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  • 93
    Millipore p3x flag cmv
    P3x Flag Cmv, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 91 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore p3x flag cmv 10
    P3x Flag Cmv 10, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore p3x flag cmv 26
    P3x Flag Cmv 26, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore p3x flag cmv 14
    P3x Flag Cmv 14, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore p3x flag cmv 13
    P3x Flag Cmv 13, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Millipore p3x flag cmv 7 1
    P3x Flag Cmv 7 1, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore p3x flag cmv 10 vector
    P3x Flag Cmv 10 Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore expression vector p3x flag cmv 9
    Cleavage of MUC16 is independent of Υ-secretase, neutrophil elastase and MMP-7 and intracellular cues. (a) MUC16 does not undergo Υ-secretase-mediated regulated intra-membrane proteolysis (RIP). Schematic representations of luciferase reporter construct to assess RIP of MUC16-Cter. A GAL4 (DNA-binding domain)-VP16 (Activation domain) fusion was cloned into the C-terminus of the MUC16-Cter <t>(CMV9-FLAG-114</t> amino acid fragment) (top panel). Bottom panel: HEK293T cells were cotransfected with empty CMV9 vector (pCMV9) or with M16-114-GAL4-VP16 (pCMV9-M16-114-GV) or APP-C99-GAL4-VP16 (pSG5-C99-GV, positive control for Υ-secretase cleavage) and a luciferase reporter driven by the GAL4 upstream sequence (pFR-Luc) along with pRenilla-Luc for transfection control in the presence or absence of Υ-secretase inhibitor, Inhibitor X (Inh X). The bars represent the normalized luciferase activity of pFR-Luc to pRenilla-Luc of a representative experiment and is presented as mean ± s.e.m, n = 3. (b) MUC16 cleavage was independent of intracellular cues. Amino acids capable of any kind of post-translational modifications were mutated to Ala in the CMV9-F114HA construct and were transfected into HEK293T cells. Cell lysates were immunoblotted with qanti-HA and FLAG antibodies (left panel). Bars on the right represent the normalized cleaved fraction measured by generating a ratio of normalized (with actin) bottom-HA/total-HA (see cleaved fraction calculation in materials and methods). (c) Expression of ELA2 and MMP-7 in multiple cells lines. Expression of ELA2 and MMP-7 were assessed using reverse transcriptase PCR (RT-PCR). U-937 cells were used as a positive control for ELA2 expression. (d) Skin fibroblasts established from Mmp7 −/− and Mmp2 −/− mice were analyzed for the expression of Mmp2 and Mmp7 using RT-PCR. KCT960 cells were used as a positive control for Mmp7 expression. (e) Skin fibroblasts from Mmp7 −/− and Mmp2 −/− mice were transiently transfected with control (CMV9) and MUC16-Cter (F114HA) plasmids and the cell lysates were immunoblotted with respective antibodies to assess the role of Mmp7 (and therefore MMP7) in the cleavage of MUC16. Mmp2 −/− fibroblasts were used as a control.
    Expression Vector P3x Flag Cmv 9, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore hindiii ecorv digested p3x flag cmv 13
    Cleavage of MUC16 is independent of Υ-secretase, neutrophil elastase and MMP-7 and intracellular cues. (a) MUC16 does not undergo Υ-secretase-mediated regulated intra-membrane proteolysis (RIP). Schematic representations of luciferase reporter construct to assess RIP of MUC16-Cter. A GAL4 (DNA-binding domain)-VP16 (Activation domain) fusion was cloned into the C-terminus of the MUC16-Cter <t>(CMV9-FLAG-114</t> amino acid fragment) (top panel). Bottom panel: HEK293T cells were cotransfected with empty CMV9 vector (pCMV9) or with M16-114-GAL4-VP16 (pCMV9-M16-114-GV) or APP-C99-GAL4-VP16 (pSG5-C99-GV, positive control for Υ-secretase cleavage) and a luciferase reporter driven by the GAL4 upstream sequence (pFR-Luc) along with pRenilla-Luc for transfection control in the presence or absence of Υ-secretase inhibitor, Inhibitor X (Inh X). The bars represent the normalized luciferase activity of pFR-Luc to pRenilla-Luc of a representative