Cell Signaling Technology); anti-macroH2A1 (1:1000; ab37264, Abcam); anti-p14ARF (1:1000; ARF 4C6/4, sc-53392, Santa Cruz Biotechnology); anti-GAPDH (1:5000; 6C5, sc-32233, Santa Cruz Biotechnology); anti-actin (1:10,000; A5441, Sigma-Aldrich); and anti-lamin A/C (1:1000; E1, sc-376248).



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    (A) Schematic representation of the stability profiling experiment, in which the Ultimate ORFeome GPS expression library was used to identify proteins exhibiting increased stability in MAEA KO and <t>TWA1</t> KO cells. (B-C) Identification of AAMP, AEN and NATD1 as CTLH substrates. Screen profiles are depicted in (B) , while individual validation experiments by flow cytometry in the presence and absence of Torin-1 (dotted lines) are shown in (C) . See also . (D) Schematic representation of the proteomic experiment, in which TMT mass spectrometry was used to identify proteins more abundant in cells lacking the CTLH subunits TWA1 and Muskelin. Cells expressing GPS-ZMYND19 were used to allow purification of populations of cells in which TWA1 and Muskelin had been successfully ablated by FACS. See also . (E-F) AAMP is more abundant in cells lacking CTLH subunits. The scatterplot in (E) represents the mean fold change of each protein quantified in both TWA1 KO and Muskelin KO cells, with proteins showing a >1.2-fold increase in abundance in both conditions highlighted in red; the performance of AAMP compared to the known substrate HMGCS1 is depicted in (F) . Exogenous expression of ZMYND19 precludes assessment of the true magnitude of the stabilization of the endogenous ZMYND19 protein in this experiment.
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    (A) Schematic representation of the stability profiling experiment, in which the Ultimate ORFeome GPS expression library was used to identify proteins exhibiting increased stability in MAEA KO and <t>TWA1</t> KO cells. (B-C) Identification of AAMP, AEN and NATD1 as CTLH substrates. Screen profiles are depicted in (B) , while individual validation experiments by flow cytometry in the presence and absence of Torin-1 (dotted lines) are shown in (C) . See also . (D) Schematic representation of the proteomic experiment, in which TMT mass spectrometry was used to identify proteins more abundant in cells lacking the CTLH subunits TWA1 and Muskelin. Cells expressing GPS-ZMYND19 were used to allow purification of populations of cells in which TWA1 and Muskelin had been successfully ablated by FACS. See also . (E-F) AAMP is more abundant in cells lacking CTLH subunits. The scatterplot in (E) represents the mean fold change of each protein quantified in both TWA1 KO and Muskelin KO cells, with proteins showing a >1.2-fold increase in abundance in both conditions highlighted in red; the performance of AAMP compared to the known substrate HMGCS1 is depicted in (F) . Exogenous expression of ZMYND19 precludes assessment of the true magnitude of the stabilization of the endogenous ZMYND19 protein in this experiment.
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    (A) Schematic representation of the stability profiling experiment, in which the Ultimate ORFeome GPS expression library was used to identify proteins exhibiting increased stability in MAEA KO and <t>TWA1</t> KO cells. (B-C) Identification of AAMP, AEN and NATD1 as CTLH substrates. Screen profiles are depicted in (B) , while individual validation experiments by flow cytometry in the presence and absence of Torin-1 (dotted lines) are shown in (C) . See also . (D) Schematic representation of the proteomic experiment, in which TMT mass spectrometry was used to identify proteins more abundant in cells lacking the CTLH subunits TWA1 and Muskelin. Cells expressing GPS-ZMYND19 were used to allow purification of populations of cells in which TWA1 and Muskelin had been successfully ablated by FACS. See also . (E-F) AAMP is more abundant in cells lacking CTLH subunits. The scatterplot in (E) represents the mean fold change of each protein quantified in both TWA1 KO and Muskelin KO cells, with proteins showing a >1.2-fold increase in abundance in both conditions highlighted in red; the performance of AAMP compared to the known substrate HMGCS1 is depicted in (F) . Exogenous expression of ZMYND19 precludes assessment of the true magnitude of the stabilization of the endogenous ZMYND19 protein in this experiment.
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    Image Search Results


    (A) Schematic representation of the stability profiling experiment, in which the Ultimate ORFeome GPS expression library was used to identify proteins exhibiting increased stability in MAEA KO and TWA1 KO cells. (B-C) Identification of AAMP, AEN and NATD1 as CTLH substrates. Screen profiles are depicted in (B) , while individual validation experiments by flow cytometry in the presence and absence of Torin-1 (dotted lines) are shown in (C) . See also . (D) Schematic representation of the proteomic experiment, in which TMT mass spectrometry was used to identify proteins more abundant in cells lacking the CTLH subunits TWA1 and Muskelin. Cells expressing GPS-ZMYND19 were used to allow purification of populations of cells in which TWA1 and Muskelin had been successfully ablated by FACS. See also . (E-F) AAMP is more abundant in cells lacking CTLH subunits. The scatterplot in (E) represents the mean fold change of each protein quantified in both TWA1 KO and Muskelin KO cells, with proteins showing a >1.2-fold increase in abundance in both conditions highlighted in red; the performance of AAMP compared to the known substrate HMGCS1 is depicted in (F) . Exogenous expression of ZMYND19 precludes assessment of the true magnitude of the stabilization of the endogenous ZMYND19 protein in this experiment.

