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2470 microarray robot  (Aushon Biosystems)

 
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    Structured Review

    Aushon Biosystems 2470 microarray robot
    Protein <t>microarray</t> data indicate that phosphorylation of S298 in maCx35 may act as a functional switch. ( a ) Membrane topology of connexins. N- and C-terminal tails (NT and CT, respectively) and the cytoplasmic loop (CL) reside inside the cytoplasm. The two extracellular loops (EL) are also indicated. ( b ) Sequence of the C-terminal end of maCx35/mmCx36, as indicated by the box in ( a ). Sequence identity (*) is high for mmCx36 and maCx35 at the C-terminal end. The blue box indicates a PKA/CaMKII consensus site at position S315 and S298 for mmCx36 and maCx35, respectively. The last four amino acids represent a PDZ binding domain, present in both proteins. ( c ) Microarray layout (A-D); the respective baits (all fused to GST) are found below. An array probed with Alexa Fluor 555 anti-GST antibody served as positive control. Peptides fused to biotin containing the C-terminal tail of maCx35 (35 WT), phosphorylated maCx35 (35 S298 phos), and a truncated version (35 S298 ter) were used as probes and showed differential results, marked by rounded squares. 14–3–3 proteins (red) and NHERF2 aa265-288 (blue D7) showed an increased binding to the 35 S298 phospho probe compared to 35 WT. In contrast, PDZK1, PDZ10 of MUPP1, and nNOS (blue) decreased their binding to the 35 S298 phospho probe. The truncated 35 S298 ter probe showed no binding interactions.
    2470 Microarray Robot, supplied by Aushon Biosystems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/2470+microarray/2470+microarray+robot/pmc07592057-162-21-20
    Average 90 stars, based on 1 article reviews
    2470 microarray robot - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "Phosphorylation of Connexin36 near the C-terminus switches binding affinities for PDZ-domain and 14–3–3 proteins in vitro"

    Article Title: Phosphorylation of Connexin36 near the C-terminus switches binding affinities for PDZ-domain and 14–3–3 proteins in vitro

    Journal: Scientific Reports

    doi: 10.1038/s41598-020-75375-0

    Protein microarray data indicate that phosphorylation of S298 in maCx35 may act as a functional switch. ( a ) Membrane topology of connexins. N- and C-terminal tails (NT and CT, respectively) and the cytoplasmic loop (CL) reside inside the cytoplasm. The two extracellular loops (EL) are also indicated. ( b ) Sequence of the C-terminal end of maCx35/mmCx36, as indicated by the box in ( a ). Sequence identity (*) is high for mmCx36 and maCx35 at the C-terminal end. The blue box indicates a PKA/CaMKII consensus site at position S315 and S298 for mmCx36 and maCx35, respectively. The last four amino acids represent a PDZ binding domain, present in both proteins. ( c ) Microarray layout (A-D); the respective baits (all fused to GST) are found below. An array probed with Alexa Fluor 555 anti-GST antibody served as positive control. Peptides fused to biotin containing the C-terminal tail of maCx35 (35 WT), phosphorylated maCx35 (35 S298 phos), and a truncated version (35 S298 ter) were used as probes and showed differential results, marked by rounded squares. 14–3–3 proteins (red) and NHERF2 aa265-288 (blue D7) showed an increased binding to the 35 S298 phospho probe compared to 35 WT. In contrast, PDZK1, PDZ10 of MUPP1, and nNOS (blue) decreased their binding to the 35 S298 phospho probe. The truncated 35 S298 ter probe showed no binding interactions.
    Figure Legend Snippet: Protein microarray data indicate that phosphorylation of S298 in maCx35 may act as a functional switch. ( a ) Membrane topology of connexins. N- and C-terminal tails (NT and CT, respectively) and the cytoplasmic loop (CL) reside inside the cytoplasm. The two extracellular loops (EL) are also indicated. ( b ) Sequence of the C-terminal end of maCx35/mmCx36, as indicated by the box in ( a ). Sequence identity (*) is high for mmCx36 and maCx35 at the C-terminal end. The blue box indicates a PKA/CaMKII consensus site at position S315 and S298 for mmCx36 and maCx35, respectively. The last four amino acids represent a PDZ binding domain, present in both proteins. ( c ) Microarray layout (A-D); the respective baits (all fused to GST) are found below. An array probed with Alexa Fluor 555 anti-GST antibody served as positive control. Peptides fused to biotin containing the C-terminal tail of maCx35 (35 WT), phosphorylated maCx35 (35 S298 phos), and a truncated version (35 S298 ter) were used as probes and showed differential results, marked by rounded squares. 14–3–3 proteins (red) and NHERF2 aa265-288 (blue D7) showed an increased binding to the 35 S298 phospho probe compared to 35 WT. In contrast, PDZK1, PDZ10 of MUPP1, and nNOS (blue) decreased their binding to the 35 S298 phospho probe. The truncated 35 S298 ter probe showed no binding interactions.

