mouse anti src mab l4a1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc mouse anti src mab l4a1

    Mouse Anti Src Mab L4a1, 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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    1) Product Images from "Protocol to characterize extracellular c-Src tyrosine kinase function through substrate interaction and phosphorylation"

    Article Title: Protocol to characterize extracellular c-Src tyrosine kinase function through substrate interaction and phosphorylation

    Journal: STAR Protocols

    doi: 10.1016/j.xpro.2023.102755


    Figure Legend Snippet:

    Techniques Used: Recombinant, Concentration Assay, Western Blot, Modification, Protease Inhibitor, Staining, Saline, Bradford Assay, Software, Electrophoresis

    mouse anti src mab3 l4a1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc mouse anti src mab3 l4a1
    (A) Domain structure of human <t>c-Src</t> protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody <t>(mAb3)</t> (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .
    Mouse Anti Src Mab3 L4a1, 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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    Average 86 stars, based on 1 article reviews
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    mouse anti src mab3 l4a1 - by Bioz Stars, 2024-03
    86/100 stars

    Images

    1) Product Images from "PhosY-secretome profiling combined with kinase-substrate interaction screening defines active c-Src-driven extracellular signaling"

    Article Title: PhosY-secretome profiling combined with kinase-substrate interaction screening defines active c-Src-driven extracellular signaling

    Journal: Cell reports

    doi: 10.1016/j.celrep.2023.112539

    (A) Domain structure of human c-Src protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody (mAb3) (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .
    Figure Legend Snippet: (A) Domain structure of human c-Src protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody (mAb3) (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .

    Techniques Used: Residue, Construct, Transfection, Expressing, Western Blot, Molecular Weight, Plasmid Preparation, Staining


    Figure Legend Snippet:

    Techniques Used: Recombinant, Virus, Bradford Assay, Staining, Colorimetric Assay, Software

    mouse anti src mab3 l4a1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc mouse anti src mab3 l4a1
    (A) Domain structure of human <t>c-Src</t> protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody <t>(mAb3)</t> (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .
    Mouse Anti Src Mab3 L4a1, 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/mouse anti src mab3 l4a1/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
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    Images

    1) Product Images from "PhosY-secretome profiling combined with kinase-substrate interaction screening defines active c-Src-driven extracellular signaling"

    Article Title: PhosY-secretome profiling combined with kinase-substrate interaction screening defines active c-Src-driven extracellular signaling

    Journal: Cell reports

    doi: 10.1016/j.celrep.2023.112539

    (A) Domain structure of human c-Src protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody (mAb3) (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .
    Figure Legend Snippet: (A) Domain structure of human c-Src protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody (mAb3) (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .

    Techniques Used: Residue, Construct, Transfection, Expressing, Western Blot, Molecular Weight, Plasmid Preparation, Staining


    Figure Legend Snippet:

    Techniques Used: Recombinant, Virus, Bradford Assay, Staining, Colorimetric Assay, Software

    mouse anti src mab3 l4a1  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc mouse anti src mab3 l4a1
    Mouse Anti Src Mab3 L4a1, 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/mouse anti src mab3 l4a1/product/Cell Signaling Technology Inc
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    l4a1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc l4a1
    L4a1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    src l4a1 mouse mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc src l4a1 mouse mab
    Src L4a1 Mouse Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    src l4a1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc src l4a1
    Antibodies used in this study.
    Src L4a1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Does a rare mutation in PTPRA contribute to the development of Parkinson’s disease in an Australian multi-incident family?"

    Article Title: Does a rare mutation in PTPRA contribute to the development of Parkinson’s disease in an Australian multi-incident family?

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0271499

    Antibodies used in this study.
    Figure Legend Snippet: Antibodies used in this study.

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    mouse anti src l4a1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc mouse anti src l4a1
    KEY RESOURCES TABLE
    Mouse Anti Src L4a1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand"

    Article Title: A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand

    Journal: Cell reports

    doi: 10.1016/j.celrep.2022.111039

    KEY RESOURCES TABLE
    Figure Legend Snippet: KEY RESOURCES TABLE

    Techniques Used: Recombinant

    anti src l4a1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti src l4a1
    Anti Src L4a1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    l4a1 wb  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc l4a1 wb

    L4a1 Wb, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "EGFR transactivates RON to drive oncogenic crosstalk"

    Article Title: EGFR transactivates RON to drive oncogenic crosstalk

    Journal: eLife

    doi: 10.7554/eLife.63678


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    Techniques Used: Stable Transfection, Transfection, Plasmid Preparation, Construct, Generated, Cytometry, Kinase Assay, Recombinant, Sequencing, Ligation, Mutagenesis, Bicinchoninic Acid Protein Assay, Expressing, Software, Magnetic Beads

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    Cell Signaling Technology Inc mouse anti src mab l4a1

