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custom vectors for bacterial expression of ppib and tacypa  (GenScript corporation)

 
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    Structured Review

    GenScript corporation custom vectors for bacterial expression of ppib and tacypa
    a) Sequence alignment of LRT2 with cyclophilins from <t>wheat</t> <t>(TaCypA),</t> human (CypA) and E. coli <t>(PPIB).</t> b) The LRT2 homology model (green) aligned with the crystal structure of human Cyclophilin A (cyan, PDB:1awr.1) shows the conserved catalytic residues H61, R62, Q118, F120, W128 and H133 (LRT2 numbering). c) Residues in the loop preceding W121 in hCypA that are not conserved in LRT2. d) Corresponding residues in the loop preceding W128 in the LRT2 homology model
    Custom Vectors For Bacterial Expression Of Ppib And Tacypa, supplied by GenScript corporation, 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/result/custom vectors for bacterial expression of ppib and tacypa/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    custom vectors for bacterial expression of ppib and tacypa - by Bioz Stars, 2026-06
    90/100 stars

    Images

    1) Product Images from "Tuning a timing device that regulates lateral root development in rice"

    Article Title: Tuning a timing device that regulates lateral root development in rice

    Journal: Journal of biomolecular NMR

    doi: 10.1007/s10858-019-00258-0

    a) Sequence alignment of LRT2 with cyclophilins from wheat (TaCypA), human (CypA) and E. coli (PPIB). b) The LRT2 homology model (green) aligned with the crystal structure of human Cyclophilin A (cyan, PDB:1awr.1) shows the conserved catalytic residues H61, R62, Q118, F120, W128 and H133 (LRT2 numbering). c) Residues in the loop preceding W121 in hCypA that are not conserved in LRT2. d) Corresponding residues in the loop preceding W128 in the LRT2 homology model
    Figure Legend Snippet: a) Sequence alignment of LRT2 with cyclophilins from wheat (TaCypA), human (CypA) and E. coli (PPIB). b) The LRT2 homology model (green) aligned with the crystal structure of human Cyclophilin A (cyan, PDB:1awr.1) shows the conserved catalytic residues H61, R62, Q118, F120, W128 and H133 (LRT2 numbering). c) Residues in the loop preceding W121 in hCypA that are not conserved in LRT2. d) Corresponding residues in the loop preceding W128 in the LRT2 homology model

    Techniques Used: Sequencing

    Isomerization rates for LRT2 mutants and homologs determined by 1 H- 1 H ROESY and 1 H- 15 N ZZ exchange experiments.
    Figure Legend Snippet: Isomerization rates for LRT2 mutants and homologs determined by 1 H- 1 H ROESY and 1 H- 15 N ZZ exchange experiments.

    Techniques Used:

    (a-c) Expanded region of the 1H-15N NZZ exchange NMR spectrum (mixing time = 0.55s) of 15N-OsIAA1172−125 in the presence of hCypA (a) or PPIB from E. coli (b), and of the ROESY spectrum (70 ms) of OsIAA1198−109 in the presence of TaCypA (c). Exchange peaks between the 104W-NHεcis and 104W-NHεtrans auto peaks are observed in the presence of each homolog. (d-f) Fitting (lines) of normalized peak intensities for the auto (Itt and Icc) and exchange (Itc and Ict) peaks in the presence of hCypA (d), PPIB (e) and TaCypA (f) yielded the corresponding kexobs values (Table 2)
    Figure Legend Snippet: (a-c) Expanded region of the 1H-15N NZZ exchange NMR spectrum (mixing time = 0.55s) of 15N-OsIAA1172−125 in the presence of hCypA (a) or PPIB from E. coli (b), and of the ROESY spectrum (70 ms) of OsIAA1198−109 in the presence of TaCypA (c). Exchange peaks between the 104W-NHεcis and 104W-NHεtrans auto peaks are observed in the presence of each homolog. (d-f) Fitting (lines) of normalized peak intensities for the auto (Itt and Icc) and exchange (Itc and Ict) peaks in the presence of hCypA (d), PPIB (e) and TaCypA (f) yielded the corresponding kexobs values (Table 2)

    Techniques Used:



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    custom vectors for bacterial expression of ppib and tacypa  (GenScript corporation)
    90
    GenScript corporation custom vectors for bacterial expression of ppib and tacypa
    a) Sequence alignment of LRT2 with cyclophilins from <t>wheat</t> <t>(TaCypA),</t> human (CypA) and E. coli <t>(PPIB).</t> b) The LRT2 homology model (green) aligned with the crystal structure of human Cyclophilin A (cyan, PDB:1awr.1) shows the conserved catalytic residues H61, R62, Q118, F120, W128 and H133 (LRT2 numbering). c) Residues in the loop preceding W121 in hCypA that are not conserved in LRT2. d) Corresponding residues in the loop preceding W128 in the LRT2 homology model
    Custom Vectors For Bacterial Expression Of Ppib And Tacypa, supplied by GenScript corporation, 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/result/custom vectors for bacterial expression of ppib and tacypa/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    custom vectors for bacterial expression of ppib and tacypa - by Bioz Stars, 2026-06
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    a) Sequence alignment of LRT2 with cyclophilins from wheat (TaCypA), human (CypA) and E. coli (PPIB). b) The LRT2 homology model (green) aligned with the crystal structure of human Cyclophilin A (cyan, PDB:1awr.1) shows the conserved catalytic residues H61, R62, Q118, F120, W128 and H133 (LRT2 numbering). c) Residues in the loop preceding W121 in hCypA that are not conserved in LRT2. d) Corresponding residues in the loop preceding W128 in the LRT2 homology model