    Techniques Used: Microarray, Functional Assay, Sequencing, Binding Assay, Positive Control

    Related Articles

    Purification:

    Article Title: Phosphorylation of Connexin36 near the C-terminus switches binding affinities for PDZ-domain and 14–3–3 proteins in vitro
    Article Snippet: .. Purified GST fusion proteins (listed in Fig. c and Supplementary Fig. ) were spotted onto nitrocellulose-coated glass slides with an Aushon 2470 microarray robot; each protein was spotted in duplicate. .. Peptides corresponding to the C-terminus tip of maCx35 and mmCx36, their phosphorylated forms, a C-terminally truncated form of maCx35 and a scrambled form of mmCx36, each with an N-terminal biotin, were synthesized by Genscript.

    Microarray:

    Article Title: Phosphorylation of Connexin36 near the C-terminus switches binding affinities for PDZ-domain and 14–3–3 proteins in vitro
    Article Snippet: .. Purified GST fusion proteins (listed in Fig. c and Supplementary Fig. ) were spotted onto nitrocellulose-coated glass slides with an Aushon 2470 microarray robot; each protein was spotted in duplicate. .. Peptides corresponding to the C-terminus tip of maCx35 and mmCx36, their phosphorylated forms, a C-terminally truncated form of maCx35 and a scrambled form of mmCx36, each with an N-terminal biotin, were synthesized by Genscript.



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    Protein <t>microarray</t> data indicate that phosphorylation of S298 in maCx35 may act as a functional switch. ( a ) Membrane topology of connexins. N- and C-terminal tails (NT and CT, respectively) and the cytoplasmic loop (CL) reside inside the cytoplasm. The two extracellular loops (EL) are also indicated. ( b ) Sequence of the C-terminal end of maCx35/mmCx36, as indicated by the box in ( a ). Sequence identity (*) is high for mmCx36 and maCx35 at the C-terminal end. The blue box indicates a PKA/CaMKII consensus site at position S315 and S298 for mmCx36 and maCx35, respectively. The last four amino acids represent a PDZ binding domain, present in both proteins. ( c ) Microarray layout (A-D); the respective baits (all fused to GST) are found below. An array probed with Alexa Fluor 555 anti-GST antibody served as positive control. Peptides fused to biotin containing the C-terminal tail of maCx35 (35 WT), phosphorylated maCx35 (35 S298 phos), and a truncated version (35 S298 ter) were used as probes and showed differential results, marked by rounded squares. 14–3–3 proteins (red) and NHERF2 aa265-288 (blue D7) showed an increased binding to the 35 S298 phospho probe compared to 35 WT. In contrast, PDZK1, PDZ10 of MUPP1, and nNOS (blue) decreased their binding to the 35 S298 phospho probe. The truncated 35 S298 ter probe showed no binding interactions.
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    Protein <t>microarray</t> data indicate that phosphorylation of S298 in maCx35 may act as a functional switch. ( a ) Membrane topology of connexins. N- and C-terminal tails (NT and CT, respectively) and the cytoplasmic loop (CL) reside inside the cytoplasm. The two extracellular loops (EL) are also indicated. ( b ) Sequence of the C-terminal end of maCx35/mmCx36, as indicated by the box in ( a ). Sequence identity (*) is high for mmCx36 and maCx35 at the C-terminal end. The blue box indicates a PKA/CaMKII consensus site at position S315 and S298 for mmCx36 and maCx35, respectively. The last four amino acids represent a PDZ binding domain, present in both proteins. ( c ) Microarray layout (A-D); the respective baits (all fused to GST) are found below. An array probed with Alexa Fluor 555 anti-GST antibody served as positive control. Peptides fused to biotin containing the C-terminal tail of maCx35 (35 WT), phosphorylated maCx35 (35 S298 phos), and a truncated version (35 S298 ter) were used as probes and showed differential results, marked by rounded squares. 14–3–3 proteins (red) and NHERF2 aa265-288 (blue D7) showed an increased binding to the 35 S298 phospho probe compared to 35 WT. In contrast, PDZK1, PDZ10 of MUPP1, and nNOS (blue) decreased their binding to the 35 S298 phospho probe. The truncated 35 S298 ter probe showed no binding interactions.
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    Image Search Results