    Mouse Anti Src Mab L4a1, 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/mouse anti src mab l4a1/product/Cell Signaling Technology Inc
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    Cell Signaling Technology Inc mouse anti src mab3 l4a1
    (A) Domain structure of human <t>c-Src</t> protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody <t>(mAb3)</t> (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .
    Mouse Anti Src Mab3 L4a1, 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/mouse anti src mab3 l4a1/product/Cell Signaling Technology Inc
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    Cell Signaling Technology Inc l4a1
    (A) Domain structure of human <t>c-Src</t> protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody <t>(mAb3)</t> (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .
    L4a1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (A) Domain structure of human <t>c-Src</t> protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody <t>(mAb3)</t> (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .
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    Image Search Results


    Journal: STAR Protocols

    Article Title: Protocol to characterize extracellular c-Src tyrosine kinase function through substrate interaction and phosphorylation

    doi: 10.1016/j.xpro.2023.102755

    Figure Lengend Snippet:

    Article Snippet: Mouse anti-Src mAb (L4A1) Dilution: 1:10,000 (WB); 1 μg/mL for treatment , Cell Signaling Technology , Cat #2110; RRID: AB_10691385.

    Techniques: Recombinant, Concentration Assay, Western Blot, Modification, Protease Inhibitor, Staining, Saline, Bradford Assay, Software, Electrophoresis

    (A) Domain structure of human c-Src protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody (mAb3) (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .

    Journal: Cell reports

    Article Title: PhosY-secretome profiling combined with kinase-substrate interaction screening defines active c-Src-driven extracellular signaling

    doi: 10.1016/j.celrep.2023.112539

    Figure Lengend Snippet: (A) Domain structure of human c-Src protein (Uniprot: P12931) with key regulatory sites. From the N (amino) to the C (carboxyl) terminus, domains include the N-terminal SRC homology SH4 with the unique (U) (brown), SH3 (blue), SH2 (orange), kinase domain (KD; SH1) (green), and C-terminal regulatory (R) (red) domains. Domain range is indicated with residue numbers, shown below each domain (above for SH3). (B) Schematic representation of C-terminal c-Src truncated constructs (untagged) used in (C). Red asterisks: proteins detected in conditioned media (CMs). (C) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using an anti-N-term-c-Src (N-term, N-terminal) antibody (mAb3) (see ). (D) Schematic representation of N-term c-Src truncations from (E). Red asterisks: proteins detected in CMs. (E) Transiently transfected HEK293 cell extracts and CMs. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody (mAb4). (F) HEK293 cells were transiently transfected with c-Src. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src or anti-phos-Y530-Src. (G) Cell extracts and CMs from transiently transfected HEK293 cells. c-Src expression and secretion were evaluated by western blot using anti-C-term-c-Src antibody. c-Src phosphorylation was determined by immunoblotting with anti-phos-Y419-Src antibody. (H) Schematic diagram displaying how c-Src truncations impact on its secretion. Arrows indicate secretion. Red arrow indicates secretion is hindered. MW, molecular weight; WT, wild type; EV, empty vector; Ab, antibody. Empty vector (EV) was used as a control. GAPDH and Coomassie blue staining were used in all immunoblots as loading controls. See also .

    Article Snippet: Mouse anti-Src mAb3 (L4A1) , Cell Signaling Technology , Cat#2110; RRID:AB_10691385.

    Techniques: Residue, Construct, Transfection, Expressing, Western Blot, Molecular Weight, Plasmid Preparation, Staining

    Journal: Cell reports

    Article Title: PhosY-secretome profiling combined with kinase-substrate interaction screening defines active c-Src-driven extracellular signaling

    doi: 10.1016/j.celrep.2023.112539

    Figure Lengend Snippet:

    Article Snippet: Mouse anti-Src mAb3 (L4A1) , Cell Signaling Technology , Cat#2110; RRID:AB_10691385.

    Techniques: Recombinant, Virus, Bradford Assay, Staining, Colorimetric Assay, Software

    Antibodies used in this study.

    Journal: PLoS ONE

    Article Title: Does a rare mutation in PTPRA contribute to the development of Parkinson’s disease in an Australian multi-incident family?

    doi: 10.1371/journal.pone.0271499

    Figure Lengend Snippet: Antibodies used in this study.

    Article Snippet: Src (L4A1) , Cell Signalling , #2110 , 1:3000.

    Techniques:

    KEY RESOURCES TABLE

    Journal: Cell reports

    Article Title: A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand

    doi: 10.1016/j.celrep.2022.111039

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: Mouse anti-Src (L4A1) , Cell Signaling Technology , Cat# 2110; RRID:AB_10691385.

    Techniques: Recombinant

    Journal: eLife

    Article Title: EGFR transactivates RON to drive oncogenic crosstalk

    doi: 10.7554/eLife.63678

    Figure Lengend Snippet:

    Article Snippet: antibody , Anti-Src (Mouse monoclonal) , Cell Signaling Technology , Cat# 2110 RRID: AB_10691385 , Clone L4A1 WB (1:2000).

    Techniques: Stable Transfection, Transfection, Plasmid Preparation, Construct, Generated, Cytometry, Kinase Assay, Recombinant, Sequencing, Ligation, Mutagenesis, Bicinchoninic Acid Protein Assay, Expressing, Software, Magnetic Beads