cdk8 santa cruz (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology
cdk8 santa cruz
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Cdk8 Santa Cruz, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 133 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cdk8+santa+cruz/Cdk8+Antibody/bio_rxiv__2025__11__06__686927-275-0-2
Average 93 stars, based on 133 article reviews
Cdk8 Santa Cruz, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 133 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cdk8+santa+cruz/Cdk8+Antibody/bio_rxiv__2025__11__06__686927-275-0-2
Average 93 stars, based on 133 article reviews
cdk8 santa cruz - by Bioz Stars,
2026-10
93/100 stars
Images
1) Product Images from "Discovery and chemical biology of CDK8 inhibitors reveals insights for kinase inhibitor development"
Article Title: Discovery and chemical biology of CDK8 inhibitors reveals insights for kinase inhibitor development
Journal: bioRxiv
doi: 10.1101/2025.11.06.686927
Figure Legend Snippet:
Techniques Used:
Figure Legend Snippet:
Techniques Used:
Figure Legend Snippet: Superposition of docked Sorafenib (cyan carbon atoms) onto its corresponding crystallographic structure. Sorafenib from 3RGF is depicted with light gray carbon atoms. As no structure of CDK8 with ATP is available, the ATP (dark gray carbon atoms) of the superposed structure of the human CDK2/Cyclin A complex (PDB ID: 4EOQ) is shown to highlight its potential binding site in CDK8.
Techniques Used: Binding Assay
![Compounds were tested in duplicate at 10 µM in kinase assays with recombinant CDK8/Cyc C complex, in the presence of 15 µM [γ- 33 P] ATP. The graph represents the residual CDK8 activity (%) for each compound tested (blue dots); background controls (red dots) and negative control (DMSO 1%, green dots). 36 compounds inhibit CDK8 to below 50%.](https://bio-rxiv-images-cdn.bioz.com/dois_ending_with_27/10__1101_slash_2025__11__06__686927/10__1101_slash_2025__11__06__686927___F10.large.jpg "... at 10 µM in kinase assays with recombinant CDK8/Cyc C complex, in the presence of 15 µM ...")
Figure Legend Snippet: Compounds were tested in duplicate at 10 µM in kinase assays with recombinant CDK8/Cyc C complex, in the presence of 15 µM [γ- 33 P] ATP. The graph represents the residual CDK8 activity (%) for each compound tested (blue dots); background controls (red dots) and negative control (DMSO 1%, green dots). 36 compounds inhibit CDK8 to below 50%.
Techniques Used: Recombinant, Activity Assay, Negative Control
Figure Legend Snippet: Thirty six selected compounds and Senexin A (SNX A) were tested in dose-response on CDK8/Cyc C in kinase assays. IC 50 is expressed in µM and calculated from dose-response curves (each curve was performed in duplicate). The graph represents the distribution of IC 50 obtained, with two threshold lines: at 100 nM (red line) and 1 µM (green line).
Techniques Used:
Figure Legend Snippet: A. Left, DepMap analysis of dependecy of cancer cell lines on CDK8 and CDK1 (an example of an essential CDK), from genome-wide CRISPR screens. Score 0 indicates a non essential gene; score of -1 corresponds to a median of all common essential genes. Right, number of cancer cell lines dependent on the indicated gene according to the DepMap CRISPR screen database. All CDKs and kinases used to screen for CDK8/19 inhibitor specificity are shown. B. Expression levels (from RNAseq data, TPM-normalised and represented as log2(TPM+1)) and relative copy number (based on whole exome sequencing) in cancer cell lines. C. cBioPortal mutation analysis of the indicated genes in pancancer TCGA data.
Techniques Used: Genome Wide, CRISPR, Expressing, Sequencing, Mutagenesis
Figure Legend Snippet: Induced fit docking experiments were performed using either CDK8 (PDB: 3RGF) or CDK2 (PDB: 4GCJ) structures as protein target. Upper panels: ID and structural formula of the seven selected compounds. Lower panels: 3D arrangement of the best docking pose (white carbon atoms) into CDK8 or CDK2 active site with its corresponding docking score. Amino acids from the CDK8 DMG loop are represented in ball and stick; corresponding residues (DFG) in CDK2 structure are also highlighted.