experiment and is presented as mean ± s.e.m, n = 3. (b) MUC16 cleavage was independent of intracellular cues. Amino acids capable of any kind of post-translational modifications were mutated to Ala in the CMV9-F114HA construct and were transfected into HEK293T cells. Cell lysates were immunoblotted with qanti-HA and FLAG antibodies (left panel). Bars on the right represent the normalized cleaved fraction measured by generating a ratio of normalized (with actin) bottom-HA/total-HA (see cleaved fraction calculation in materials and methods). (c) Expression of ELA2 and MMP-7 in multiple cells lines. Expression of ELA2 and MMP-7 were assessed using reverse transcriptase PCR (RT-PCR). U-937 cells were used as a positive control for ELA2 expression. (d) Skin fibroblasts established from Mmp7 −/− and Mmp2 −/− mice were analyzed for the expression of Mmp2 and Mmp7 using RT-PCR. KCT960 cells were used as a positive control for Mmp7 expression. (e) Skin fibroblasts from Mmp7 −/− and Mmp2 −/− mice were transiently transfected with control (CMV9) and MUC16-Cter (F114HA) plasmids and the cell lysates were immunoblotted with respective antibodies to assess the role of Mmp7 (and therefore MMP7) in the cleavage of MUC16. Mmp2 −/− fibroblasts were used as a control.
    Hindiii Ecorv Digested P3x Flag Cmv 13, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore p3x flag myc cmv 24 vector
    Cleavage of MUC16 is independent of Υ-secretase, neutrophil elastase and MMP-7 and intracellular cues. (a) MUC16 does not undergo Υ-secretase-mediated regulated intra-membrane proteolysis (RIP). Schematic representations of luciferase reporter construct to assess RIP of MUC16-Cter. A GAL4 (DNA-binding domain)-VP16 (Activation domain) fusion was cloned into the C-terminus of the MUC16-Cter <t>(CMV9-FLAG-114</t> amino acid fragment) (top panel). Bottom panel: HEK293T cells were cotransfected with empty CMV9 vector (pCMV9) or with M16-114-GAL4-VP16 (pCMV9-M16-114-GV) or APP-C99-GAL4-VP16 (pSG5-C99-GV, positive control for Υ-secretase cleavage) and a luciferase reporter driven by the GAL4 upstream sequence (pFR-Luc) along with pRenilla-Luc for transfection control in the presence or absence of Υ-secretase inhibitor, Inhibitor X (Inh X). The bars represent the normalized luciferase activity of pFR-Luc to pRenilla-Luc of a representative experiment and is presented as mean ± s.e.m, n = 3. (b) MUC16 cleavage was independent of intracellular cues. Amino acids capable of any kind of post-translational modifications were mutated to Ala in the CMV9-F114HA construct and were transfected into HEK293T cells. Cell lysates were immunoblotted with qanti-HA and FLAG antibodies (left panel). Bars on the right represent the normalized cleaved fraction measured by generating a ratio of normalized (with actin) bottom-HA/total-HA (see cleaved fraction calculation in materials and methods). (c) Expression of ELA2 and MMP-7 in multiple cells lines. Expression of ELA2 and MMP-7 were assessed using reverse transcriptase PCR (RT-PCR). U-937 cells were used as a positive control for ELA2 expression. (d) Skin fibroblasts established from Mmp7 −/− and Mmp2 −/− mice were analyzed for the expression of Mmp2 and Mmp7 using RT-PCR. KCT960 cells were used as a positive control for Mmp7 expression. (e) Skin fibroblasts from Mmp7 −/− and Mmp2 −/− mice were transiently transfected with control (CMV9) and MUC16-Cter (F114HA) plasmids and the cell lysates were immunoblotted with respective antibodies to assess the role of Mmp7 (and therefore MMP7) in the cleavage of MUC16. Mmp2 −/− fibroblasts were used as a control.
    P3x Flag Myc Cmv 24 Vector, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Westat p3x flag tpp1 cmv plasmid
