pgex-2t Search Results


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  • 95
    GE Healthcare pgex 2t
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 95/100, based on 2196 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t/product/GE Healthcare
    Average 95 stars, based on 2196 article reviews
    Price from $9.99 to $1999.99
    pgex 2t - by Bioz Stars, 2020-04
    95/100 stars
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    92
    Promega pgex 2t
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Pgex 2t, supplied by Promega, used in various techniques. Bioz Stars score: 92/100, based on 64 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t/product/Promega
    Average 92 stars, based on 64 article reviews
    Price from $9.99 to $1999.99
    pgex 2t - by Bioz Stars, 2020-04
    92/100 stars
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    90
    Addgene inc pgex 2t
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Pgex 2t, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t/product/Addgene inc
    Average 90 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    pgex 2t - by Bioz Stars, 2020-04
    90/100 stars
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    83
    GE Healthcare pgex 2t 1
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Pgex 2t 1, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 83/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 83 stars, based on 20 article reviews
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    pgex 2t 1 - by Bioz Stars, 2020-04
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    91
    Addgene inc pgex 2t rhoa
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Pgex 2t Rhoa, supplied by Addgene inc, used in various techniques. Bioz Stars score: 91/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pgex 2t rhoa - by Bioz Stars, 2020-04
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    81
    GE Healthcare pgex 2t system
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Pgex 2t System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 81/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t system/product/GE Healthcare
    Average 81 stars, based on 11 article reviews
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    pgex 2t system - by Bioz Stars, 2020-04
    81/100 stars
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    81
    GE Healthcare pgex 2t 4t
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Pgex 2t 4t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 81/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 81 stars, based on 10 article reviews
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    pgex 2t 4t - by Bioz Stars, 2020-04
    81/100 stars
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    80
    GE Healthcare template pgex 2t
    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the <t>pGEX-2T</t> vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.
    Template Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 80/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 80 stars, based on 6 article reviews
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    template pgex 2t - by Bioz Stars, 2020-04
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    93
    GE Healthcare vector pgex 2t
    (A) Schematic representation of various truncated p53 constructs and TIP30. p53 constructs were fused in frame to the 3′ end of the GST gene in the <t>pGEX-2T</t> vector. His-tagged constructs of TIP30 and p53 DBD or CTD were fused in frame at the 3′
    Vector Pgex 2t, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 433 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 433 article reviews
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    vector pgex 2t - by Bioz Stars, 2020-04
    93/100 stars
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    85
    Stratagene pgex 2t
    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
    Pgex 2t, supplied by Stratagene, used in various techniques. Bioz Stars score: 85/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t/product/Stratagene
    Average 85 stars, based on 42 article reviews
    Price from $9.99 to $1999.99
    pgex 2t - by Bioz Stars, 2020-04
    85/100 stars
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    84
    Promega pgex 2t vector
    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
    Pgex 2t Vector, supplied by Promega, used in various techniques. Bioz Stars score: 84/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t vector/product/Promega
    Average 84 stars, based on 53 article reviews
    Price from $9.99 to $1999.99
    pgex 2t vector - by Bioz Stars, 2020-04
    84/100 stars
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    85
    Stratagene pgex 2t vector
    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
    Pgex 2t Vector, supplied by Stratagene, used in various techniques. Bioz Stars score: 85/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t vector/product/Stratagene
    Average 85 stars, based on 36 article reviews
    Price from $9.99 to $1999.99
    pgex 2t vector - by Bioz Stars, 2020-04
    85/100 stars
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    91
    TaKaRa pgex 2t vector
    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
    Pgex 2t Vector, supplied by TaKaRa, used in various techniques. Bioz Stars score: 91/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t vector/product/TaKaRa
    Average 91 stars, based on 29 article reviews
    Price from $9.99 to $1999.99
    pgex 2t vector - by Bioz Stars, 2020-04
    91/100 stars
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    97
    GE Healthcare pgex 2t plin2
    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
    Pgex 2t Plin2, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 97/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t plin2/product/GE Healthcare
    Average 97 stars, based on 22 article reviews
    Price from $9.99 to $1999.99
    pgex 2t plin2 - by Bioz Stars, 2020-04
    97/100 stars
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    75
    Addgene inc pgex 2t ptp1b
    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
    Pgex 2t Ptp1b, supplied by Addgene inc, used in various techniques. Bioz Stars score: 75/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t ptp1b/product/Addgene inc
    Average 75 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pgex 2t ptp1b - by Bioz Stars, 2020-04
    75/100 stars
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    93
    TaKaRa pgex 2t
    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
    Pgex 2t, supplied by TaKaRa, used in various techniques. Bioz Stars score: 93/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t/product/TaKaRa
    Average 93 stars, based on 22 article reviews
    Price from $9.99 to $1999.99
    pgex 2t - by Bioz Stars, 2020-04
    93/100 stars
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    94
    Millipore plasmid pgex 2t
    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
    Plasmid Pgex 2t, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 23 article reviews
    Price from $9.99 to $1999.99
    plasmid pgex 2t - by Bioz Stars, 2020-04
    94/100 stars
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    92
    Thermo Fisher pgex 2t vector
    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
    Pgex 2t Vector, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 55 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgex 2t vector/product/Thermo Fisher
    Average 92 stars, based on 55 article reviews
    Price from $9.99 to $1999.99
    pgex 2t vector - by Bioz Stars, 2020-04
    92/100 stars
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    93
    Addgene inc pgex 2t gst cdc42wt
    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
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    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
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    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into <t>pGEX-2T</t> and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector <t>pGEX-2T.</t> b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences
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    Image Search Results


    Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the pGEX-2T vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.

    Journal: Biochemical Journal

    Article Title: Characterization of a sterol carrier protein 2/3-oxoacyl-CoA thiolase from the cotton leafworm (Spodoptera littoralis): a lepidopteran mechanism closer to that in mammals than that in dipterans

    doi: 10.1042/BJ20040717

    Figure Lengend Snippet: Western-blot analysis of the SCP2 domain Left panel: proteins from various tissues within the last larval instar were used. Lane 1, midgut; lane 2, fat body; lane 3, Malpighian tubules; lane 4, recombinant protein corresponding to the SCP2 domain of SCPx. The antibody against the SCP2 domain of S. littoralis SCPx protein was used. Right panel: Western-blot analysis of the recombinant S. littoralis SCPx protein using anti-(SCP2 domain) antibody. Lane 1, proteins from E. coli carrying the pGEX-2T vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression.

    Article Snippet: The product was cut out with Bam HI and Eco RI from the plasmid and transferred into pGEX-2T (Amersham Biosciences).

    Techniques: Western Blot, Recombinant, Plasmid Preparation, Expressing

    The developmental profile of SCPx during the sixth instar ( A ) A 10 #x3BC;g portion of total RNA from midgut at various time points within the sixth larval instar, as indicated, was used. The blot was hybridized with a 32 P-labelled SCPx cDNA probe corresponding to the open reading frame. The same blot was stripped and reprobed with 18S rRNA probe. G, W and PP refer to the stages ‘gut purge’, ‘wandering’and ‘prepupa’ respectively that occur before pupation. ( B ) Western-blot analysis of SCPx protein. Top panel: 100 #x3BC;g of protein from midgut at various time points within the sixth larval instar, as indicated, was used. Bottom panel: Western-blot analysis of the recombinant S. littoralis SCPx protein. Lane 1, proteins from E. coli carrying the pGEX-2T vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing the SCPx cDNA without induction of expression; lane 3, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression; lane 4, whole extract from C. elegans . The antibody against C. elegans P-44 was used to detect the SCPx protein.

    Journal: Biochemical Journal

    Article Title: Characterization of a sterol carrier protein 2/3-oxoacyl-CoA thiolase from the cotton leafworm (Spodoptera littoralis): a lepidopteran mechanism closer to that in mammals than that in dipterans

    doi: 10.1042/BJ20040717

    Figure Lengend Snippet: The developmental profile of SCPx during the sixth instar ( A ) A 10 #x3BC;g portion of total RNA from midgut at various time points within the sixth larval instar, as indicated, was used. The blot was hybridized with a 32 P-labelled SCPx cDNA probe corresponding to the open reading frame. The same blot was stripped and reprobed with 18S rRNA probe. G, W and PP refer to the stages ‘gut purge’, ‘wandering’and ‘prepupa’ respectively that occur before pupation. ( B ) Western-blot analysis of SCPx protein. Top panel: 100 #x3BC;g of protein from midgut at various time points within the sixth larval instar, as indicated, was used. Bottom panel: Western-blot analysis of the recombinant S. littoralis SCPx protein. Lane 1, proteins from E. coli carrying the pGEX-2T vector without the SCPx cDNA; lane 2, proteins from E. coli carrying the pGEX-2T vector containing the SCPx cDNA without induction of expression; lane 3, proteins from E. coli carrying the pGEX-2T vector containing SCPx cDNA with induction of expression; lane 4, whole extract from C. elegans . The antibody against C. elegans P-44 was used to detect the SCPx protein.

