di c16 ptdins 3 p  (Echelon Biosciences)


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    Echelon Biosciences di c16 ptdins 3 p
    ( A ) Interactions of retromer with TBC1D5, SNX3, SNX27, and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for retromer, while GST-tagged retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550–568 present), ( D ) SNX27 PDZ , and ( E ) GST-Fam21 R19-R21 with retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS–polyacrylamide gel electrophoresis (PAGE) and Western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586–593 cargo peptide  with SNX27 PDZ alone (yellow), retromer + RT-L4 (red), retromer + SNX27 PDZ (green), and retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27. All ITC graphs represent the integrated and normalized data fit with a 1-to-1 binding ratio. The binding affinity ( K d ) is given as means of at least two independent experiments. ( H ) Liposome binding assay of retromer with membrane-associated SNX3-cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CI-MPR 2347–2376 peptide (schematic diagram on top). “S” and “P” indicate unbound supernatant and bound pellet, respectively. Control experiments are shown in fig. S7 (B and C). ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on retromer engagement with known regulatory, adaptor, and bacterial effector proteins.
    Di C16 Ptdins 3 P, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 1 article reviews
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    di c16 ptdins 3 p - by Bioz Stars, 2024-05
    93/100 stars

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    1) Product Images from "De novo macrocyclic peptides for inhibiting, stabilizing, and probing the function of the retromer endosomal trafficking complex"

    Article Title: De novo macrocyclic peptides for inhibiting, stabilizing, and probing the function of the retromer endosomal trafficking complex

    Journal: Science Advances

    doi: 10.1126/sciadv.abg4007

    ( A ) Interactions of retromer with TBC1D5, SNX3, SNX27, and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for retromer, while GST-tagged retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550–568 present), ( D ) SNX27 PDZ , and ( E ) GST-Fam21 R19-R21 with retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS–polyacrylamide gel electrophoresis (PAGE) and Western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586–593 cargo peptide  with SNX27 PDZ alone (yellow), retromer + RT-L4 (red), retromer + SNX27 PDZ (green), and retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27. All ITC graphs represent the integrated and normalized data fit with a 1-to-1 binding ratio. The binding affinity ( K d ) is given as means of at least two independent experiments. ( H ) Liposome binding assay of retromer with membrane-associated SNX3-cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CI-MPR 2347–2376 peptide (schematic diagram on top). “S” and “P” indicate unbound supernatant and bound pellet, respectively. Control experiments are shown in fig. S7 (B and C). ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on retromer engagement with known regulatory, adaptor, and bacterial effector proteins.
    Figure Legend Snippet: ( A ) Interactions of retromer with TBC1D5, SNX3, SNX27, and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for retromer, while GST-tagged retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550–568 present), ( D ) SNX27 PDZ , and ( E ) GST-Fam21 R19-R21 with retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS–polyacrylamide gel electrophoresis (PAGE) and Western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586–593 cargo peptide with SNX27 PDZ alone (yellow), retromer + RT-L4 (red), retromer + SNX27 PDZ (green), and retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27. All ITC graphs represent the integrated and normalized data fit with a 1-to-1 binding ratio. The binding affinity ( K d ) is given as means of at least two independent experiments. ( H ) Liposome binding assay of retromer with membrane-associated SNX3-cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CI-MPR 2347–2376 peptide (schematic diagram on top). “S” and “P” indicate unbound supernatant and bound pellet, respectively. Control experiments are shown in fig. S7 (B and C). ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on retromer engagement with known regulatory, adaptor, and bacterial effector proteins.