    Protein microarray data indicate that phosphorylation of S298 in maCx35 may act as a functional switch. ( a ) Membrane topology of connexins. N- and C-terminal tails (NT and CT, respectively) and the cytoplasmic loop (CL) reside inside the cytoplasm. The two extracellular loops (EL) are also indicated. ( b ) Sequence of the C-terminal end of maCx35/mmCx36, as indicated by the box in ( a ). Sequence identity (*) is high for mmCx36 and maCx35 at the C-terminal end. The blue box indicates a PKA/CaMKII consensus site at position S315 and S298 for mmCx36 and maCx35, respectively. The last four amino acids represent a PDZ binding domain, present in both proteins. ( c ) Microarray layout (A-D); the respective baits (all fused to GST) are found below. An array probed with Alexa Fluor 555 anti-GST antibody served as positive control. Peptides fused to biotin containing the C-terminal tail of maCx35 (35 WT), phosphorylated maCx35 (35 S298 phos), and a truncated version (35 S298 ter) were used as probes and showed differential results, marked by rounded squares. 14–3–3 proteins (red) and NHERF2 aa265-288 (blue D7) showed an increased binding to the 35 S298 phospho probe compared to 35 WT. In contrast, PDZK1, PDZ10 of MUPP1, and nNOS (blue) decreased their binding to the 35 S298 phospho probe. The truncated 35 S298 ter probe showed no binding interactions.

    Journal: Scientific Reports

    Article Title: Phosphorylation of Connexin36 near the C-terminus switches binding affinities for PDZ-domain and 14–3–3 proteins in vitro

    doi: 10.1038/s41598-020-75375-0

    Figure Lengend Snippet: Protein microarray data indicate that phosphorylation of S298 in maCx35 may act as a functional switch. ( a ) Membrane topology of connexins. N- and C-terminal tails (NT and CT, respectively) and the cytoplasmic loop (CL) reside inside the cytoplasm. The two extracellular loops (EL) are also indicated. ( b ) Sequence of the C-terminal end of maCx35/mmCx36, as indicated by the box in ( a ). Sequence identity (*) is high for mmCx36 and maCx35 at the C-terminal end. The blue box indicates a PKA/CaMKII consensus site at position S315 and S298 for mmCx36 and maCx35, respectively. The last four amino acids represent a PDZ binding domain, present in both proteins. ( c ) Microarray layout (A-D); the respective baits (all fused to GST) are found below. An array probed with Alexa Fluor 555 anti-GST antibody served as positive control. Peptides fused to biotin containing the C-terminal tail of maCx35 (35 WT), phosphorylated maCx35 (35 S298 phos), and a truncated version (35 S298 ter) were used as probes and showed differential results, marked by rounded squares. 14–3–3 proteins (red) and NHERF2 aa265-288 (blue D7) showed an increased binding to the 35 S298 phospho probe compared to 35 WT. In contrast, PDZK1, PDZ10 of MUPP1, and nNOS (blue) decreased their binding to the 35 S298 phospho probe. The truncated 35 S298 ter probe showed no binding interactions.