    Article Snippet: The product was cut out with Bam HI and Eco RI from the plasmid and transferred into pGEX-2T (Amersham Biosciences).

    Techniques: Western Blot, Recombinant, Plasmid Preparation, Expressing

    (A) Schematic representation of various truncated p53 constructs and TIP30. p53 constructs were fused in frame to the 3′ end of the GST gene in the pGEX-2T vector. His-tagged constructs of TIP30 and p53 DBD or CTD were fused in frame at the 3′

    Journal: Molecules and Cells

    Article Title: TIP30 Directly Binds p53 Tumor Suppressor Protein In Vitro

    doi: 10.1007/s10059-012-0232-x

    Figure Lengend Snippet: (A) Schematic representation of various truncated p53 constructs and TIP30. p53 constructs were fused in frame to the 3′ end of the GST gene in the pGEX-2T vector. His-tagged constructs of TIP30 and p53 DBD or CTD were fused in frame at the 3′

    Article Snippet: GST-tagged p53 constructs for use in GST pull-down assays were prepared by digesting PCR products with Bam HI and Eco RI and inserting into the corresponding sites in the pGEX-2T vector (GE Healthcare).

    Techniques: Construct, Plasmid Preparation

    The protein and response element constructs used in crystallization and their contacts. Sequences and interactions (legend is provided within the figure) are shown for UspDBD ( A ) and EcRDBD ( B ), respectively. The numbering of the amino acid residues is relative to the first conserved cysteine, with the authentic numbers ( 7 , 10 ) appearing in parentheses The sequences defined previously ( 16 ) as corresponding to T-box ( 42 ) and A-box ( 33 , 34 ) are highlighted in green and red, respectively. In gray boxes the N- and C-terminal residues not visible in the electron density maps are listed. Cloning artifacts from the pGEX-2T plasmid are indicated by lower case letters. The α-helices are boxed and the residues from β-sheets are circled following the definition of DSSP ( 43 ). ( C ) The hsp27pal -based DNA used in cocrystallization. The symbols are as in ( A ) and ( B ).

    Journal: Nucleic Acids Research

    Article Title: Novel DNA-binding element within the C-terminal extension of the nuclear receptor DNA-binding domain

    doi: 10.1093/nar/gkm162

    Figure Lengend Snippet: The protein and response element constructs used in crystallization and their contacts. Sequences and interactions (legend is provided within the figure) are shown for UspDBD ( A ) and EcRDBD ( B ), respectively. The numbering of the amino acid residues is relative to the first conserved cysteine, with the authentic numbers ( 7 , 10 ) appearing in parentheses The sequences defined previously ( 16 ) as corresponding to T-box ( 42 ) and A-box ( 33 , 34 ) are highlighted in green and red, respectively. In gray boxes the N- and C-terminal residues not visible in the electron density maps are listed. Cloning artifacts from the pGEX-2T plasmid are indicated by lower case letters. The α-helices are boxed and the residues from β-sheets are circled following the definition of DSSP ( 43 ). ( C ) The hsp27pal -based DNA used in cocrystallization. The symbols are as in ( A ) and ( B ).

    Article Snippet: Construction of expression vectors, site-directed mutagenesis, overexpression and purification of the wild-type and mutant proteins The plasmid pGEX-2T (Amersham Biosciences, Freiburg, Germany) containing the lac Iq gene was used for the expression of DBDs as fusion proteins with Schistosoma japonicum glutathione-S-transferase (GST) in Escherichia coli strain BL21(DE3)pLysS (Novagen, Germany).

    Techniques: Construct, Crystallization Assay, Clone Assay, Plasmid Preparation

    PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into pGEX-2T and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.

