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anti p53  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology anti p53
Figure 2. Analysis of UNC45A p.Leu237Pro variant expression, stability, and in silico prediction of structural changes. (A) Immunoblot analysis of endogenous UNC45A and NMIIA in fibroblasts originating from skin biopsies of P2.1, a healthy heterozygous family member, and a nonrelated individual (Ctr). β-Actin served as a loading control. (B) Parental U2OS, UNC45A-KO, and stably complemented UNC45A wild-type and mutant cells were analyzed for endogenous and ectopic UNC45A expression by immunoblotting. The protein levels of selected myosins were tested using NMIIA- and MYO5B-specific antibodies, and β-actin was used to control the loading. (C) U2OS UNC45A-KO cells were transiently transfected with HA-tagged UNC45A wild-type and mutant constructs and treated with 100 μg/mL cycloheximide (CHX) for the indicated times. UNC45A levels were analyzed using HA-specific antibody with <t>p53</t> levels as a control for CHX treatment and β-actin as a protein loading control. (D) Ribbon representation of the human UNC45A protein structure predicted by AlphaFold (accession code: AF-Q9H3U1-F1; upper panel). Vibrational entropy changes (ΔΔSVib) between wild-type and mutant are indicated in red and represent a gain in structural flexibility. Differences
Anti P53, supplied by Santa Cruz Biotechnology, 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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Figure 2. Analysis of UNC45A p.Leu237Pro variant expression, stability, and in silico prediction of structural changes. (A) Immunoblot analysis of endogenous UNC45A and NMIIA in fibroblasts originating from skin biopsies of P2.1, a healthy heterozygous family member, and a nonrelated individual (Ctr). β-Actin served as a loading control. (B) Parental U2OS, UNC45A-KO, and stably complemented UNC45A wild-type and mutant cells were analyzed for endogenous and ectopic UNC45A expression by immunoblotting. The protein levels of selected myosins were tested using NMIIA- and MYO5B-specific antibodies, and β-actin was used to control the loading. (C) U2OS UNC45A-KO cells were transiently transfected with HA-tagged UNC45A wild-type and mutant constructs and treated with 100 μg/mL cycloheximide (CHX) for the indicated times. UNC45A levels were analyzed using HA-specific antibody with p53 levels as a control for CHX treatment and β-actin as a protein loading control. (D) Ribbon representation of the human UNC45A protein structure predicted by AlphaFold (accession code: AF-Q9H3U1-F1; upper panel). Vibrational entropy changes (ΔΔSVib) between wild-type and mutant are indicated in red and represent a gain in structural flexibility. Differences

Journal: JCI insight

Article Title: Altered chaperone-nonmuscle myosin II interactions drive pathogenicity of the UNC45A c.710T>C variant in osteo-oto-hepato-enteric syndrome.

doi: 10.1172/jci.insight.185508

Figure Lengend Snippet: Figure 2. Analysis of UNC45A p.Leu237Pro variant expression, stability, and in silico prediction of structural changes. (A) Immunoblot analysis of endogenous UNC45A and NMIIA in fibroblasts originating from skin biopsies of P2.1, a healthy heterozygous family member, and a nonrelated individual (Ctr). β-Actin served as a loading control. (B) Parental U2OS, UNC45A-KO, and stably complemented UNC45A wild-type and mutant cells were analyzed for endogenous and ectopic UNC45A expression by immunoblotting. The protein levels of selected myosins were tested using NMIIA- and MYO5B-specific antibodies, and β-actin was used to control the loading. (C) U2OS UNC45A-KO cells were transiently transfected with HA-tagged UNC45A wild-type and mutant constructs and treated with 100 μg/mL cycloheximide (CHX) for the indicated times. UNC45A levels were analyzed using HA-specific antibody with p53 levels as a control for CHX treatment and β-actin as a protein loading control. (D) Ribbon representation of the human UNC45A protein structure predicted by AlphaFold (accession code: AF-Q9H3U1-F1; upper panel). Vibrational entropy changes (ΔΔSVib) between wild-type and mutant are indicated in red and represent a gain in structural flexibility. Differences

Article Snippet: The following primary antibodies were used for immunoblotting: anti-UNC45A (ENZO, ADI-SRA-1800-F; and Invitrogen, PA5-58703, both in a dilution of 1:1,000), 6x-Histag monoclonal antibody (Invitrogen, MA1-21315, diluted 1:1,000), anti-HA (BioLegend, 101501, diluted 1:1,000), anti-p53 (Santa Cruz Biotechnology, sc-126, diluted 1:1,000), anti-MYO5B (Novus Biologicals, Bio-Techne; NBP1-87746, diluted 1:500), and anti–β-actin (Cell Signaling Technology, 3700S, diluted 1:1,000).

Techniques: Variant Assay, Expressing, In Silico, Western Blot, Control, Stable Transfection, Mutagenesis, Transfection, Construct