    Cleavage of MUC16 is independent of Υ-secretase, neutrophil elastase and MMP-7 and intracellular cues. (a) MUC16 does not undergo Υ-secretase-mediated regulated intra-membrane proteolysis (RIP). Schematic representations of luciferase reporter construct to assess RIP of MUC16-Cter. A GAL4 (DNA-binding domain)-VP16 (Activation domain) fusion was cloned into the C-terminus of the MUC16-Cter <t>(CMV9-FLAG-114</t> amino acid fragment) (top panel). Bottom panel: HEK293T cells were cotransfected with empty CMV9 vector (pCMV9) or with M16-114-GAL4-VP16 (pCMV9-M16-114-GV) or APP-C99-GAL4-VP16 (pSG5-C99-GV, positive control for Υ-secretase cleavage) and a luciferase reporter driven by the GAL4 upstream sequence (pFR-Luc) along with pRenilla-Luc for transfection control in the presence or absence of Υ-secretase inhibitor, Inhibitor X (Inh X). The bars represent the normalized luciferase activity of pFR-Luc to pRenilla-Luc of a representative experiment and is presented as mean ± s.e.m, n = 3. (b) MUC16 cleavage was independent of intracellular cues. Amino acids capable of any kind of post-translational modifications were mutated to Ala in the CMV9-F114HA construct and were transfected into HEK293T cells. Cell lysates were immunoblotted with qanti-HA and FLAG antibodies (left panel). Bars on the right represent the normalized cleaved fraction measured by generating a ratio of normalized (with actin) bottom-HA/total-HA (see cleaved fraction calculation in materials and methods). (c) Expression of ELA2 and MMP-7 in multiple cells lines. Expression of ELA2 and MMP-7 were assessed using reverse transcriptase PCR (RT-PCR). U-937 cells were used as a positive control for ELA2 expression. (d) Skin fibroblasts established from Mmp7 −/− and Mmp2 −/− mice were analyzed for the expression of Mmp2 and Mmp7 using RT-PCR. KCT960 cells were used as a positive control for Mmp7 expression. (e) Skin fibroblasts from Mmp7 −/− and Mmp2 −/− mice were transiently transfected with control (CMV9) and MUC16-Cter (F114HA) plasmids and the cell lysates were immunoblotted with respective antibodies to assess the role of Mmp7 (and therefore MMP7) in the cleavage of MUC16. Mmp2 −/− fibroblasts were used as a control.
    P3x Flag Tpp1 Cmv Plasmid, supplied by Westat, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Cleavage of MUC16 is independent of Υ-secretase, neutrophil elastase and MMP-7 and intracellular cues. (a) MUC16 does not undergo Υ-secretase-mediated regulated intra-membrane proteolysis (RIP). Schematic representations of luciferase reporter construct to assess RIP of MUC16-Cter. A GAL4 (DNA-binding domain)-VP16 (Activation domain) fusion was cloned into the C-terminus of the MUC16-Cter (CMV9-FLAG-114 amino acid fragment) (top panel). Bottom panel: HEK293T cells were cotransfected with empty CMV9 vector (pCMV9) or with M16-114-GAL4-VP16 (pCMV9-M16-114-GV) or APP-C99-GAL4-VP16 (pSG5-C99-GV, positive control for Υ-secretase cleavage) and a luciferase reporter driven by the GAL4 upstream sequence (pFR-Luc) along with pRenilla-Luc for transfection control in the presence or absence of Υ-secretase inhibitor, Inhibitor X (Inh X). The bars represent the normalized luciferase activity of pFR-Luc to pRenilla-Luc of a representative experiment and is presented as mean ± s.e.m, n = 3. (b) MUC16 cleavage was independent of intracellular cues. Amino acids capable of any kind of post-translational modifications were mutated to Ala in the CMV9-F114HA construct and were transfected into HEK293T cells. Cell lysates were immunoblotted with qanti-HA and FLAG antibodies (left panel). Bars on the right represent the normalized cleaved fraction measured by generating a ratio of normalized (with actin) bottom-HA/total-HA (see cleaved fraction calculation in materials and methods). (c) Expression of ELA2 and MMP-7 in multiple cells lines. Expression of ELA2 and MMP-7 were assessed using reverse transcriptase PCR (RT-PCR). U-937 cells were used as a positive control for ELA2 expression. (d) Skin fibroblasts established from Mmp7 −/− and Mmp2 −/− mice were analyzed for the expression of Mmp2 and Mmp7 using RT-PCR. KCT960 cells were used as a positive control for Mmp7 expression. (e) Skin fibroblasts from Mmp7 −/− and Mmp2 −/− mice were transiently transfected with control (CMV9) and MUC16-Cter (F114HA) plasmids and the cell lysates were immunoblotted with respective antibodies to assess the role of Mmp7 (and therefore MMP7) in the cleavage of MUC16. Mmp2 −/− fibroblasts were used as a control.

