anti gfp d5 1 mab rabbit  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti gfp d5 1 mab rabbit
    KEY RESOURCES TABLE
    Anti Gfp D5 1 Mab Rabbit, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gfp d5 1 mab rabbit/product/Cell Signaling Technology Inc
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    1) Product Images from "Transcriptional kinetic synergy: A complex landscape revealed by integrating modeling and synthetic biology"

    Article Title: Transcriptional kinetic synergy: A complex landscape revealed by integrating modeling and synthetic biology

    Journal: Cell systems

    doi: 10.1016/j.cels.2023.02.003

    KEY RESOURCES TABLE
    Figure Legend Snippet: KEY RESOURCES TABLE

    Techniques Used: Recombinant, SYBR Green Assay, Plasmid Preparation, Software, Flow Cytometry

    anti gfp d5 1 rabbit monoclonal antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti gfp d5 1 rabbit monoclonal antibody
    KEY RESOURCES TABLE
    Anti Gfp D5 1 Rabbit Monoclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gfp d5 1 rabbit monoclonal antibody/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
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    1) Product Images from "Transcriptional kinetic synergy: A complex landscape revealed by integrating modeling and synthetic biology"

    Article Title: Transcriptional kinetic synergy: A complex landscape revealed by integrating modeling and synthetic biology

    Journal: Cell systems

    doi: 10.1016/j.cels.2023.02.003

    KEY RESOURCES TABLE
    Figure Legend Snippet: KEY RESOURCES TABLE

    Techniques Used: Recombinant, SYBR Green Assay, Plasmid Preparation, Software, Flow Cytometry

    gfp d5 1 rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc gfp d5 1 rabbit mab
    Gfp D5 1 Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti gfp d5 1 xp rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti gfp d5 1 xp rabbit mab
    Anti Gfp D5 1 Xp Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gfp d5 1 xp rabbit mab/product/Cell Signaling Technology Inc
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    gfp d5 1 rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc gfp d5 1 rabbit mab
    Identification of EDRF1 as another substrate of dengue virus protease (A and B) In vitro pull-down assay from K562 cell lysate with pRSET-A NS2BNS3pro purified protein and (B) negative control. The arrows indicate the bands used for identification. See also <xref ref-type=Figures S2 A and S2B. (C and D) Identification data of the protein bands obtained from above in vitro pull-down assay. (E–G) The graph represents the Mascot search result showing the identified protein as EDRF1 with the top score 57. Western blotting analysis of the fractions of pull-down assay by using anti-EDRF1 antibody, experimental (F), and negative control (G). (H) Western blot analysis after 48 h of co-transfection. HEK cells were transfected with single or co-transfected with recombinant vectors as indicated on the blots and probed with anti-myc tag antibodies. (I) Ponceau S staining of the above membrane Lanes: 7–12 and M (protein marker). (J) The above membrane was stripped and probed with anti-GFP antibodies. " width="250" height="auto" />
    Gfp D5 1 Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gfp d5 1 rabbit mab/product/Cell Signaling Technology Inc
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    1) Product Images from "Differential localization of dengue virus protease affects cell homeostasis and triggers to thrombocytopenia"

    Article Title: Differential localization of dengue virus protease affects cell homeostasis and triggers to thrombocytopenia