    Journal: Journal of biomolecular NMR

    Article Title: Tuning a timing device that regulates lateral root development in rice

    doi: 10.1007/s10858-019-00258-0

    Figure Lengend Snippet: a) Sequence alignment of LRT2 with cyclophilins from wheat (TaCypA), human (CypA) and E. coli (PPIB). b) The LRT2 homology model (green) aligned with the crystal structure of human Cyclophilin A (cyan, PDB:1awr.1) shows the conserved catalytic residues H61, R62, Q118, F120, W128 and H133 (LRT2 numbering). c) Residues in the loop preceding W121 in hCypA that are not conserved in LRT2. d) Corresponding residues in the loop preceding W128 in the LRT2 homology model

    Article Snippet: Custom vectors for bacterial expression of PPIB (Uniprot entry {"type":"entrez-protein","attrs":{"text":"P23869","term_id":"2507227","term_text":"P23869"}} P23869 ) and TaCypA (Uniprot entry {"type":"entrez-protein","attrs":{"text":"Q93W25","term_id":"75305737","term_text":"Q93W25"}} Q93W25 ) were purchased from GenScript (Piscataway, NJ).

    Techniques: Sequencing

    Isomerization rates for LRT2 mutants and homologs determined by 1 H- 1 H ROESY and 1 H- 15 N ZZ exchange experiments.

    Journal: Journal of biomolecular NMR

    Article Title: Tuning a timing device that regulates lateral root development in rice

    doi: 10.1007/s10858-019-00258-0

    Figure Lengend Snippet: Isomerization rates for LRT2 mutants and homologs determined by 1 H- 1 H ROESY and 1 H- 15 N ZZ exchange experiments.

    Article Snippet: Custom vectors for bacterial expression of PPIB (Uniprot entry {"type":"entrez-protein","attrs":{"text":"P23869","term_id":"2507227","term_text":"P23869"}} P23869 ) and TaCypA (Uniprot entry {"type":"entrez-protein","attrs":{"text":"Q93W25","term_id":"75305737","term_text":"Q93W25"}} Q93W25 ) were purchased from GenScript (Piscataway, NJ).

    Techniques:

    (a-c) Expanded region of the 1H-15N NZZ exchange NMR spectrum (mixing time = 0.55s) of 15N-OsIAA1172−125 in the presence of hCypA (a) or PPIB from E. coli (b), and of the ROESY spectrum (70 ms) of OsIAA1198−109 in the presence of TaCypA (c). Exchange peaks between the 104W-NHεcis and 104W-NHεtrans auto peaks are observed in the presence of each homolog. (d-f) Fitting (lines) of normalized peak intensities for the auto (Itt and Icc) and exchange (Itc and Ict) peaks in the presence of hCypA (d), PPIB (e) and TaCypA (f) yielded the corresponding kexobs values (Table 2)

    Journal: Journal of biomolecular NMR

    Article Title: Tuning a timing device that regulates lateral root development in rice

    doi: 10.1007/s10858-019-00258-0

    Figure Lengend Snippet: (a-c) Expanded region of the 1H-15N NZZ exchange NMR spectrum (mixing time = 0.55s) of 15N-OsIAA1172−125 in the presence of hCypA (a) or PPIB from E. coli (b), and of the ROESY spectrum (70 ms) of OsIAA1198−109 in the presence of TaCypA (c). Exchange peaks between the 104W-NHεcis and 104W-NHεtrans auto peaks are observed in the presence of each homolog. (d-f) Fitting (lines) of normalized peak intensities for the auto (Itt and Icc) and exchange (Itc and Ict) peaks in the presence of hCypA (d), PPIB (e) and TaCypA (f) yielded the corresponding kexobs values (Table 2)

    Article Snippet: Custom vectors for bacterial expression of PPIB (Uniprot entry {"type":"entrez-protein","attrs":{"text":"P23869","term_id":"2507227","term_text":"P23869"}} P23869 ) and TaCypA (Uniprot entry {"type":"entrez-protein","attrs":{"text":"Q93W25","term_id":"75305737","term_text":"Q93W25"}} Q93W25 ) were purchased from GenScript (Piscataway, NJ).

    Techniques: