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ranbp9 rabbit pab  (Novus Biologicals)


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    Structured Review

    Novus Biologicals ranbp9 rabbit pab
    Fig. 3. WDR26 mutants affect formation of supramolecular WDR26-CTLH E3 assembly. (A) Cartoon of the wildtype supramolecular CTLH E3 assembly and the potential CTLH (sub-) complexes (I, II, and III) caused by WDR26 SKDEAS-associated mutations. Group I: variants maintaining formation of the supramolecular CTLH E3 assembly; group II: variants disrupting CTLH E3 supramolecular assembly but retaining interactions with <t>RANBP9;</t> and group III: variants abolishing both the higher order CTLH E3 assembly and interactions with RANBP9. HA-tagged WDR26 subunits are indicated. (B) Cell lysates of K562 parental, WDR26- and MKLN1-deficient double knockout K562 cells (WDR26/; MKLN1/), and WDR26/; MKLN1/ cells with stably reintroduced HA-tagged WDR26 were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Fractions with supramolecular assemblies > 670 kDa are indicated with a red box, and smaller subcomplexes with a blue box. (C, D) Cell lysates of K562 WDR26/; MKLN1/ stably reintroduced HA-tagged WDR26 variants from different individuals (Ind#) were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Supramolecular assemblies and subcomplexes are boxed in red and blue, respectively. Immunoblot data of individual WDR26 variant are grouped into LisH-CTLH-CRA mutants (C) and WDR26 b-propeller mutants (D). Uncropped blots are provided in Figs S1–S3.
    Ranbp9 Rabbit Pab, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ranbp9 rabbit pab/product/Novus Biologicals
    Average 94 stars, based on 1 article reviews
    ranbp9 rabbit pab - by Bioz Stars, 2026-03
    94/100 stars

    Images

    1) Product Images from "Skraban-Deardorff intellectual disability syndrome-associated mutations in WDR26 impair CTLH E3 complex assembly."

    Article Title: Skraban-Deardorff intellectual disability syndrome-associated mutations in WDR26 impair CTLH E3 complex assembly.

    Journal: FEBS letters

    doi: 10.1002/1873-3468.14866

    Fig. 3. WDR26 mutants affect formation of supramolecular WDR26-CTLH E3 assembly. (A) Cartoon of the wildtype supramolecular CTLH E3 assembly and the potential CTLH (sub-) complexes (I, II, and III) caused by WDR26 SKDEAS-associated mutations. Group I: variants maintaining formation of the supramolecular CTLH E3 assembly; group II: variants disrupting CTLH E3 supramolecular assembly but retaining interactions with RANBP9; and group III: variants abolishing both the higher order CTLH E3 assembly and interactions with RANBP9. HA-tagged WDR26 subunits are indicated. (B) Cell lysates of K562 parental, WDR26- and MKLN1-deficient double knockout K562 cells (WDR26/; MKLN1/), and WDR26/; MKLN1/ cells with stably reintroduced HA-tagged WDR26 were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Fractions with supramolecular assemblies > 670 kDa are indicated with a red box, and smaller subcomplexes with a blue box. (C, D) Cell lysates of K562 WDR26/; MKLN1/ stably reintroduced HA-tagged WDR26 variants from different individuals (Ind#) were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Supramolecular assemblies and subcomplexes are boxed in red and blue, respectively. Immunoblot data of individual WDR26 variant are grouped into LisH-CTLH-CRA mutants (C) and WDR26 b-propeller mutants (D). Uncropped blots are provided in Figs S1–S3.
    Figure Legend Snippet: Fig. 3. WDR26 mutants affect formation of supramolecular WDR26-CTLH E3 assembly. (A) Cartoon of the wildtype supramolecular CTLH E3 assembly and the potential CTLH (sub-) complexes (I, II, and III) caused by WDR26 SKDEAS-associated mutations. Group I: variants maintaining formation of the supramolecular CTLH E3 assembly; group II: variants disrupting CTLH E3 supramolecular assembly but retaining interactions with RANBP9; and group III: variants abolishing both the higher order CTLH E3 assembly and interactions with RANBP9. HA-tagged WDR26 subunits are indicated. (B) Cell lysates of K562 parental, WDR26- and MKLN1-deficient double knockout K562 cells (WDR26/; MKLN1/), and WDR26/; MKLN1/ cells with stably reintroduced HA-tagged WDR26 were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Fractions with supramolecular assemblies > 670 kDa are indicated with a red box, and smaller subcomplexes with a blue box. (C, D) Cell lysates of K562 WDR26/; MKLN1/ stably reintroduced HA-tagged WDR26 variants from different individuals (Ind#) were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Supramolecular assemblies and subcomplexes are boxed in red and blue, respectively. Immunoblot data of individual WDR26 variant are grouped into LisH-CTLH-CRA mutants (C) and WDR26 b-propeller mutants (D). Uncropped blots are provided in Figs S1–S3.