    Journal: iScience

    doi: 10.1016/j.isci.2023.107024

    Identification of EDRF1 as another substrate of dengue virus protease (A and B) In vitro pull-down assay from K562 cell lysate with pRSET-A NS2BNS3pro purified protein and (B) negative control. The arrows indicate the bands used for identification. See also <xref ref-type=Figures S2 A and S2B. (C and D) Identification data of the protein bands obtained from above in vitro pull-down assay. (E–G) The graph represents the Mascot search result showing the identified protein as EDRF1 with the top score 57. Western blotting analysis of the fractions of pull-down assay by using anti-EDRF1 antibody, experimental (F), and negative control (G). (H) Western blot analysis after 48 h of co-transfection. HEK cells were transfected with single or co-transfected with recombinant vectors as indicated on the blots and probed with anti-myc tag antibodies. (I) Ponceau S staining of the above membrane Lanes: 7–12 and M (protein marker). (J) The above membrane was stripped and probed with anti-GFP antibodies. " title="... The above membrane was stripped and probed with anti-GFP antibodies. " property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Identification of EDRF1 as another substrate of dengue virus protease (A and B) In vitro pull-down assay from K562 cell lysate with pRSET-A NS2BNS3pro purified protein and (B) negative control. The arrows indicate the bands used for identification. See also Figures S2 A and S2B. (C and D) Identification data of the protein bands obtained from above in vitro pull-down assay. (E–G) The graph represents the Mascot search result showing the identified protein as EDRF1 with the top score 57. Western blotting analysis of the fractions of pull-down assay by using anti-EDRF1 antibody, experimental (F), and negative control (G). (H) Western blot analysis after 48 h of co-transfection. HEK cells were transfected with single or co-transfected with recombinant vectors as indicated on the blots and probed with anti-myc tag antibodies. (I) Ponceau S staining of the above membrane Lanes: 7–12 and M (protein marker). (J) The above membrane was stripped and probed with anti-GFP antibodies.

    Techniques Used: In Vitro, Pull Down Assay, Purification, Negative Control, Western Blot, Cotransfection, Transfection, Recombinant, Staining, Marker


    Figure Legend Snippet:

    Techniques Used: Infection, Recombinant, Staining, Plasmid Preparation, Isolation, Gel Extraction, Derivative Assay, Software

    rabbit anti gfp monoclonal antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti gfp monoclonal antibody
    Rabbit Anti Gfp Monoclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti gfp d5 1 xp rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti gfp d5 1 xp rabbit mab
    Pacsin 2 SH3 domain interacts with the N-cadherin cytoplasmic region to regulate cell–cell contact formation. (A) Schematically illustrated domain structures of human pacsin 2 and human N-cadherin. Cyto, cytoplasmic domain; EC, extracellular domain; TM, transmembrane domain. Numbers indicate amino acid positions. (B) Amino acid sequences of the cytoplasmic domain of N-cadherin. Two PxxP motifs (bold and underlined) and p120-binding regions (italicized and underlined) are shown. Numbers indicate amino acid positions. (C) Interaction between pacsin 2 SH3 domain and N-cadherin in T24 cells in GST pull-down assays. Immunoblot probed with anti-N-cadherin antibody (IB: αNCAD) and a CBB-stained SDS–PAGE gel (CBB) for input (Inp; 0.16% of total lysate) and pulled-down fractions with either GST beads (GST) or GST–pacsin 2 SH3 beads (GST–SH3) are shown. The positions of endogenous N-cadherin in T24 cells, and of GST–SH3 and GST alone, are marked by arrowheads. (D) Interaction between pacsin 2 SH3 domain and N-cadherin cytoplasmic domain in GST pull-down assays. Immunoblots probed <t>with</t> <t>anti-GFP</t> antibody (IB: αGFP) and CBB-stained SDS–PAGE gels (CBB) for input (Inp; 0.16% of total lysate) and pulled-down fractions with either GST beads (GST) or GST–pacsin 2 SH3 beads (GST–SH3) are shown. Positions of wild-type (wt) and mutant (P818/821A, P847/850/851A and P818/821/847/850/851A) forms of GFP-tagged N-cadherin cytoplasmic domain (GFP–NCADcyto), and of GST (GST) and GST-tagged pacsin 2 SH3 domain (GST–SH3), are marked by arrowheads. (E) Interaction between pacsin 2 SH3 domain and full-length N-cadherin in GST pull-down assays. Immunoblots probed <t>with</t> <t>anti-GFP</t> antibody (IB: αGFP) and CBB-stained SDS–PAGE gels (CBB) for input (Inp; 0.16% of total lysate) and pulled-down fractions with either GST beads (GST) or GST–pacsin 2 SH3 beads (GST–SH3) are shown. Positions of wild-type (Wt) or the PxxP mutant form (P818/821/847/850/851A) of GFP-tagged N-cadherin (NCAD–GFP), and of GST (GST) and GST-tagged pacsin 2 SH3 domain (GST–SH3), are marked by arrowheads. Images shown in C–E are representative of three independent experiments. (F) Expression of pacsin 2-binding-defective N-cadherin phenocopies the effects of pacsin 2 depletion. Immunofluorescence images showing exogenously expressed GFP-tagged wild-type (NCADWt–GFP) or PA mutant (P818/821/847/850/851A mutations; NCADPA–GFP) N-cadherin, and F-actin in T24 cells. Merged images show GFP-tagged N-cadherin (green), F-actin (red) and DNA (blue). Scale bar: 10 μm. (G) Expression of pacsin 2-binding-defective N-cadherin induces accumulations of a junctional component. Immunofluorescence images showing exogenously expressed GFP-tagged wild-type (NCADWt–GFP) or PA mutant (NCADPA–GFP) N-cadherin, and α-catenin in T24 cells. Merged images show GFP-tagged N-cadherin (green), α-catenin (red) and DNA (blue). Scale bar: 10 μm. (H) Quantification of GFP-tagged N-cadherin (NCAD–GFP) signal intensity at cell–cell contact sites for wild-type (Wt) and PA mutant (PA) (Wt, n =63; PA, n =105). (I) Quantification of α-catenin signal intensity at cell–cell contact sites in cells expressing either wild-type (Wt) or PA mutant (PA) NCAD–GFP (Wt, n =63; PA, n =105). (J) The relative intensity of either wild-type (Wt) or PA mutant (PA) NCAD–GFP at cell–cell contact sites, normalized to α-catenin intensity (Wt, n =63; PA, n =105). Horizontal lines in H–J indicate the median. P -values in H–J were calculated using a two-tailed Mann–Whitney test (ns, not significant). (K) Quantification of cell contact formation upon expression of either wild-type (Wt) or PA mutant (PA) NCAD–GFP. Data are presented as mean±s.d. ( n ≥110 cells, N =3). P -values were calculated using an unpaired two-tailed t -test.
    Anti Gfp D5 1 Xp Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gfp d5 1 xp rabbit mab/product/Cell Signaling Technology Inc
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    Images