Techniques Used:
Figure Legend Snippet: A. MEFs seeded at 10 6 in 10 cm plates were grown for 5 days at 10 μM of drugs and imaged. B. Colony formation assay (CFA) with WT SV-40-immortalised MEFs, seeded at 15 000 in 10cm plates, treated with inhibitors at 10 μM for 8 days. N=2. C. CFA with immortalised MEFs, WT, CDK8 -/- , CDK19 -/- , or double knock-out, treated with inhibitors at 10μM for 6d. N = 2. D. 3T3-immortalised MEFs were treated for 2h with the indicated inhibitors, after which γIFN (at 100 ng/ml) was added for 1h, without changing the media. Cells were collected and samples prepared for WB analysis. CDK8/19 double knockout MEF cells were used as a positive control (for the absence of STAT1-S727ph signal). N=2. E. HCT116 cells grown in spheroids were pre-incubated with γIFN (at 20 ng/ml) for 3h and treated with selected inhibitors at 10 μM or DMSO at 0.1% for 3h. Spheroids were lysed and analysed by Western blotting for the indicated proteins. Normalised STAT1-S727ph/STAT1 signal ratio are shown. N=2.
Techniques Used: Colony Assay, Knock-Out, Double Knockout, Positive Control, Incubation, Western Blot
Figure Legend Snippet: SV-40-immortalised MEF cell lysates (A, in vitro N=4) or MEF cells (B, in vivo , N=6) were treated with the indicated CDK8/19 inhibitors, or DMSO as a control, followed by heat treatment at the indicated temperatures and Western Blot analysis with anti-CDK8 antibody.
Techniques Used: In Vitro, In Vivo, Control, Western Blot
Figure Legend Snippet: A. CDK8 was immunoprecipitated from interphase egg extract and the beads were blotted for the indicated proteins. B. Interphase egg extract was fractionated by sucrose gradient and fractions were blotted for the indicated proteins. C. Left, chromosomal DNA replication quantified by 32 P-dCTP incorporation assay, in control conditions, or after addition of recombinant Geminin, to block replication licencing. Right, chromatin loading of pre-replication complex (ORC2, MCM5 and CDC6) and pre-initiation complex (PCNA) replication factors, CDK8 and Cyclin C during DNA replication time course. N=4. D. Left, immunodepletion of CDK8 (but not using Mock beads) removes majority of the kinase from the interphase egg extract; GADPH was used as loading control. Right, chromatin fractions from CDK8- or Mock-immunodepleted egg extract, or CDK8-depleted extract supplemented with recombinant CDK8-Cyclin C complex were analysed by WB with the indidated proteins. Slower migrating recombinant GST-CDK8 and His-Cyclin C are indidated. E. Chromosomal DNA replication in immunodepleted extracts, as in D, was quantified. N=3. Error bars show standard deviation. F,G. Chromosomal DNA replication quantified by 32 P-dCTP incorporation assay, in control conditions (DMSO), or in the presense of the indicated inhibitors.
Techniques Used: Immunoprecipitation, Control, Recombinant, Blocking Assay, Immunodepletion, Standard Deviation
Figure Legend Snippet: A. Alignment of the 20 CDK sequences. Only the regions containing the amino acids responsible for interactions with the compounds are shown. Interacting amino acids and their conservation are highlighted. B. View of the CDK8 amino acid residues involved in contact with compounds. The seven compounds are superposed and shown with gray balls. Interacting residues are depicted by colored balls and sticks according to their percentage of conservation (red: highly conserved residues (71-100%); pink: moderately conserved residues (35-70%); green: poorly conserved resides (10-34%)). C. Highlight of virtually mutated residues. Left panel: wild-type CDK8 showing the seven residues selected (ball and stick and dark grey carbon) to assess the effect of point mutations on compound binding. The induced fit pose of molecule #82 is shown (ball and stick and light grey carbon). Right panel: superposition of the poses obtained for each mutant following induced-fit docking. For clarity, only one of the two side chains is shown (ball and stick and dark grey carbon) in the case of the A100M/L and L158R/W mutants. In contrast, all the positions obtained for compound #82 are shown (ball and stick and light grey carbon).
Techniques Used: Binding Assay, Mutagenesis
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Techniques Used: Generated, Residue, Binding Assay
Figure Legend Snippet:
Techniques Used: Binding Assay
Figure Legend Snippet: Overlay of structures of selected inhibitors with the inactive (DMG-out, PDB 3RGF; A, cyan) and active (DMG-in) conformations, without (PDB 5XS2; A and B, blue) and with MED12 (PDB 8TQ2; B, cyan). Zoom-in on ATP-binding pocket of CDK8, with side chains of D173 and M174 shown. In red, inhibitor docked into 5XS2; in yellow, inhibitor docked into 3RGF, A, and 8TQ2, B. Induced fit docking scores for compared structures are indicated.
Techniques Used: Binding Assay
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