    Techniques Used: Incubation, Polyacrylamide Gel Electrophoresis, Western Blot, Binding Assay

    di c16 ptdins 3 p  (Echelon Biosciences)


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    Echelon Biosciences di c16 ptdins 3 p
    ( A ) Interactions of retromer with TBC1D5, SNX3, SNX27, and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for retromer, while GST-tagged retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550–568 present), ( D ) SNX27 PDZ , and ( E ) GST-Fam21 R19-R21 with retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS–polyacrylamide gel electrophoresis (PAGE) and Western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586–593 cargo peptide  with SNX27 PDZ alone (yellow), retromer + RT-L4 (red), retromer + SNX27 PDZ (green), and retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27. All ITC graphs represent the integrated and normalized data fit with a 1-to-1 binding ratio. The binding affinity ( K d ) is given as means of at least two independent experiments. ( H ) Liposome binding assay of retromer with membrane-associated SNX3-cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CI-MPR 2347–2376 peptide (schematic diagram on top). “S” and “P” indicate unbound supernatant and bound pellet, respectively. Control experiments are shown in fig. S7 (B and C). ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on retromer engagement with known regulatory, adaptor, and bacterial effector proteins.
    Di C16 Ptdins 3 P, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 1 article reviews
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    1) Product Images from "De novo macrocyclic peptides for inhibiting, stabilizing, and probing the function of the retromer endosomal trafficking complex"

    Article Title: De novo macrocyclic peptides for inhibiting, stabilizing, and probing the function of the retromer endosomal trafficking complex

    Journal: Science Advances

    doi: 10.1126/sciadv.abg4007

    ( A ) Interactions of retromer with TBC1D5, SNX3, SNX27, and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for retromer, while GST-tagged retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550–568 present), ( D ) SNX27 PDZ , and ( E ) GST-Fam21 R19-R21 with retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS–polyacrylamide gel electrophoresis (PAGE) and Western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586–593 cargo peptide  with SNX27 PDZ alone (yellow), retromer + RT-L4 (red), retromer + SNX27 PDZ (green), and retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27. All ITC graphs represent the integrated and normalized data fit with a 1-to-1 binding ratio. The binding affinity ( K d ) is given as means of at least two independent experiments. ( H ) Liposome binding assay of retromer with membrane-associated SNX3-cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CI-MPR 2347–2376 peptide (schematic diagram on top). “S” and “P” indicate unbound supernatant and bound pellet, respectively. Control experiments are shown in fig. S7 (B and C). ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on retromer engagement with known regulatory, adaptor, and bacterial effector proteins.
    Figure Legend Snippet: ( A ) Interactions of retromer with TBC1D5, SNX3, SNX27, and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for retromer, while GST-tagged retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550–568 present), ( D ) SNX27 PDZ , and ( E ) GST-Fam21 R19-R21 with retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS–polyacrylamide gel electrophoresis (PAGE) and Western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586–593 cargo peptide with SNX27 PDZ alone (yellow), retromer + RT-L4 (red), retromer + SNX27 PDZ (green), and retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27. All ITC graphs represent the integrated and normalized data fit with a 1-to-1 binding ratio. The binding affinity ( K d ) is given as means of at least two independent experiments. ( H ) Liposome binding assay of retromer with membrane-associated SNX3-cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CI-MPR 2347–2376 peptide (schematic diagram on top). “S” and “P” indicate unbound supernatant and bound pellet, respectively. Control experiments are shown in fig. S7 (B and C). ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on retromer engagement with known regulatory, adaptor, and bacterial effector proteins.

    Techniques Used: Incubation, Polyacrylamide Gel Electrophoresis, Western Blot, Binding Assay

    di c16 ptdins 3 p  (Echelon Biosciences)


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    Echelon Biosciences di c16 ptdins 3 p
    ( A ) Interactions of Retromer with TBC1D5, SNX3, SNX27 and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for Retromer, while GST-tagged Retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550-568 present), ( D ) SNX27, and ( E ) GST-Fam21 R19-R21 with Retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS-PAGE and western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586-593 cargo peptide  with SNX27 PDZ alone (yellow), Retromer + RT-L4 (red), Retromer + SNX27 PDZ (green) and Retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of Retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27 All ITC graphs represent the integrated and normalized data fit with a 1 to 1 binding ratio. The binding affinity (K d ) is given as mean of at least two independent experiments. ( H ) Liposome-binding assay of Retromer with membrane-associated SNX3 cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids, or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CIMPR 2347-2376 peptide (schematic diagram on top). “S” and “P” indicates unbound supernatant and bound pellet respectively. Control experiments are shown in  and S7C . ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on Retromer engagement with known regulatory and adaptor proteins.
    Di C16 Ptdins 3 P, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "De novo macrocyclic peptides for inhibiting, stabilising and probing the function of the Retromer endosomal trafficking complex"