    1) Product Images from "Pacsin 2-dependent N-cadherin internalization regulates the migration behaviour of malignant cancer cells"

    Article Title: Pacsin 2-dependent N-cadherin internalization regulates the migration behaviour of malignant cancer cells

    Journal: Journal of Cell Science

    doi: 10.1242/jcs.260827

    Pacsin 2 SH3 domain interacts with the N-cadherin cytoplasmic region to regulate cell–cell contact formation. (A) Schematically illustrated domain structures of human pacsin 2 and human N-cadherin. Cyto, cytoplasmic domain; EC, extracellular domain; TM, transmembrane domain. Numbers indicate amino acid positions. (B) Amino acid sequences of the cytoplasmic domain of N-cadherin. Two PxxP motifs (bold and underlined) and p120-binding regions (italicized and underlined) are shown. Numbers indicate amino acid positions. (C) Interaction between pacsin 2 SH3 domain and N-cadherin in T24 cells in GST pull-down assays. Immunoblot probed with anti-N-cadherin antibody (IB: αNCAD) and a CBB-stained SDS–PAGE gel (CBB) for input (Inp; 0.16% of total lysate) and pulled-down fractions with either GST beads (GST) or GST–pacsin 2 SH3 beads (GST–SH3) are shown. The positions of endogenous N-cadherin in T24 cells, and of GST–SH3 and GST alone, are marked by arrowheads. (D) Interaction between pacsin 2 SH3 domain and N-cadherin cytoplasmic domain in GST pull-down assays. Immunoblots probed with anti-GFP antibody (IB: αGFP) and CBB-stained SDS–PAGE gels (CBB) for input (Inp; 0.16% of total lysate) and pulled-down fractions with either GST beads (GST) or GST–pacsin 2 SH3 beads (GST–SH3) are shown. Positions of wild-type (wt) and mutant (P818/821A, P847/850/851A and P818/821/847/850/851A) forms of GFP-tagged N-cadherin cytoplasmic domain (GFP–NCADcyto), and of GST (GST) and GST-tagged pacsin 2 SH3 domain (GST–SH3), are marked by arrowheads. (E) Interaction between pacsin 2 SH3 domain and full-length N-cadherin in GST pull-down assays. Immunoblots probed with anti-GFP antibody (IB: αGFP) and CBB-stained SDS–PAGE gels (CBB) for input (Inp; 0.16% of total lysate) and pulled-down fractions with either GST beads (GST) or GST–pacsin 2 SH3 beads (GST–SH3) are shown. Positions of wild-type (Wt) or the PxxP mutant form (P818/821/847/850/851A) of GFP-tagged N-cadherin (NCAD–GFP), and of GST (GST) and GST-tagged pacsin 2 SH3 domain (GST–SH3), are marked by arrowheads. Images shown in C–E are representative of three independent experiments. (F) Expression of pacsin 2-binding-defective N-cadherin phenocopies the effects of pacsin 2 depletion. Immunofluorescence images showing exogenously expressed GFP-tagged wild-type (NCADWt–GFP) or PA mutant (P818/821/847/850/851A mutations; NCADPA–GFP) N-cadherin, and F-actin in T24 cells. Merged images show GFP-tagged N-cadherin (green), F-actin (red) and DNA (blue). Scale bar: 10 μm. (G) Expression of pacsin 2-binding-defective N-cadherin induces accumulations of a junctional component. Immunofluorescence images showing exogenously expressed GFP-tagged wild-type (NCADWt–GFP) or PA mutant (NCADPA–GFP) N-cadherin, and α-catenin in T24 cells. Merged images show GFP-tagged N-cadherin (green), α-catenin (red) and DNA (blue). Scale bar: 10 μm. (H) Quantification of GFP-tagged N-cadherin (NCAD–GFP) signal intensity at cell–cell contact sites for wild-type (Wt) and PA mutant (PA) (Wt, n =63; PA, n =105). (I) Quantification of α-catenin signal intensity at cell–cell contact sites in cells expressing either wild-type (Wt) or PA mutant (PA) NCAD–GFP (Wt, n =63; PA, n =105). (J) The relative intensity of either wild-type (Wt) or PA mutant (PA) NCAD–GFP at cell–cell contact sites, normalized to α-catenin intensity (Wt, n =63; PA, n =105). Horizontal lines in H–J indicate the median. P -values in H–J were calculated using a two-tailed Mann–Whitney test (ns, not significant). (K) Quantification of cell contact formation upon expression of either wild-type (Wt) or PA mutant (PA) NCAD–GFP. Data are presented as mean±s.d. ( n ≥110 cells, N =3). P -values were calculated using an unpaired two-tailed t -test.