    Journal: bioRxiv

    Article Title: Proteome-wide C-degron activity profiling connects conditional regulation of the CTLH E3 ligase complex to ribosome biogenesis

    doi: 10.64898/2026.01.14.698769

    Figure Lengend Snippet: (A) Schematic representation of the stability profiling experiment, in which the Ultimate ORFeome GPS expression library was used to identify proteins exhibiting increased stability in MAEA KO and TWA1 KO cells. (B-C) Identification of AAMP, AEN and NATD1 as CTLH substrates. Screen profiles are depicted in (B) , while individual validation experiments by flow cytometry in the presence and absence of Torin-1 (dotted lines) are shown in (C) . See also . (D) Schematic representation of the proteomic experiment, in which TMT mass spectrometry was used to identify proteins more abundant in cells lacking the CTLH subunits TWA1 and Muskelin. Cells expressing GPS-ZMYND19 were used to allow purification of populations of cells in which TWA1 and Muskelin had been successfully ablated by FACS. See also . (E-F) AAMP is more abundant in cells lacking CTLH subunits. The scatterplot in (E) represents the mean fold change of each protein quantified in both TWA1 KO and Muskelin KO cells, with proteins showing a >1.2-fold increase in abundance in both conditions highlighted in red; the performance of AAMP compared to the known substrate HMGCS1 is depicted in (F) . Exogenous expression of ZMYND19 precludes assessment of the true magnitude of the stabilization of the endogenous ZMYND19 protein in this experiment.

    Article Snippet: Primary antibodies used were: rabbit α-MAEA (Proteintech, #28363-1-AP), rabbit α-TWA1 (Novus Biologicals, #NBP1-32596), mouse α-Muskelin (Santa Cruz, #sc-398956), mouse α-RanBP9 (Santa Cruz, #sc-271727), rabbit α-RanBP10 (Proteintech, #21107-1-AP), mouse α-ARMC8 (Santa Cruz, #sc-365307), rabbit α-WDR26 (Bethyl, #A302-244A), rabbit α-YPEL5 (Proteintech, #11730-1-AP), rabbit α-AAMP (Abcam, #EPR12369), rabbit α-ISG20L2 (Proteintech, #24639-1-AP), rabbit α-HMGCS1 (Proteintech, #17643-1-AP), mouse α-UBE2H (Santa Cruz, #sc-100620), rabbit α-uL16/RPL10 (Proteintech, #17013-1-AP), rabbit α-uL14/RPL23 (Abcam, #ab264369), mouse α-eS6/RPS6 (Cell Signaling Technology, #2317), mouse α-β-actin (Merck, #A2228), mouse α-vinculin (Merck, #V9131), rabbit α-HA-tag (Cell Signaling Technology, #C29F4), mouse α-FLAG (Merck #F1804), rabbit α-GFP (Abcam, #ab290), mouse α-GFP (Roche, #11814460001) and rabbit α-Phospho-p70 S6 Kinase (Thr389) (Cell Signaling Technology, #9205).

    Techniques: Expressing, Biomarker Discovery, Flow Cytometry, Mass Spectrometry, Purification

    RanBPM and TWA1 are essential for complex stability. Whole cell extracts prepared from control shRNA and RanBPM shRNA HEK293 cells ( a ), or from control (labelled as C), TWA1, RMND5A, MAEA, ARMC8 and muskelin HEK293 CRISPR knockout cells ( b – f ) were analyzed by Western blot with antibodies to CTLH complex members, as indicated. Vinculin was used as a loading control. Quantifications are shown below each blot and protein levels are shown relative to control cells set to 1 and normalized to Vinculin levels. Data represent averages from three separate experiments, with error bars indicating SD. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

    Journal: Scientific Reports

    Article Title: The mammalian CTLH complex is an E3 ubiquitin ligase that targets its subunit muskelin for degradation

    doi: 10.1038/s41598-019-46279-5

    Figure Lengend Snippet: RanBPM and TWA1 are essential for complex stability. Whole cell extracts prepared from control shRNA and RanBPM shRNA HEK293 cells ( a ), or from control (labelled as C), TWA1, RMND5A, MAEA, ARMC8 and muskelin HEK293 CRISPR knockout cells ( b – f ) were analyzed by Western blot with antibodies to CTLH complex members, as indicated. Vinculin was used as a loading control. Quantifications are shown below each blot and protein levels are shown relative to control cells set to 1 and normalized to Vinculin levels. Data represent averages from three separate experiments, with error bars indicating SD. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

    Article Snippet: Gels were transferred to polyvinylidene fluoride membranes, blocked in 5% milk and hybridized with the following antibodies: ARMC8 (E-1, sc-365307; Santa Cruz Biotechnology, Santa Cruz, CA, USA); FLAG (M2, F1804, Sigma-Aldrich, St. Louis, MO, USA); HA (HA-7, H3663 Sigma-Aldrich); MAEA (AF7288, R&D Systems, Minneapolis, MN, USA); Muskelin (C-12, sc-398956, Santa Cruz Biotechnology); RanBPM (5M, 71-001, Bioacademia, Japan); RMND5A (NBP1-92337, Novus Biologicals, Littleton, CO, USA); TWA1 (NBP1-32596, Novus Biologicals); Vinculin (E1E9V, Cell Signaling Technology, Danvers, MA, USA); WDR26 (ab85962, Abcam, Cambridge, UK); β-actin (A5441, Sigma-Aldrich) and His (MAB050, R&D Systems).

    Techniques: Control, shRNA, CRISPR, Knock-Out, Western Blot