    Article Title: De novo macrocyclic peptides for inhibiting, stabilising and probing the function of the Retromer endosomal trafficking complex

    Journal: bioRxiv

    doi: 10.1101/2020.12.03.410779

    ( A ) Interactions of Retromer with TBC1D5, SNX3, SNX27 and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for Retromer, while GST-tagged Retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550-568 present), ( D ) SNX27, and ( E ) GST-Fam21 R19-R21 with Retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS-PAGE and western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586-593 cargo peptide  with SNX27 PDZ alone (yellow), Retromer + RT-L4 (red), Retromer + SNX27 PDZ (green) and Retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of Retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27 All ITC graphs represent the integrated and normalized data fit with a 1 to 1 binding ratio. The binding affinity (K d ) is given as mean of at least two independent experiments. ( H ) Liposome-binding assay of Retromer with membrane-associated SNX3 cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids, or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CIMPR 2347-2376 peptide (schematic diagram on top). “S” and “P” indicates unbound supernatant and bound pellet respectively. Control experiments are shown in  and S7C . ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on Retromer engagement with known regulatory and adaptor proteins.
    Figure Legend Snippet: ( A ) Interactions of Retromer with TBC1D5, SNX3, SNX27 and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for Retromer, while GST-tagged Retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550-568 present), ( D ) SNX27, and ( E ) GST-Fam21 R19-R21 with Retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS-PAGE and western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586-593 cargo peptide with SNX27 PDZ alone (yellow), Retromer + RT-L4 (red), Retromer + SNX27 PDZ (green) and Retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of Retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27 All ITC graphs represent the integrated and normalized data fit with a 1 to 1 binding ratio. The binding affinity (K d ) is given as mean of at least two independent experiments. ( H ) Liposome-binding assay of Retromer with membrane-associated SNX3 cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids, or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CIMPR 2347-2376 peptide (schematic diagram on top). “S” and “P” indicates unbound supernatant and bound pellet respectively. Control experiments are shown in and S7C . ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on Retromer engagement with known regulatory and adaptor proteins.