    Techniques Used: Double Knockout, Stable Transfection, Western Blot, Variant Assay



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    ranbp9 rabbit pab  (Novus Biologicals)
    94
    Novus Biologicals ranbp9 rabbit pab
    Fig. 3. WDR26 mutants affect formation of supramolecular WDR26-CTLH E3 assembly. (A) Cartoon of the wildtype supramolecular CTLH E3 assembly and the potential CTLH (sub-) complexes (I, II, and III) caused by WDR26 SKDEAS-associated mutations. Group I: variants maintaining formation of the supramolecular CTLH E3 assembly; group II: variants disrupting CTLH E3 supramolecular assembly but retaining interactions with <t>RANBP9;</t> and group III: variants abolishing both the higher order CTLH E3 assembly and interactions with RANBP9. HA-tagged WDR26 subunits are indicated. (B) Cell lysates of K562 parental, WDR26- and MKLN1-deficient double knockout K562 cells (WDR26/; MKLN1/), and WDR26/; MKLN1/ cells with stably reintroduced HA-tagged WDR26 were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Fractions with supramolecular assemblies > 670 kDa are indicated with a red box, and smaller subcomplexes with a blue box. (C, D) Cell lysates of K562 WDR26/; MKLN1/ stably reintroduced HA-tagged WDR26 variants from different individuals (Ind#) were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Supramolecular assemblies and subcomplexes are boxed in red and blue, respectively. Immunoblot data of individual WDR26 variant are grouped into LisH-CTLH-CRA mutants (C) and WDR26 b-propeller mutants (D). Uncropped blots are provided in Figs S1–S3.
    Ranbp9 Rabbit Pab, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ranbp9 rabbit pab/product/Novus Biologicals
    Average 94 stars, based on 1 article reviews
    ranbp9 rabbit pab - by Bioz Stars, 2026-03
    94/100 stars
    		  Buy from Supplier

    Image Search Results


    Fig. 3. WDR26 mutants affect formation of supramolecular WDR26-CTLH E3 assembly. (A) Cartoon of the wildtype supramolecular CTLH E3 assembly and the potential CTLH (sub-) complexes (I, II, and III) caused by WDR26 SKDEAS-associated mutations. Group I: variants maintaining formation of the supramolecular CTLH E3 assembly; group II: variants disrupting CTLH E3 supramolecular assembly but retaining interactions with RANBP9; and group III: variants abolishing both the higher order CTLH E3 assembly and interactions with RANBP9. HA-tagged WDR26 subunits are indicated. (B) Cell lysates of K562 parental, WDR26- and MKLN1-deficient double knockout K562 cells (WDR26/; MKLN1/), and WDR26/; MKLN1/ cells with stably reintroduced HA-tagged WDR26 were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Fractions with supramolecular assemblies > 670 kDa are indicated with a red box, and smaller subcomplexes with a blue box. (C, D) Cell lysates of K562 WDR26/; MKLN1/ stably reintroduced HA-tagged WDR26 variants from different individuals (Ind#) were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Supramolecular assemblies and subcomplexes are boxed in red and blue, respectively. Immunoblot data of individual WDR26 variant are grouped into LisH-CTLH-CRA mutants (C) and WDR26 b-propeller mutants (D). Uncropped blots are provided in Figs S1–S3.

    Journal: FEBS letters

    Article Title: Skraban-Deardorff intellectual disability syndrome-associated mutations in WDR26 impair CTLH E3 complex assembly.

    doi: 10.1002/1873-3468.14866

    Figure Lengend Snippet: Fig. 3. WDR26 mutants affect formation of supramolecular WDR26-CTLH E3 assembly. (A) Cartoon of the wildtype supramolecular CTLH E3 assembly and the potential CTLH (sub-) complexes (I, II, and III) caused by WDR26 SKDEAS-associated mutations. Group I: variants maintaining formation of the supramolecular CTLH E3 assembly; group II: variants disrupting CTLH E3 supramolecular assembly but retaining interactions with RANBP9; and group III: variants abolishing both the higher order CTLH E3 assembly and interactions with RANBP9. HA-tagged WDR26 subunits are indicated. (B) Cell lysates of K562 parental, WDR26- and MKLN1-deficient double knockout K562 cells (WDR26/; MKLN1/), and WDR26/; MKLN1/ cells with stably reintroduced HA-tagged WDR26 were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Fractions with supramolecular assemblies > 670 kDa are indicated with a red box, and smaller subcomplexes with a blue box. (C, D) Cell lysates of K562 WDR26/; MKLN1/ stably reintroduced HA-tagged WDR26 variants from different individuals (Ind#) were fractionated on a continuous 5–40% sucrose gradient, and fractions analyzed by immunoblotting. Supramolecular assemblies and subcomplexes are boxed in red and blue, respectively. Immunoblot data of individual WDR26 variant are grouped into LisH-CTLH-CRA mutants (C) and WDR26 b-propeller mutants (D). Uncropped blots are provided in Figs S1–S3.

    Article Snippet: Membranes were incubated over night at 4 °C with the primary antibodies: HA (C29F4) Rabbit mAb (CST, Danvers, MA, USA; 3724S, RRID: AB_1549585, lot 10 + 11, 1 : 2000), RANBP9 Rabbit pAB (Novus Biologicals, Centannial, CO, USA; PAB16671, RRID: AB_10677213, lot 3, 1 : 1000), MAEA Sheep pAb (R&D Systems, Minneapolis, MN, USA; AF7288, RRID: AB_10971438, CGG10119091, 1 : 1000), YPEL5 pAb (Thermo Fisher Scientific; PA5-26957, RRID: AB_2544457, lot VH3047907, 1 : 1000 in 5% BSA, TBS-T), ACTIN (CST; 4967L, RRID: AB_330288, lot 3, 1 : 1000) or DYKDDDDK Tag (D6W5B) Rabbit mAb (CST; 14793S, RRID: AB_2572291, lot 4, 1 : 1000).

    Techniques: Double Knockout, Stable Transfection, Western Blot, Variant Assay