Addgene inc amino acids 1 81
Amino Acids 1 81, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/amino+acids+1+81/Quas%3AGFPpA%3BBetacrystallin%3ACFP+(Plasmid+%2381181)/ppr0868854-154-5-19
Average 93 stars, based on 1 article reviews

amino acids 1 81 - by Bioz Stars, 2026-09

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mouse monoclonal anti cytochrome c (Novus Biologicals)

Novus Biologicals mouse monoclonal anti cytochrome c
Mouse Monoclonal Anti Cytochrome C, 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/product/amino+acids+1+81/Cytochrome+c+Antibody+(7H8%2E2C12)+-+BSA+Free/pmc09580253-48-26-32
Average 94 stars, based on 1 article reviews

mouse monoclonal anti cytochrome c - by Bioz Stars, 2026-09

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saline tween 20 (ProSci Incorporated)

ProSci Incorporated saline tween 20
Saline Tween 20, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/amino+acids+1+81/AKR7A3+Antibody/pm26151763-42-11-48
Average 96 stars, based on 1 article reviews

saline tween 20 - by Bioz Stars, 2026-09

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c 2 (Santa Cruz Biotechnology)

Santa Cruz Biotechnology c 2
C 2, supplied by Santa Cruz Biotechnology, 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/product/amino+acids+1+81/1%2C2/pmc03152212-71-19-24
Average 94 stars, based on 1 article reviews

c 2 - by Bioz Stars, 2026-09

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bait p53 (Proteintech)

Proteintech bait p53

1. HDM2 expression constructs (blue and purple bars) appended with 2CONA <t>p53</t> response element (“RE”, green) and HA-tag coding sequence (black) and <t>p53</t> <t>expression</t> construct (red bar) are segregated into aqueous emulsion compartments along with PM2 (cyan helix). Protein expression occurs within compartments. PM2 inhibition of HDM2 results in no HDM2-p53-DNA complex formation (left bubble), whereas resistant HDM2 can form the complex (right bubble). 2–3 . The emulsion is broken and complexes captured with anti-HA antibody. DNA encoding resistant HDM2 variants is amplified by PCR. 4. Selectants further evaluated by secondary pull-down assay or subjected to further rounds of selection.

Bait P53, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/amino+acids+1+81/P53+Antibody/pmc05078010-178-4-29
Average 96 stars, based on 1 article reviews

bait p53 - by Bioz Stars, 2026-09

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anticytochrome c antibody (Novus Biologicals)

Novus Biologicals anticytochrome c antibody

Anticytochrome C Antibody, 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/product/amino+acids+1+81/Cytochrome+c+Antibody+(7H8%2E2C12)+-+BSA+Free/pm40107336-158-13-19
Average 94 stars, based on 1 article reviews

anticytochrome c antibody - by Bioz Stars, 2026-09

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Image Search Results

1. HDM2 expression constructs (blue and purple bars) appended with 2CONA p53 response element (“RE”, green) and HA-tag coding sequence (black) and p53 expression construct (red bar) are segregated into aqueous emulsion compartments along with PM2 (cyan helix). Protein expression occurs within compartments. PM2 inhibition of HDM2 results in no HDM2-p53-DNA complex formation (left bubble), whereas resistant HDM2 can form the complex (right bubble). 2–3 . The emulsion is broken and complexes captured with anti-HA antibody. DNA encoding resistant HDM2 variants is amplified by PCR. 4. Selectants further evaluated by secondary pull-down assay or subjected to further rounds of selection.

Journal: Oncotarget

Article Title: Avoiding drug resistance through extended drug target interfaces: a case for stapled peptides

doi: 10.18632/oncotarget.8572

Figure Lengend Snippet: 1. HDM2 expression constructs (blue and purple bars) appended with 2CONA p53 response element (“RE”, green) and HA-tag coding sequence (black) and p53 expression construct (red bar) are segregated into aqueous emulsion compartments along with PM2 (cyan helix). Protein expression occurs within compartments. PM2 inhibition of HDM2 results in no HDM2-p53-DNA complex formation (left bubble), whereas resistant HDM2 can form the complex (right bubble). 2–3 . The emulsion is broken and complexes captured with anti-HA antibody. DNA encoding resistant HDM2 variants is amplified by PCR. 4. Selectants further evaluated by secondary pull-down assay or subjected to further rounds of selection.