    Figure Legend Snippet: Pacsin 2 SH3 domain interacts with the N-cadherin cytoplasmic region to regulate cell–cell contact formation. (A) Schematically illustrated domain structures of human pacsin 2 and human N-cadherin. Cyto, cytoplasmic domain; EC, extracellular domain; TM, transmembrane domain. Numbers indicate amino acid positions. (B) Amino acid sequences of the cytoplasmic domain of N-cadherin. Two PxxP motifs (bold and underlined) and p120-binding regions (italicized and underlined) are shown. Numbers indicate amino acid positions. (C) Interaction between pacsin 2 SH3 domain and N-cadherin in T24 cells in GST pull-down assays. Immunoblot probed with anti-N-cadherin antibody (IB: αNCAD) and a CBB-stained SDS–PAGE gel (CBB) for input (Inp; 0.16% of total lysate) and pulled-down fractions with either GST beads (GST) or GST–pacsin 2 SH3 beads (GST–SH3) are shown. The positions of endogenous N-cadherin in T24 cells, and of GST–SH3 and GST alone, are marked by arrowheads. (D) Interaction between pacsin 2 SH3 domain and N-cadherin cytoplasmic domain in GST pull-down assays. Immunoblots probed with anti-GFP antibody (IB: αGFP) and CBB-stained SDS–PAGE gels (CBB) for input (Inp; 0.16% of total lysate) and pulled-down fractions with either GST beads (GST) or GST–pacsin 2 SH3 beads (GST–SH3) are shown. Positions of wild-type (wt) and mutant (P818/821A, P847/850/851A and P818/821/847/850/851A) forms of GFP-tagged N-cadherin cytoplasmic domain (GFP–NCADcyto), and of GST (GST) and GST-tagged pacsin 2 SH3 domain (GST–SH3), are marked by arrowheads. (E) Interaction between pacsin 2 SH3 domain and full-length N-cadherin in GST pull-down assays. Immunoblots probed with anti-GFP antibody (IB: αGFP) and CBB-stained SDS–PAGE gels (CBB) for input (Inp; 0.16% of total lysate) and pulled-down fractions with either GST beads (GST) or GST–pacsin 2 SH3 beads (GST–SH3) are shown. Positions of wild-type (Wt) or the PxxP mutant form (P818/821/847/850/851A) of GFP-tagged N-cadherin (NCAD–GFP), and of GST (GST) and GST-tagged pacsin 2 SH3 domain (GST–SH3), are marked by arrowheads. Images shown in C–E are representative of three independent experiments. (F) Expression of pacsin 2-binding-defective N-cadherin phenocopies the effects of pacsin 2 depletion. Immunofluorescence images showing exogenously expressed GFP-tagged wild-type (NCADWt–GFP) or PA mutant (P818/821/847/850/851A mutations; NCADPA–GFP) N-cadherin, and F-actin in T24 cells. Merged images show GFP-tagged N-cadherin (green), F-actin (red) and DNA (blue). Scale bar: 10 μm. (G) Expression of pacsin 2-binding-defective N-cadherin induces accumulations of a junctional component. Immunofluorescence images showing exogenously expressed GFP-tagged wild-type (NCADWt–GFP) or PA mutant (NCADPA–GFP) N-cadherin, and α-catenin in T24 cells. Merged images show GFP-tagged N-cadherin (green), α-catenin (red) and DNA (blue). Scale bar: 10 μm. (H) Quantification of GFP-tagged N-cadherin (NCAD–GFP) signal intensity at cell–cell contact sites for wild-type (Wt) and PA mutant (PA) (Wt, n =63; PA, n =105). (I) Quantification of α-catenin signal intensity at cell–cell contact sites in cells expressing either wild-type (Wt) or PA mutant (PA) NCAD–GFP (Wt, n =63; PA, n =105). (J) The relative intensity of either wild-type (Wt) or PA mutant (PA) NCAD–GFP at cell–cell contact sites, normalized to α-catenin intensity (Wt, n =63; PA, n =105). Horizontal lines in H–J indicate the median. P -values in H–J were calculated using a two-tailed Mann–Whitney test (ns, not significant). (K) Quantification of cell contact formation upon expression of either wild-type (Wt) or PA mutant (PA) NCAD–GFP. Data are presented as mean±s.d. ( n ≥110 cells, N =3). P -values were calculated using an unpaired two-tailed t -test.

