Review



di c16 ptdins 3 p  (Echelon Biosciences)


Bioz Verified Symbol Echelon Biosciences is a verified supplier
Bioz Manufacturer Symbol Echelon Biosciences manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    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: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/di c16 ptdins 3 p/product/Echelon Biosciences
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    di c16 ptdins 3 p - by Bioz Stars, 2025-01
    94/100 stars

    Images

    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



    Similar Products

    94
    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: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/di c16 ptdins 3 p/product/Echelon Biosciences
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    di c16 ptdins 3 p - by Bioz Stars, 2025-01
    94/100 stars
      Buy from Supplier

    94
    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: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/long chain di c16 ptdins 3 4 5 p3/product/Echelon Biosciences
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    long chain di c16 ptdins 3 4 5 p3 - by Bioz Stars, 2025-01
    94/100 stars
      Buy from Supplier

    Image Search Results


    ( 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