    Journal: Cell

    Article Title: RAS and RHO Families of GTPases Directly Regulate Distinct Phosphoinositide 3-Kinase Isoforms

    doi: 10.1016/j.cell.2013.04.031

    Figure Lengend Snippet: PI 3-Kinase p110β Is Unable to Interact with RAS, Related to Figure 1 (A) Active RAS proteins fail to stimulate p110β in cells. Constitutively active mutants of HRAS, KRAS and NRAS were expressed in COS7 cells along with empty vector, p110α/p85 or p110β/p85. Cells were serum-starved and protein lysates were made for western blot analysis. (B) p110β-RBD-DM is functionally compromised in intact cells. Wild-type p110β or p110β-RBD-DM were expressed at low levels in COS7 cells, along with p85. Cells were serum-starved and protein lysates were made for western blot analysis. Gβγ, coexpression of Gβ 2 and Gγ 1 ; Myr, myristoylated p110β. (C) DIRAS1 and DIRAS2 bind p110β in a GTP-dependent manner. cDNAs encoding all 34 murine members of the RAS subfamily of small GTPases (RFGs) were cloned into pGEX-2T and verified by sequencing. GST-tagged RFGs were expressed in E. coli , purified on glutathione agarose, loaded with GDP/GTPγS in vitro and incubated with lysates from transfected COS7 cells, expressing FLAG-p110β/p85. (D) Non-β isoforms bind to RAS proteins and a number of closely related RFGs. GST-tagged RFGs were purified from E. coli lysates and loaded with GDP/GTPγS in vitro. FLAG-tagged p110α, p110γ and p110δ were expressed in COS7 cells along with their respective regulatory subunits p85 or p101. COS7 cell lysates were incubated with GTPases for 1 hr and bound p110 was detected by western blot for FLAG.

    Article Snippet: Protein Purification To produce purified recombinant GTPases on beads, cDNAs in pGEX-2T were transformed into BL21 E. coli (Stratagene).

    Techniques: Plasmid Preparation, Western Blot, Clone Assay, Sequencing, Purification, In Vitro, Incubation, Transfection, Expressing

    Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector pGEX-2T. b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences

    Journal: Inflammation Research

    Article Title: Monoclonal antibodies for human and porcine histamine N-methyltransferase (HMT) facilitate protein expression and localization studies

    doi: 10.1007/s00011-016-0987-1

    Figure Lengend Snippet: Recombinant HMT antigens used for immunizations. a Recombinant human and porcine GST-HMT fusion proteins cloned in the bacterial expression vector pGEX-2T. b 12.5 % Silver-stained polyacrylamide gel of the purified human ( lane 1 ) and porcine ( lane 3 ) GST-HMT fusion proteins used for the immunization of mice and the HMT and GST products resulting from cleavage with thrombin protease ( lanes 2 and 4 ). The sizes of molecular weight markers ( M ) are given on the left in kilodalton. c Sequence alignment and percent sequence identity of the HMT proteins from man, pig, mouse and rat obtained with the NCBI Constrained-based Multiple Alignment Tool ( www.ncbi.nlm.nih.gov/tools/cobalt/cobalt.cgi?link_loc=BlastHomeLink ). Residues identical in all four proteins are shaded black , residues identical in three proteins are shaded gray , and residues that have been shown to interact with histamine and S-adenosylhomocysteine in human HMT [ 7 ] are shaded red (indicated by plus symbol on top) and blue (indicated by hash on top), respectively. Antigenicity plots of human ( d ) and porcine ( e ) HMT produced with the BepiPred Linear Epitope Prediction Tool ( www.tools.immuneepitope.org/bcell ) [ 32 ] show similar predicted B-cell epitopes ( yellow peaks on top of the threshold line with reference to amino acid positions) for both protein sequences

    Article Snippet: Preparation of recombinant HMT proteins Full-length human and porcine HMT cDNAs [ , , ] were amplified by PCR with specific primers from total human and porcine kidney cDNA, respectively, and cloned in frame into the bacterial expression vector pGEX-2T (GE Healthcare, Vienna, Austria).

    Techniques: Recombinant, HMT Assay, Clone Assay, Expressing, Plasmid Preparation, Staining, Purification, Mouse Assay, Molecular Weight, Sequencing, Produced