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human hsp90ab1 antibody  (Boster Bio)


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    Boster Bio human hsp90ab1 antibody
    Fig. 2 The differential abundance of <t>HSP90AB1,</t> HSPD1 and HSPA13 in villi tissues was verified by Western blot. A The representative of Western blot analysis to verify selected differentially expressed proteins HSP90AB1, HSPD1 and HSPA13 in the villi tissue of embryo from EMA (n = 6) and control(n = 6). B The scatter plot of HSP90AB1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). C The scatter plot of HSPD1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). D The scatter plot of HSPA13 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01)
    Human Hsp90ab1 Antibody, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 2 article reviews
    human hsp90ab1 antibody - by Bioz Stars, 2026-02
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    1) Product Images from "PRM-based quantitative proteomics analysis of altered HSP abundance in villi and decidua of patients with early missed abortion."

    Article Title: PRM-based quantitative proteomics analysis of altered HSP abundance in villi and decidua of patients with early missed abortion.

    Journal: Proteome science

    doi: 10.1186/s12953-023-00213-w

    Fig. 2 The differential abundance of HSP90AB1, HSPD1 and HSPA13 in villi tissues was verified by Western blot. A The representative of Western blot analysis to verify selected differentially expressed proteins HSP90AB1, HSPD1 and HSPA13 in the villi tissue of embryo from EMA (n = 6) and control(n = 6). B The scatter plot of HSP90AB1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). C The scatter plot of HSPD1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). D The scatter plot of HSPA13 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01)
    Figure Legend Snippet: Fig. 2 The differential abundance of HSP90AB1, HSPD1 and HSPA13 in villi tissues was verified by Western blot. A The representative of Western blot analysis to verify selected differentially expressed proteins HSP90AB1, HSPD1 and HSPA13 in the villi tissue of embryo from EMA (n = 6) and control(n = 6). B The scatter plot of HSP90AB1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). C The scatter plot of HSPD1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). D The scatter plot of HSPA13 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01)

    Techniques Used: Western Blot, Control

    Fig. 3 A, B, C Immunohistochemical staining for HSP90AB1, HSPD1, and HSPA13 observed in the cytoplasm of syncytiotrophoblast and cytotrophoblast cells (× 200, × 400). Villus from 22 patients with EMA showed lower; D-F Quantitative scoring results of IHC analyses w shown as box plots
    Figure Legend Snippet: Fig. 3 A, B, C Immunohistochemical staining for HSP90AB1, HSPD1, and HSPA13 observed in the cytoplasm of syncytiotrophoblast and cytotrophoblast cells (× 200, × 400). Villus from 22 patients with EMA showed lower; D-F Quantitative scoring results of IHC analyses w shown as box plots

    Techniques Used: Immunohistochemical staining, Staining



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    Fig. 2 The differential abundance of <t>HSP90AB1,</t> HSPD1 and HSPA13 in villi tissues was verified by Western blot. A The representative of Western blot analysis to verify selected differentially expressed proteins HSP90AB1, HSPD1 and HSPA13 in the villi tissue of embryo from EMA (n = 6) and control(n = 6). B The scatter plot of HSP90AB1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). C The scatter plot of HSPD1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). D The scatter plot of HSPA13 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01)
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    Kdm3a interacts with Hsp90 and other cellular chaperones in vitro and in vivo. (A) Positive clones identified from a large two-hybrid screen using Hsp90 as baits were purified, retransformed into yeast, and mated to reassess interactions. The catalytic domain of Kdm3a can rescue amino acid deficiency of the parental yeast strain only when Hsp90ab1 is the bait. Diagram illustrates JmjC region contained in two-hybrid and GST constructs. (B) Bacterially expressed C-terminal end of Kdm3a-GST: GST-JmjC (aa 1136–1323), GST-ΔJmjC (aa 1283–1323), and GST vectors were incubated with HeLa cell extracts. Proteins bound to glutathione beads were resolved and blotted with the indicated antibodies to determine interactions of GST constructs with Hsp90. (C) TrueBlue stain of whole adult testis extracts immunopurified with Kdm3a or an irrelevant antibody used as control (Ir Ab). The gel section indicated was cut for mass spectrometry (MS). (D) Table shows the number of unique peptides identified with >99% confidence for three independent immunopurifications resolved as shown in (C) for each genotype. Only proteins shared by the six runs and not found in control samples are included. (E) An antibody directed to the N-terminal end of Kdm3a pulls down endogenous Hsp90 from testis. Note that the in-frame deletion Kdm3a protein encoded by the floxed Kdm3a allele still binds Hsp90aa1 and Hsp90ab1 strongly. (F) Total extracts from adult testis immunoblotted with Kdm3a show absence of full-length (FL) and low levels of truncated (ΔJC) Kdm3a protein in Kdm3a ΔJC/ΔJC animals. Kdm3a-FL (red arrow) in wild-type (WT) and heterozygous (Het) but not control pool is indicated. 1–3 identify an animal for each genotype.

    Journal: Molecular Biology of the Cell

    Article Title: Kdm3a lysine demethylase is an Hsp90 client required for cytoskeletal rearrangements during spermatogenesis

    doi: 10.1091/mbc.E13-08-0471

    Figure Lengend Snippet: Kdm3a interacts with Hsp90 and other cellular chaperones in vitro and in vivo. (A) Positive clones identified from a large two-hybrid screen using Hsp90 as baits were purified, retransformed into yeast, and mated to reassess interactions. The catalytic domain of Kdm3a can rescue amino acid deficiency of the parental yeast strain only when Hsp90ab1 is the bait. Diagram illustrates JmjC region contained in two-hybrid and GST constructs. (B) Bacterially expressed C-terminal end of Kdm3a-GST: GST-JmjC (aa 1136–1323), GST-ΔJmjC (aa 1283–1323), and GST vectors were incubated with HeLa cell extracts. Proteins bound to glutathione beads were resolved and blotted with the indicated antibodies to determine interactions of GST constructs with Hsp90. (C) TrueBlue stain of whole adult testis extracts immunopurified with Kdm3a or an irrelevant antibody used as control (Ir Ab). The gel section indicated was cut for mass spectrometry (MS). (D) Table shows the number of unique peptides identified with >99% confidence for three independent immunopurifications resolved as shown in (C) for each genotype. Only proteins shared by the six runs and not found in control samples are included. (E) An antibody directed to the N-terminal end of Kdm3a pulls down endogenous Hsp90 from testis. Note that the in-frame deletion Kdm3a protein encoded by the floxed Kdm3a allele still binds Hsp90aa1 and Hsp90ab1 strongly. (F) Total extracts from adult testis immunoblotted with Kdm3a show absence of full-length (FL) and low levels of truncated (ΔJC) Kdm3a protein in Kdm3a ΔJC/ΔJC animals. Kdm3a-FL (red arrow) in wild-type (WT) and heterozygous (Het) but not control pool is indicated. 1–3 identify an animal for each genotype.

    Article Snippet: The antibodies used along this study are to KDM3A (12835; Proteintech; and NB100-77282; Novus Biologicals, Littleton, CO); KDM3B (IHC 00189; Bethyl Laboratories, Montgomery, TX); Cct4 (ARP34271; Aviva); anti–mono- and dimethylated lysines (ab23366 and ab76118; Abcam, Cambridge, MA); anti-GFP (sc-8334), monoclonal to GAPDH (5019A-2; Imgenex, San Diego, CA), β-gal (A-11132; Molecular Probes), GST (C83271; LSBio); HP1a (clone 15.1952; Upstate); γ-tubulin (GTU-88; Sigma-Aldrich, St. Louis, MO), β-actin (ab8229; Abcam), Hsp90ab1 (MAB32861; R&D Systems), Hsp90aa1 (10713715; Pierce, Rockford, IL), Actbl2 (ab134977; Abcam).

    Techniques: In Vitro, In Vivo, Clone Assay, Two Hybrid Screening, Purification, Construct, Incubation, Staining, Control, Mass Spectrometry

    Fig. 2 The differential abundance of HSP90AB1, HSPD1 and HSPA13 in villi tissues was verified by Western blot. A The representative of Western blot analysis to verify selected differentially expressed proteins HSP90AB1, HSPD1 and HSPA13 in the villi tissue of embryo from EMA (n = 6) and control(n = 6). B The scatter plot of HSP90AB1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). C The scatter plot of HSPD1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). D The scatter plot of HSPA13 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01)

    Journal: Proteome science

    Article Title: PRM-based quantitative proteomics analysis of altered HSP abundance in villi and decidua of patients with early missed abortion.

    doi: 10.1186/s12953-023-00213-w

    Figure Lengend Snippet: Fig. 2 The differential abundance of HSP90AB1, HSPD1 and HSPA13 in villi tissues was verified by Western blot. A The representative of Western blot analysis to verify selected differentially expressed proteins HSP90AB1, HSPD1 and HSPA13 in the villi tissue of embryo from EMA (n = 6) and control(n = 6). B The scatter plot of HSP90AB1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). C The scatter plot of HSPD1 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01). D The scatter plot of HSPA13 abundance in the villi tissue of embryo from EMA (n = 22) vs control (n = 22) (P < 0.01)

    Article Snippet: Human HSP90AB1 antibody (Boster, Wuhan, China, no. BM4191, 1:2000 dilution), human HSPD1 antibody (Boster, Wuhan, China, no. M01280-3, 1:2000 dilution) and human HSPA13 antibody (Proteintech, Wuhan, China, no. 12667–2-AP, 1:2000 dilution) were used as the primary antibodies for Western blot analysis.

    Techniques: Western Blot, Control

    Fig. 3 A, B, C Immunohistochemical staining for HSP90AB1, HSPD1, and HSPA13 observed in the cytoplasm of syncytiotrophoblast and cytotrophoblast cells (× 200, × 400). Villus from 22 patients with EMA showed lower; D-F Quantitative scoring results of IHC analyses w shown as box plots

    Journal: Proteome science

    Article Title: PRM-based quantitative proteomics analysis of altered HSP abundance in villi and decidua of patients with early missed abortion.

    doi: 10.1186/s12953-023-00213-w

    Figure Lengend Snippet: Fig. 3 A, B, C Immunohistochemical staining for HSP90AB1, HSPD1, and HSPA13 observed in the cytoplasm of syncytiotrophoblast and cytotrophoblast cells (× 200, × 400). Villus from 22 patients with EMA showed lower; D-F Quantitative scoring results of IHC analyses w shown as box plots

    Article Snippet: Human HSP90AB1 antibody (Boster, Wuhan, China, no. BM4191, 1:2000 dilution), human HSPD1 antibody (Boster, Wuhan, China, no. M01280-3, 1:2000 dilution) and human HSPA13 antibody (Proteintech, Wuhan, China, no. 12667–2-AP, 1:2000 dilution) were used as the primary antibodies for Western blot analysis.

    Techniques: Immunohistochemical staining, Staining