    Journal: Scientific Reports

    Article Title: Membrane proximal ectodomain cleavage of MUC16 occurs in the acidifying Golgi/post-Golgi compartments

    doi: 10.1038/srep09759

    Figure Lengend Snippet: Cleavage of MUC16 is independent of Υ-secretase, neutrophil elastase and MMP-7 and intracellular cues. (a) MUC16 does not undergo Υ-secretase-mediated regulated intra-membrane proteolysis (RIP). Schematic representations of luciferase reporter construct to assess RIP of MUC16-Cter. A GAL4 (DNA-binding domain)-VP16 (Activation domain) fusion was cloned into the C-terminus of the MUC16-Cter (CMV9-FLAG-114 amino acid fragment) (top panel). Bottom panel: HEK293T cells were cotransfected with empty CMV9 vector (pCMV9) or with M16-114-GAL4-VP16 (pCMV9-M16-114-GV) or APP-C99-GAL4-VP16 (pSG5-C99-GV, positive control for Υ-secretase cleavage) and a luciferase reporter driven by the GAL4 upstream sequence (pFR-Luc) along with pRenilla-Luc for transfection control in the presence or absence of Υ-secretase inhibitor, Inhibitor X (Inh X). The bars represent the normalized luciferase activity of pFR-Luc to pRenilla-Luc of a representative experiment and is presented as mean ± s.e.m, n = 3. (b) MUC16 cleavage was independent of intracellular cues. Amino acids capable of any kind of post-translational modifications were mutated to Ala in the CMV9-F114HA construct and were transfected into HEK293T cells. Cell lysates were immunoblotted with qanti-HA and FLAG antibodies (left panel). Bars on the right represent the normalized cleaved fraction measured by generating a ratio of normalized (with actin) bottom-HA/total-HA (see cleaved fraction calculation in materials and methods). (c) Expression of ELA2 and MMP-7 in multiple cells lines. Expression of ELA2 and MMP-7 were assessed using reverse transcriptase PCR (RT-PCR). U-937 cells were used as a positive control for ELA2 expression. (d) Skin fibroblasts established from Mmp7 −/− and Mmp2 −/− mice were analyzed for the expression of Mmp2 and Mmp7 using RT-PCR. KCT960 cells were used as a positive control for Mmp7 expression. (e) Skin fibroblasts from Mmp7 −/− and Mmp2 −/− mice were transiently transfected with control (CMV9) and MUC16-Cter (F114HA) plasmids and the cell lysates were immunoblotted with respective antibodies to assess the role of Mmp7 (and therefore MMP7) in the cleavage of MUC16. Mmp2 −/− fibroblasts were used as a control.

    Article Snippet: For expression in the mammalian system, p3X-FLAG-CMV9 (Sigma) and pSecTag2C (Invitrogen) plasmids were used to make various constructs.

