rabbit anti his6 (Bethyl)
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Bethyl
rabbit anti his6
Rabbit Anti His6, supplied by Bethyl, used in various techniques. Bioz Stars score: 93/100, based on 117 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+6+his/6-His+Tag+Antibody/pmc12905349-19-0-3
Average 93 stars, based on 117 article reviews
Rabbit Anti His6, supplied by Bethyl, used in various techniques. Bioz Stars score: 93/100, based on 117 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+6+his/6-His+Tag+Antibody/pmc12905349-19-0-3
Average 93 stars, based on 117 article reviews
rabbit anti his6 - by Bioz Stars,
2026-10
93/100 stars
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Binding Assay:Article Title: Structure and Functional Binding Epitope of V-domain Ig Suppressor of T Cell Activation. Article Snippet: For VSTB pre-complexed experiments, 1 mM of VISTAwas incubatedwith 1 nM– 5000 nMof VSTB in individual eppendorf tubes overnight and then added to VSIG3-coated ELISA plates. .. Binding of VISTA was detected indirectly by first adding 1:750 Article Title: Structure and Functional Binding Epitope of V-domain Ig Suppressor of T-cell Activation (VISTA) Article Snippet: For VSTB pre-complexed experiments, 1 μM of VISTA was incubated with 1 nM – 5000 nM of VSTB in individual eppendorf tubes overnight and then added to VSIG3-coated ELISA plates. .. Binding of VISTA was detected indirectly by first adding 1:750 Sequencing:Article Title: Identification of trypsin-degrading commensals in the large intestine Article Snippet: In some earlier experiments, SDS–PAGE and PVDF membrane (0.2 μm Transfer Membranes Immobilon-P SQ , Merck Millipore) transfer were performed according to the manufacturer’s (XV Pantera System (DRC)) instructions. iBind Western Systems (Thermo Fisher Scientific) were used for staining throughout the study. .. The antibodies used in this study are as follows: rabbit anti-mouse PRSS2 (Cosmo Bio, CPA, Japan, custom-made), rabbit anti-mouse HSP90 antibody (4877, C45G5, Cell Signaling Technology), rabbit anti-human PRSS2 (LS-B15726, LSBio), rabbit anti-human PRSS1 (LS-331381, LSBio), rabbit anti-mouse TMPRSS2 (LS-C373022, LSBio, raised against a sequence at the protease domain), Article Title: Identification of trypsin-degrading commensals in the large intestine. Article Snippet: In some earlier experiments, SDS–PAGE and PVDF membrane (0.2 μm Transfer Membranes Immobilon-PSQ, Merck Millipore) transfer were performed according to the manufacturer’s (XV Pantera System (DRC)) instructions. iBind Western Systems (Thermo Fisher Scientific) were used for staining throughout the study. .. The antibodies used in this study are as follows: rabbit anti-mouse PRSS2 (Cosmo Bio, CPA, Japan, custom-made), rabbit anti-mouse HSP90 antibody (4877, C45G5, Cell Signaling Technology), rabbit anti-human PRSS2 (LS-B15726, LSBio), rabbit anti-human PRSS1 (LS-331381, LSBio), rabbit anti-mouse TMPRSS2 (LS-C373022, LSBio, raised against a sequence at the protease domain), Recombinant:Article Title: Identification of trypsin-degrading commensals in the large intestine Article Snippet: In some earlier experiments, SDS–PAGE and PVDF membrane (0.2 μm Transfer Membranes Immobilon-P SQ , Merck Millipore) transfer were performed according to the manufacturer’s (XV Pantera System (DRC)) instructions. iBind Western Systems (Thermo Fisher Scientific) were used for staining throughout the study. .. The antibodies used in this study are as follows: rabbit anti-mouse PRSS2 (Cosmo Bio, CPA, Japan, custom-made), rabbit anti-mouse HSP90 antibody (4877, C45G5, Cell Signaling Technology), rabbit anti-human PRSS2 (LS-B15726, LSBio), rabbit anti-human PRSS1 (LS-331381, LSBio), rabbit anti-mouse TMPRSS2 (LS-C373022, LSBio, raised against a sequence at the protease domain), Article Title: Identification of trypsin-degrading commensals in the large intestine. Article Snippet: In some earlier experiments, SDS–PAGE and PVDF membrane (0.2 μm Transfer Membranes Immobilon-PSQ, Merck Millipore) transfer were performed according to the manufacturer’s (XV Pantera System (DRC)) instructions. iBind Western Systems (Thermo Fisher Scientific) were used for staining throughout the study. .. The antibodies used in this study are as follows: rabbit anti-mouse PRSS2 (Cosmo Bio, CPA, Japan, custom-made), rabbit anti-mouse HSP90 antibody (4877, C45G5, Cell Signaling Technology), rabbit anti-human PRSS2 (LS-B15726, LSBio), rabbit anti-human PRSS1 (LS-331381, LSBio), rabbit anti-mouse TMPRSS2 (LS-C373022, LSBio, raised against a sequence at the protease domain), |