    Techniques Used: Binding Assay, Western Blot, Staining, SDS Page, Mutagenesis, Expressing, Immunofluorescence, Two Tailed Test, MANN-WHITNEY

    A N-cadherin mutant with defective pacsin 2 binding shows attenuated internalization. (A) Representative immunoblots of N-cadherin internalization experiments. Surface GFP-tagged N-cadherin was biotinylated at 4°C, and cells were subsequently incubated at 37°C for the indicated periods to allow endocytosis. MESNa was added, as indicated, to remove biotin remaining at the cell surface. Immunoblots using an anti-GFP antibody (IB: αGFP) to detect total GFP-tagged N-cadherin (Input, arrowheads) and internalized GFP-tagged N-cadherin (Pull-down, arrowheads) from T24 cells expressing either wild-type (NCADWt–GFP) or PA mutant (NCADPA–GFP) N-cadherin are shown. (B) Quantification of internalized GFP-tagged N-cadherin from cells expressing either wild-type (NCADWt–GFP) or PA mutant (NCADPA–GFP) N-cadherin after normalizing the internalized GFP-tagged N-cadherin (Pull-down) to the total amount of GFP-tagged N-cadherin (Input) in experiments as shown in A. Data are mean±s.d. ( n =3).
    Figure Legend Snippet: A N-cadherin mutant with defective pacsin 2 binding shows attenuated internalization. (A) Representative immunoblots of N-cadherin internalization experiments. Surface GFP-tagged N-cadherin was biotinylated at 4°C, and cells were subsequently incubated at 37°C for the indicated periods to allow endocytosis. MESNa was added, as indicated, to remove biotin remaining at the cell surface. Immunoblots using an anti-GFP antibody (IB: αGFP) to detect total GFP-tagged N-cadherin (Input, arrowheads) and internalized GFP-tagged N-cadherin (Pull-down, arrowheads) from T24 cells expressing either wild-type (NCADWt–GFP) or PA mutant (NCADPA–GFP) N-cadherin are shown. (B) Quantification of internalized GFP-tagged N-cadherin from cells expressing either wild-type (NCADWt–GFP) or PA mutant (NCADPA–GFP) N-cadherin after normalizing the internalized GFP-tagged N-cadherin (Pull-down) to the total amount of GFP-tagged N-cadherin (Input) in experiments as shown in A. Data are mean±s.d. ( n =3).