    Techniques Used: Incubation, SDS Page, Western Blot, Binding Assay

    ( A ) ITC measurements of RT-L4 with Retromer, SNX27 PDZ , TBC1D5 TBC and SNX3 demonstrate the binding specificity of the cyclic peptide to Retromer. ( B ) Liposome-binding assay of SNX3 and Retromer using Folch I liposomes containing 10% PtdIns(3) P and 10% N-terminal palmitoylated CIMPR 2347-2376 peptide. ( C ) Liposome-binding assay of Retromer and SNX3 mixture as in ( B ) except Folch I liposomes contain only 10% PtdIns(3) P without the CI-MPR cargo. Retromer binds only weakly to Folch liposomes in the absence of either SNX3 or cargo sequence. In all three SDS-PAGE gels, “S” indicates unbound supernatant and “P” indicates bound pellet after ultracentrifugation. ( D ) ITC measurement of SNX3 with Vps26A –Vps35 1-390 subcomplex in the presence of CIMPR 2347-2376 cargo peptide. The graph represents the integrated and normalized data fit with a 1 to 1 binding ratio. The binding affinity (K d ) is given as mean of at two three independent experiments. ( E ) Sequence alignment of the C-terminal region of Vps26 and ( F ) the N-terminal region of Vps35 showing the similarity between species. Key residues involve in contacts with Vps35 (yellow arrow) and Vps26 (blue dots) are labelled on top of the sequence. h, Homo sapiens ; zf, Danio rerio ; Ct, Chaetomium thermophilum ; m, Mus musculus .
    Figure Legend Snippet: ( A ) ITC measurements of RT-L4 with Retromer, SNX27 PDZ , TBC1D5 TBC and SNX3 demonstrate the binding specificity of the cyclic peptide to Retromer. ( B ) Liposome-binding assay of SNX3 and Retromer using Folch I liposomes containing 10% PtdIns(3) P and 10% N-terminal palmitoylated CIMPR 2347-2376 peptide. ( C ) Liposome-binding assay of Retromer and SNX3 mixture as in ( B ) except Folch I liposomes contain only 10% PtdIns(3) P without the CI-MPR cargo. Retromer binds only weakly to Folch liposomes in the absence of either SNX3 or cargo sequence. In all three SDS-PAGE gels, “S” indicates unbound supernatant and “P” indicates bound pellet after ultracentrifugation. ( D ) ITC measurement of SNX3 with Vps26A –Vps35 1-390 subcomplex in the presence of CIMPR 2347-2376 cargo peptide. The graph represents the integrated and normalized data fit with a 1 to 1 binding ratio. The binding affinity (K d ) is given as mean of at two three independent experiments. ( E ) Sequence alignment of the C-terminal region of Vps26 and ( F ) the N-terminal region of Vps35 showing the similarity between species. Key residues involve in contacts with Vps35 (yellow arrow) and Vps26 (blue dots) are labelled on top of the sequence. h, Homo sapiens ; zf, Danio rerio ; Ct, Chaetomium thermophilum ; m, Mus musculus .

    Techniques Used: Binding Assay, Sequencing, SDS Page

    long chain di c16 ptdins 3 4 5 p3  (Echelon Biosciences)


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    Long Chain Di C16 Ptdins 3 4 5 P3, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Echelon Biosciences di c16 ptdins 3 p
    ( A ) Interactions of retromer with TBC1D5, SNX3, SNX27, and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for retromer, while GST-tagged retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550–568 present), ( D ) SNX27 PDZ , and ( E ) GST-Fam21 R19-R21 with retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS–polyacrylamide gel electrophoresis (PAGE) and Western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586–593 cargo peptide  with SNX27 PDZ alone (yellow), retromer + RT-L4 (red), retromer + SNX27 PDZ (green), and retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27. All ITC graphs represent the integrated and normalized data fit with a 1-to-1 binding ratio. The binding affinity ( K d ) is given as means of at least two independent experiments. ( H ) Liposome binding assay of retromer with membrane-associated SNX3-cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CI-MPR 2347–2376 peptide (schematic diagram on top). “S” and “P” indicate unbound supernatant and bound pellet, respectively. Control experiments are shown in fig. S7 (B and C). ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on retromer engagement with known regulatory, adaptor, and bacterial effector proteins.
    Di C16 Ptdins 3 P, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Echelon Biosciences long chain di c16 ptdins 3 4 5 p3
    ( A ) Interactions of retromer with TBC1D5, SNX3, SNX27, and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for retromer, while GST-tagged retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550–568 present), ( D ) SNX27 PDZ , and ( E ) GST-Fam21 R19-R21 with retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS–polyacrylamide gel electrophoresis (PAGE) and Western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586–593 cargo peptide  with SNX27 PDZ alone (yellow), retromer + RT-L4 (red), retromer + SNX27 PDZ (green), and retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27. All ITC graphs represent the integrated and normalized data fit with a 1-to-1 binding ratio. The binding affinity ( K d ) is given as means of at least two independent experiments. ( H ) Liposome binding assay of retromer with membrane-associated SNX3-cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CI-MPR 2347–2376 peptide (schematic diagram on top). “S” and “P” indicate unbound supernatant and bound pellet, respectively. Control experiments are shown in fig. S7 (B and C). ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on retromer engagement with known regulatory, adaptor, and bacterial effector proteins.
    Long Chain Di C16 Ptdins 3 4 5 P3, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ( A ) Interactions of retromer with TBC1D5, SNX3, SNX27, and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for retromer, while GST-tagged retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550–568 present), ( D ) SNX27 PDZ , and ( E ) GST-Fam21 R19-R21 with retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS–polyacrylamide gel electrophoresis (PAGE) and Western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586–593 cargo peptide  with SNX27 PDZ alone (yellow), retromer + RT-L4 (red), retromer + SNX27 PDZ (green), and retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27. All ITC graphs represent the integrated and normalized data fit with a 1-to-1 binding ratio. The binding affinity ( K d ) is given as means of at least two independent experiments. ( H ) Liposome binding assay of retromer with membrane-associated SNX3-cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CI-MPR 2347–2376 peptide (schematic diagram on top). “S” and “P” indicate unbound supernatant and bound pellet, respectively. Control experiments are shown in fig. S7 (B and C). ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on retromer engagement with known regulatory, adaptor, and bacterial effector proteins.