Article Snippet: Plasmids encoding the GFP-tagged bait p53 (amino acids 1-81) fusion protein and different RFP-tagged prey HDM2 (amino acids 7-134) fusion proteins were co-transfected into transgenic F2H-BHK cells (F2H-Kit Basic, ChromoTek GmbH) [ ] in 96 multiwell plates (μClear Greiner Bio-One, Germany) using the Lipofectamine 2000 (Life Technologies) reverse transfection protocol according to manufacturer's instructions with 0.2 μg DNA and 0.4 μl Lipofectamine 2000 per well.

Techniques: Expressing, Construct, Sequencing, Inhibition, Amplification, Pull Down Assay, Selection

A. In vitro pull-down assay showing reduced inhibition by PM2 (10 μM) to binding of p53 for indicated parental HDM2 variants and WT HDM2 (residues 1-125). Note: exposure time for HDM2 inputs is 8 hours and 1 second for all other panels. B. in vitro pull-down assay showing little impact upon reversion of the M62A mutation to PM2 binding in HDM2-C8 (residues1-125). Blank indicates background p53 binding in absence of HDM2. Note: exposure time for HDM2 inputs (developed using film) is 8 hours and 10 second for all other panels (digitally acquired).

Journal: Oncotarget

Article Title: Avoiding drug resistance through extended drug target interfaces: a case for stapled peptides

doi: 10.18632/oncotarget.8572

Figure Lengend Snippet: A. In vitro pull-down assay showing reduced inhibition by PM2 (10 μM) to binding of p53 for indicated parental HDM2 variants and WT HDM2 (residues 1-125). Note: exposure time for HDM2 inputs is 8 hours and 1 second for all other panels. B. in vitro pull-down assay showing little impact upon reversion of the M62A mutation to PM2 binding in HDM2-C8 (residues1-125). Blank indicates background p53 binding in absence of HDM2. Note: exposure time for HDM2 inputs (developed using film) is 8 hours and 10 second for all other panels (digitally acquired).

Techniques: In Vitro, Pull Down Assay, Inhibition, Binding Assay, Mutagenesis

In vitro pull-down assay showing reduced inhibition by PM2 (10 μM) to indicated point mutants (asterisk) derived from HDM2-C8 (residues 1-125). The point mutants L34P, F55L, Y60C and C77R also show reduced inhibition by Nutlin (10μM). Blank indicates background p53 binding in absence of HDM2. Note: exposure time for HDM2 inputs is 8 hours (developed using film) and 3 minutes for all other panels (digitally acquired).

Journal: Oncotarget

Article Title: Avoiding drug resistance through extended drug target interfaces: a case for stapled peptides

doi: 10.18632/oncotarget.8572

Figure Lengend Snippet: In vitro pull-down assay showing reduced inhibition by PM2 (10 μM) to indicated point mutants (asterisk) derived from HDM2-C8 (residues 1-125). The point mutants L34P, F55L, Y60C and C77R also show reduced inhibition by Nutlin (10μM). Blank indicates background p53 binding in absence of HDM2. Note: exposure time for HDM2 inputs is 8 hours (developed using film) and 3 minutes for all other panels (digitally acquired).

Techniques: In Vitro, Pull Down Assay, Inhibition, Derivative Assay, Binding Assay

A. In vitro pull-down assay showing reduced inhibition by PM2 (10 μM) to indicated C8-derived point mutants (asterisk) present in full-length HDM2 The point mutant F55L also shows reduced inhibition by Nutlin (10μM). Blank indicates background p53 binding in absence of HDM2. B. As in A, additionally showing levels of wild type and indicated HDM2 variants co-eluted off beads after pull-down following mock (panel 3) and PM2 treatment (panel 4). Note exposure time for p53 pull-down in absence of treatment (panel 1) is 5s and 10 minutes for pull-down after PM2 treatment (panel 2, developed using film). Exposure time for HDM2 input and HDM2 (+ indicated variants) eluted off beads after pull-down is 30 seconds (digitally acquired).