![Hypoxia induces the site-specific crotonylation of heat shock protein 90 alpha family class B member 1 <t>(HSP90AB1)</t> at lysine 265 (K265) to regulate redox homeostasis in OSCC. (A) Volcano plot of crotonylation sites in CAL27 cells after 24 h of hypoxia versus normoxia. Sites are colored red for fold changes >1.5 and P < 0.05 and blue for fold changes <−1.5 and P < 0.05. (B and C) Subcellular localization analysis of (B) up-regulated and (C) down-regulated crotonylated proteins. (D) Immunoprecipitation (IP) of endogenous HSP90AB1 in CAL27/HSC3 cells under normoxia/hypoxia (24 h) and probing with a pan-Kcr antibody (IgG, immunoglobulin G; WCL, whole-cell lysate). (E) IP of Flag-HSP90AB1 in HEK293T cells under normoxia and hypoxia probed with a pan-Kcr antibody. (F) Crotonylation levels of Flag-HSP90AB1 in HEK293T cells treated with sodium crotonate (0 to 10 mM) under normoxia (24 h). (G) Domain structure of HSP90AB1 (NTD, N-terminal domain; MD, middle domain; CD, charged domain; CTD, C-terminal domain) and K265 mutation schematic (K, lysine; R, arginine; Q, glutamine). (H and I) IP of Flag-HSP90AB1 in HEK293T cells reconstituted with HSP90AB1 variants (wild type [WT], K265R, and K265Q) under normoxia/hypoxia (24 h) and probed with (H) pan-Kcr and (I) site-specific <t>K265cr</t> antibodies. (J) Representative confocal images of DCFH-DA staining in HSP90AB1-knockdown CAL27/HSC3 cells reconstituted with HSP90AB1 variants under normoxia/hypoxia (24 h) (200×, scale bars, 100 μm). NC, negative control; N, normoxia; H, hypoxia. (K) Quantification of DCFH-DA fluorescence intensity in HSP90AB1-knockdown CAL27/HSC3 cells reconstituted with HSP90AB1 variants under normoxia/hypoxia (24 h) (** P < 0.01 and *** P < 0.001, one-way ANOVA).](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_6717/pmc12886717/pmc12886717__research.1129.fig.003.jpg)
![K265 crotonylation induces conformational remodeling of HSP90AB1 to enhance TXN binding and stabilization. (A) Co-IP of endogenous HSP90AB1–TXN complexes in CAL27/HSC3 cells under normoxia or hypoxia. (B) Molecular dynamics simulation snapshots (100 ns) of the HSP90AB1–TXN complex: HSP90AB1 with K265 crotonylation (red), TXN (blue), and the crotonyl moiety at K265 (green). (C) Root mean square deviation (RMSD) trajectory of the HSP90AB1–TXN complex during molecular dynamics simulation. (D) Root mean square fluctuation (RMSF) per residue analysis of HSP90AB1 during simulation. (E) Radius of gyration measurements of HSP90AB1 during simulation. (F) Secondary structure composition analysis of HSP90AB1 (Define Secondary Structure of Proteins [DSSP] method). (G) Hydrogen bond formation between HSP90AB1 and TXN with simulation time. (H) Solvent-accessible surface area (SASA) measurements of the HSP90AB1–TXN complex during simulation. (I) Structural superposition of the initial (red) and equilibrated (cyan) HSP90AB1 conformations. (J) Molecular docking model of K265cr-modified HSP90AB1 (green) with TXN (purple/cyan). (K) Co-IP of Flag-HSP90AB1 in HSP90AB1-knockdown CAL27/HSC3 cells reconstituted with HSP90AB1 variants under normoxia/hypoxia (24 h). (L) Representative confocal microscopy images of DCFH-DA-stained CAL27/HSC3 cells expressing HSP90AB1 variants with/without TXN overexpression under normoxia/hypoxia (24 h) (200×, scale bars, 100 μm). (M) Quantification of DCFH-DA fluorescence intensity in CAL27/HSC3 cells expressing HSP90AB1 variants with/without TXN overexpression under normoxia/hypoxia (24 h) (** P < 0.01 and *** P < 0.001, one-way ANOVA).](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_6717/pmc12886717/pmc12886717__research.1129.fig.005.jpg)