    Techniques Used: Mutagenesis, Binding Assay, Western Blot, Incubation, Expressing

    rabbit monoclonal anti gfp  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal anti gfp
    Rabbit Monoclonal Anti Gfp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit monoclonal anti gfp/product/Cell Signaling Technology Inc
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    rabbit monoclonal gfp antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal gfp antibody
    Key resources table
    Rabbit Monoclonal Gfp Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit monoclonal gfp antibody/product/Cell Signaling Technology Inc
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    1) Product Images from "Bcl-x short-isoform is essential for maintaining homeostasis of multiple tissues"

    Article Title: Bcl-x short-isoform is essential for maintaining homeostasis of multiple tissues

    Journal: iScience

    doi: 10.1016/j.isci.2023.106409

    Key resources table
    Figure Legend Snippet: Key resources table

    Techniques Used: Subcloning, Recombinant, Transfection, Protease Inhibitor, Clone Assay, SYBR Green Assay, Plasmid Preparation, Purification, Gel Extraction, Isolation, Viability Assay, Knock-Out, Cell Culture, Mutagenesis, Software, Imaging, Modification

    rabbit monoclonal gfp antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal gfp antibody
    Key resources table
    Rabbit Monoclonal Gfp Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit monoclonal gfp antibody/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit monoclonal gfp antibody - by Bioz Stars, 2023-09
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    1) Product Images from "Bcl-x short-isoform is essential for maintaining homeostasis of multiple tissues"

    Article Title: Bcl-x short-isoform is essential for maintaining homeostasis of multiple tissues

    Journal: iScience

    doi: 10.1016/j.isci.2023.106409

    Key resources table
    Figure Legend Snippet: Key resources table

    Techniques Used: Subcloning, Recombinant, Transfection, Protease Inhibitor, Clone Assay, SYBR Green Assay, Plasmid Preparation, Purification, Gel Extraction, Isolation, Viability Assay, Knock-Out, Cell Culture, Mutagenesis, Software, Imaging, Modification

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    Cell Signaling Technology Inc anti gfp d5 1 mab rabbit
    KEY RESOURCES TABLE
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    KEY RESOURCES TABLE

    Journal: Cell systems

    Article Title: Transcriptional kinetic synergy: A complex landscape revealed by integrating modeling and synthetic biology

    doi: 10.1016/j.cels.2023.02.003

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: anti-GFP D5.1 mAb (rabbit) , Cell Signaling , Cat# 2956; RRID:AB_1196615.

    Techniques: Recombinant, SYBR Green Assay, Plasmid Preparation, Software, Flow Cytometry

    KEY RESOURCES TABLE

    Journal: Cell systems

    Article Title: Transcriptional kinetic synergy: A complex landscape revealed by integrating modeling and synthetic biology

    doi: 10.1016/j.cels.2023.02.003

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: Immunodetection was performed using anti-HA-tag (6E2) mouse monoclonal antibody (Cell Signaling) and anti-GFP (D5.1) rabbit monoclonal antibody (Cell Signaling) 1:200 in 1%BSA/PBS overnight.

    Techniques: Recombinant, SYBR Green Assay, Plasmid Preparation, Software, Flow Cytometry

    Key resources table

    Journal: iScience

    Article Title: Bcl-x short-isoform is essential for maintaining homeostasis of multiple tissues

    doi: 10.1016/j.isci.2023.106409

    Figure Lengend Snippet: Key resources table

    Article Snippet: rabbit monoclonal GFP antibody , Cell Signaling Technology , #2956.

    Techniques: Subcloning, Recombinant, Transfection, Protease Inhibitor, Clone Assay, SYBR Green Assay, Plasmid Preparation, Purification, Gel Extraction, Isolation, Viability Assay, Knock-Out, Cell Culture, Mutagenesis, Software, Imaging, Modification