Journal: Oncotarget

Article Title: Avoiding drug resistance through extended drug target interfaces: a case for stapled peptides

doi: 10.18632/oncotarget.8572

Figure Lengend Snippet: A. In vitro pull-down assay showing reduced inhibition by PM2 (10 μM) to indicated C8-derived point mutants (asterisk) present in full-length HDM2 The point mutant F55L also shows reduced inhibition by Nutlin (10μM). Blank indicates background p53 binding in absence of HDM2. B. As in A, additionally showing levels of wild type and indicated HDM2 variants co-eluted off beads after pull-down following mock (panel 3) and PM2 treatment (panel 4). Note exposure time for p53 pull-down in absence of treatment (panel 1) is 5s and 10 minutes for pull-down after PM2 treatment (panel 2, developed using film). Exposure time for HDM2 input and HDM2 (+ indicated variants) eluted off beads after pull-down is 30 seconds (digitally acquired).

Techniques: In Vitro, Pull Down Assay, Inhibition, Derivative Assay, Mutagenesis, Binding Assay

A. Wild-type and HDM2-C8 (full-length) were co-transfected with p53 and p53-reporter gene, and reporter gene activity measured in the presence of PM2 (20 μM) or Nutlin (10 μM). p53 activity is denoted as percentage of that observed when p53-alone co-transfected with reporter gene. Shown below are Western blots indicating expression levels of HDM2 variants and p53 cotransfected into DKO cells. B and C. As in ‘A’, with wild-type HDM2 and indicated HDM2-C8 derived point mutants (full length) co-transfected into DKO cells. p53 activity is denoted as percentage of that observed when p53-alone co-transfected with reporter gene. Shown below are Western blots indicating expression levels of HDM2 variants and p53 cotransfected into DKO cells.

Journal: Oncotarget

Article Title: Avoiding drug resistance through extended drug target interfaces: a case for stapled peptides

doi: 10.18632/oncotarget.8572

Figure Lengend Snippet: A. Wild-type and HDM2-C8 (full-length) were co-transfected with p53 and p53-reporter gene, and reporter gene activity measured in the presence of PM2 (20 μM) or Nutlin (10 μM). p53 activity is denoted as percentage of that observed when p53-alone co-transfected with reporter gene. Shown below are Western blots indicating expression levels of HDM2 variants and p53 cotransfected into DKO cells. B and C. As in ‘A’, with wild-type HDM2 and indicated HDM2-C8 derived point mutants (full length) co-transfected into DKO cells. p53 activity is denoted as percentage of that observed when p53-alone co-transfected with reporter gene. Shown below are Western blots indicating expression levels of HDM2 variants and p53 cotransfected into DKO cells.

Techniques: Transfection, Activity Assay, Western Blot, Expressing, Derivative Assay

Overlay of p53 peptide (green) and MO6 stapled peptide (cyan, with staple moiety in grey) when bound to HDM2 N-terminal domains. The relative configurations of the key F19 and W23 residues are conserved, with some deviation in the orientation of L26. Adapted from 1YCR and 4UMN. Shown below is alignment of p53 peptide, PM2 and MO6, with signature residues shaded and residue differing between PM2 and MO6 highlighted in red.

Journal: Oncotarget

Article Title: Avoiding drug resistance through extended drug target interfaces: a case for stapled peptides

doi: 10.18632/oncotarget.8572

Figure Lengend Snippet: Overlay of p53 peptide (green) and MO6 stapled peptide (cyan, with staple moiety in grey) when bound to HDM2 N-terminal domains. The relative configurations of the key F19 and W23 residues are conserved, with some deviation in the orientation of L26. Adapted from 1YCR and 4UMN. Shown below is alignment of p53 peptide, PM2 and MO6, with signature residues shaded and residue differing between PM2 and MO6 highlighted in red.

Techniques:

Left: Overlay of p53 peptide (green) and MO6 stapled peptide (cyan, staple in gray) bound to HDM2 N-terminal domain (magenta, surface representation). The positions of the F55 and I99 residues are indicated in yellow. Right: Same as left, highlighting the relative orientation of the p53 peptide and MO6 stapled peptide L26 side chains in respect to I99 in HDM2.

Journal: Oncotarget

Article Title: Avoiding drug resistance through extended drug target interfaces: a case for stapled peptides

doi: 10.18632/oncotarget.8572

Figure Lengend Snippet: Left: Overlay of p53 peptide (green) and MO6 stapled peptide (cyan, staple in gray) bound to HDM2 N-terminal domain (magenta, surface representation). The positions of the F55 and I99 residues are indicated in yellow. Right: Same as left, highlighting the relative orientation of the p53 peptide and MO6 stapled peptide L26 side chains in respect to I99 in HDM2.

Techniques:

amino acids 1 81 Search Results

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