    Journal: Science Advances

    Article Title: De novo macrocyclic peptides for inhibiting, stabilizing, and probing the function of the retromer endosomal trafficking complex

    doi: 10.1126/sciadv.abg4007

    Figure Lengend Snippet: ( A ) Interactions of retromer with TBC1D5, SNX3, SNX27, and Fam21 in the presence of either RT-D3 or RT-L4. GST-TBC1D5 TBC and GST-Fam21 R19-R21 were used as baits for retromer, while GST-tagged retromer (Vps29 subunit) was used as bait for SNX3 and SNX27. ( B ) ITC measurement of TBC1D5 TBC , ( C ) SNX3 (with DMT1-II 550–568 present), ( D ) SNX27 PDZ , and ( E ) GST-Fam21 R19-R21 with retromer in the presence or absence of RT-D3 or RT-L4. ( F ) Hela cell lysates were incubated with streptavidin agarose coated with biotinylated RT-D3 or RT-L4 and bound proteins subjected to SDS–polyacrylamide gel electrophoresis (PAGE) and Western blotting with antibodies against indicated proteins. ( G ) ITC measurement of PTHR 586–593 cargo peptide with SNX27 PDZ alone (yellow), retromer + RT-L4 (red), retromer + SNX27 PDZ (green), and retromer + SNX27 PDZ + RT-L4 (blue). RT-L4 allosterically enhances the affinity of retromer + SNX27 PDZ for cargo. The cargo peptide binds to SNX27. All ITC graphs represent the integrated and normalized data fit with a 1-to-1 binding ratio. The binding affinity ( K d ) is given as means of at least two independent experiments. ( H ) Liposome binding assay of retromer with membrane-associated SNX3-cargo complex in the presence of cyclic peptides. Multilamellar vesicles were composed of either control PC/PE lipids or Folch I lipids containing added PtdIns(3) P and N-terminal palmitoylated CI-MPR 2347–2376 peptide (schematic diagram on top). “S” and “P” indicate unbound supernatant and bound pellet, respectively. Control experiments are shown in fig. S7 (B and C). ( I ) Schematic summarizing the effects of RT-D3 and RT-L4 on retromer engagement with known regulatory, adaptor, and bacterial effector proteins.

    Article Snippet: Briefly, cargo-loaded Folch liposomes were made by mixing 25 μl of N-terminal palmitoylated CI-MPR 2347–2376 peptide (4 mg/ml), 50 μl of Folch fraction I (Sigma-Aldrich) (10 mg/ml), and 50 μl of di-C16 PtdIns(3) P (1 mg/ml) (Echelon Biosciences), each freshly prepared in chloroform, to a total volume of 500 μl of chloroform.

    Techniques: Incubation, Polyacrylamide Gel Electrophoresis, Western Blot, Binding Assay