    Article Snippet: Purified GST fusion proteins (listed in Fig. c and Supplementary Fig. ) were spotted onto nitrocellulose-coated glass slides with an Aushon 2470 microarray robot; each protein was spotted in duplicate.

    Techniques: Microarray, Functional Assay, Sequencing, Binding Assay, Positive Control

    Materials

    Journal: Journal of visualized experiments : JoVE

    Article Title: Analysis of Histone Antibody Specificity with Peptide Microarrays

    doi: 10.3791/55912

    Figure Lengend Snippet: Materials

    Article Snippet: contact microarray printer , Aushon , 2470 , Aushon 2470 Microarray Printer.

    Techniques: Microscopy, Microarray, Blocking Assay, Plasmid Preparation, Hybridization, Peptide Microarray, Modification, High Throughput Screening Assay

    A screen shot of the ArrayNinja design module is shown in the dotted line. The control panel (top) shows all of the parameters that can be altered on the microarray printer. As these parameters are adjusted, the cartoon image of the slide layout (bottom left) updates in real time. After the layout is set, the user can mouse over individual spots to enter unique feature identifiers. ArrayNinja constructs from this user input a map of the position of each feature in the source plate(s) (bottom right) needed to fabricate a specified microarray slide layout.

    Journal: Journal of visualized experiments : JoVE

    Article Title: Analysis of Histone Antibody Specificity with Peptide Microarrays

    doi: 10.3791/55912

    Figure Lengend Snippet: A screen shot of the ArrayNinja design module is shown in the dotted line. The control panel (top) shows all of the parameters that can be altered on the microarray printer. As these parameters are adjusted, the cartoon image of the slide layout (bottom left) updates in real time. After the layout is set, the user can mouse over individual spots to enter unique feature identifiers. ArrayNinja constructs from this user input a map of the position of each feature in the source plate(s) (bottom right) needed to fabricate a specified microarray slide layout.

    Article Snippet: contact microarray printer , Aushon , 2470 , Aushon 2470 Microarray Printer.

    Techniques: Microarray, Construct

    (A) Histone peptide microarray fabrication on streptavidin-coated microscope slides using a contact microarray printer. (B) Microarrays fabricated with 3 subarrays of a 48 × 48 grid of peptide features. Separation of (C) 3 subarrays with a hydrophobic wax pen, (D) 2 subarrays with a silicon adhesive, and (E) 48 subarrays with a wax imprint. All microarrays shown are fabricated using 25 × 75 mm microscope slides.

    Journal: Journal of visualized experiments : JoVE

    Article Title: Analysis of Histone Antibody Specificity with Peptide Microarrays

    doi: 10.3791/55912

    Figure Lengend Snippet: (A) Histone peptide microarray fabrication on streptavidin-coated microscope slides using a contact microarray printer. (B) Microarrays fabricated with 3 subarrays of a 48 × 48 grid of peptide features. Separation of (C) 3 subarrays with a hydrophobic wax pen, (D) 2 subarrays with a silicon adhesive, and (E) 48 subarrays with a wax imprint. All microarrays shown are fabricated using 25 × 75 mm microscope slides.

    Article Snippet: contact microarray printer , Aushon , 2470 , Aushon 2470 Microarray Printer.

    Techniques: Peptide Microarray, Microscopy, Microarray