    Techniques: Luciferase, Construct, Binding Assay, Activation Assay, Clone Assay, Plasmid Preparation, Positive Control, Sequencing, Transfection, Activity Assay, Expressing, Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, Mouse Assay

    Membrane proximal ectodomain cleavage of MUC16. (a) Schematic representation of full-length and different lengths of MUC16-Cter fragments with N-terminal FLAG and C-terminal HA-tag cloned into the p3X-FLAG-CMV9 vector (CMV9) with a preprotrypsin leader peptide (LP). The predicted cleavage sites in the last (site #1, PLARRVDR) and penultimate (site #2, DSVLV) SEA domains are indicated. (b) HEK293T cells were transiently transfected with the plasmids mentioned in (a) and were immunoblotted with anti-FLAG and anti-HA antibodies. Cleaved MUC16 is indicated by an arrow in the HA immunoblot. (c and d) Multiple cleavage events were not observed in the MUC16 carboxyl terminal region as predicted. (c) Schematic representation of a 321 amino acids fragment of the MUC16-Cter region cloned into the pSecTag2C vector with an Ig-κ leader peptide. N-terminal HA and C-terminal Myc-tags were added, with or without an internal FLAG-tag to identify multiple cleavage sites upstream with particular emphasis on the predicted DSVLV site in the penultimate SEA domain. (d) HEK293T cells were transfected with the plasmids mentioned in (c) and were immunoblotted with anti-HA, FLAG and Myc antibodies. (e and f) Domain swapping experiment reiterates the cleavage of MUC16 in the membrane proximal 12 amino acids. (e) Schematic representation of various domains of 114 and 150 amino acids from the C-ter fragments of MUC16 and MUC4 respectively (i.e. ECD, TM and CTD as shown in the schematic, top panel) were swapped with each other (bottom panel of the schematics) and cloned into the CMV9 vector with N-terminal FLAG and C-terminal HA tags. (f) HEK293T cells were transiently transfected with the plasmids shown in (e). Cell lysates were immunoblotted with anti-FLAG and anti-HA antibodies to assess the effect of different domains on cleavage.

    Journal: Scientific Reports

    Article Title: Membrane proximal ectodomain cleavage of MUC16 occurs in the acidifying Golgi/post-Golgi compartments

    doi: 10.1038/srep09759

    Figure Lengend Snippet: Membrane proximal ectodomain cleavage of MUC16. (a) Schematic representation of full-length and different lengths of MUC16-Cter fragments with N-terminal FLAG and C-terminal HA-tag cloned into the p3X-FLAG-CMV9 vector (CMV9) with a preprotrypsin leader peptide (LP). The predicted cleavage sites in the last (site #1, PLARRVDR) and penultimate (site #2, DSVLV) SEA domains are indicated. (b) HEK293T cells were transiently transfected with the plasmids mentioned in (a) and were immunoblotted with anti-FLAG and anti-HA antibodies. Cleaved MUC16 is indicated by an arrow in the HA immunoblot. (c and d) Multiple cleavage events were not observed in the MUC16 carboxyl terminal region as predicted. (c) Schematic representation of a 321 amino acids fragment of the MUC16-Cter region cloned into the pSecTag2C vector with an Ig-κ leader peptide. N-terminal HA and C-terminal Myc-tags were added, with or without an internal FLAG-tag to identify multiple cleavage sites upstream with particular emphasis on the predicted DSVLV site in the penultimate SEA domain. (d) HEK293T cells were transfected with the plasmids mentioned in (c) and were immunoblotted with anti-HA, FLAG and Myc antibodies. (e and f) Domain swapping experiment reiterates the cleavage of MUC16 in the membrane proximal 12 amino acids. (e) Schematic representation of various domains of 114 and 150 amino acids from the C-ter fragments of MUC16 and MUC4 respectively (i.e. ECD, TM and CTD as shown in the schematic, top panel) were swapped with each other (bottom panel of the schematics) and cloned into the CMV9 vector with N-terminal FLAG and C-terminal HA tags. (f) HEK293T cells were transiently transfected with the plasmids shown in (e). Cell lysates were immunoblotted with anti-FLAG and anti-HA antibodies to assess the effect of different domains on cleavage.

    Article Snippet: For expression in the mammalian system, p3X-FLAG-CMV9 (Sigma) and pSecTag2C (Invitrogen) plasmids were used to make various constructs.

    Techniques: Clone Assay, Plasmid Preparation, Transfection, FLAG-tag