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non activated trka  (Carna Inc)


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    Carna Inc non activated trka
    Mechanism of action of triazinetriones on <t>TrkA.</t> ( a ) Full-length TrkA with a HA-tag (TrkA-HA) fused to the C -terminus was purified through immunoprecipitation using anti-HA agarose beads. Purified TrkA-HA was incubated with DMSO (blue circles and hatched line), ACD855 (5 µM) (black triangles and solid line), or ACD856 (1 µM) (red squares and solid line) for approx. 5 min. Thereafter, ATP was added to yield the indicated concentration. Each data point is the mean ± SEM ( n = 3). The solid lines are the curve-fit using the Michaelis–Menten equation used to calculate the apparent Vmax(app) and km(app), and the dotted lines are the 95% confidence band for each curve fit. ( b – d ) Affinity labeling and streptavidin adsorption of Trka. ( b ) Western blot of streptavidin adsorbed TrkA-HA non-covalent labeled <t>with</t> <t>NHS-biotinylated</t> triazinetrione compound (lane 2) or covalent labeled by UV-crosslinking of 100 µM sulfo-SBED biotinylated compound (lane 3). Detection of immunoreactive band was performed with anti-TrkA antibody. Supernatant loaded to the left (lane 1) was used as positive control for the Western blot. Arrows on the left indicate the migration of molecular weight markers corresponding to 198, 98, and 62 kDa. ( c ) Anti-HA agarose immunoprecipitation of cross-linked or non-crosslinked sulfo-SBED compound (AC27019-SBED) from cell lysate incubated with 100 µM AC27019-SBED. Lane 1, non-UV-crosslinking, and lane 2, UV-crosslinking of sulfo-SBED labeled TrkA-HA, both detected with streptavidin-HRP. Lanes 3 and 4 are loading controls of lanes 1 and 2, respectively, were TrkA-HA was detected by immunoblotting using the anti-TrkA antibody. Both blots were part of the same gel, but the membrane was cut in two pieces, and the proteins were detected by streptavidin-HRP (left panel) or by an anti-TrkA antibody (right panel). ( d ) Streptavidin adsorption of biotinylated compound bound to TrkA-HA. Lane 1, cell lysate used for positive control of immunodetection; lane 3, cell lysate without biotinylated compound was adsorbed to streptavidin-agarose as negative control; lanes 5 and 7, cell lysates containing sulfo-SBED compound UV-crosslinked to TrkA (from two different experiments) were adsorbed to streptavidin-agarose and immunoblotted using anti-TrkA antibody. Lanes 2, 4, and 6 are empty lanes to avoid cross-contamination between lanes.
    Non Activated Trka, supplied by Carna Inc, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/non+activated+trka/pmc08391421-38-14-20?v=Carna+Inc
    Average 93 stars, based on 2 article reviews
    non activated trka - by Bioz Stars, 2026-07
    93/100 stars

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    1) Product Images from "Identification of Novel Positive Allosteric Modulators of Neurotrophin Receptors for the Treatment of Cognitive Dysfunction"

    Article Title: Identification of Novel Positive Allosteric Modulators of Neurotrophin Receptors for the Treatment of Cognitive Dysfunction

    Journal: Cells

    doi: 10.3390/cells10081871

    Mechanism of action of triazinetriones on TrkA. ( a ) Full-length TrkA with a HA-tag (TrkA-HA) fused to the C -terminus was purified through immunoprecipitation using anti-HA agarose beads. Purified TrkA-HA was incubated with DMSO (blue circles and hatched line), ACD855 (5 µM) (black triangles and solid line), or ACD856 (1 µM) (red squares and solid line) for approx. 5 min. Thereafter, ATP was added to yield the indicated concentration. Each data point is the mean ± SEM ( n = 3). The solid lines are the curve-fit using the Michaelis–Menten equation used to calculate the apparent Vmax(app) and km(app), and the dotted lines are the 95% confidence band for each curve fit. ( b – d ) Affinity labeling and streptavidin adsorption of Trka. ( b ) Western blot of streptavidin adsorbed TrkA-HA non-covalent labeled with NHS-biotinylated triazinetrione compound (lane 2) or covalent labeled by UV-crosslinking of 100 µM sulfo-SBED biotinylated compound (lane 3). Detection of immunoreactive band was performed with anti-TrkA antibody. Supernatant loaded to the left (lane 1) was used as positive control for the Western blot. Arrows on the left indicate the migration of molecular weight markers corresponding to 198, 98, and 62 kDa. ( c ) Anti-HA agarose immunoprecipitation of cross-linked or non-crosslinked sulfo-SBED compound (AC27019-SBED) from cell lysate incubated with 100 µM AC27019-SBED. Lane 1, non-UV-crosslinking, and lane 2, UV-crosslinking of sulfo-SBED labeled TrkA-HA, both detected with streptavidin-HRP. Lanes 3 and 4 are loading controls of lanes 1 and 2, respectively, were TrkA-HA was detected by immunoblotting using the anti-TrkA antibody. Both blots were part of the same gel, but the membrane was cut in two pieces, and the proteins were detected by streptavidin-HRP (left panel) or by an anti-TrkA antibody (right panel). ( d ) Streptavidin adsorption of biotinylated compound bound to TrkA-HA. Lane 1, cell lysate used for positive control of immunodetection; lane 3, cell lysate without biotinylated compound was adsorbed to streptavidin-agarose as negative control; lanes 5 and 7, cell lysates containing sulfo-SBED compound UV-crosslinked to TrkA (from two different experiments) were adsorbed to streptavidin-agarose and immunoblotted using anti-TrkA antibody. Lanes 2, 4, and 6 are empty lanes to avoid cross-contamination between lanes.
    Figure Legend Snippet: Mechanism of action of triazinetriones on TrkA. ( a ) Full-length TrkA with a HA-tag (TrkA-HA) fused to the C -terminus was purified through immunoprecipitation using anti-HA agarose beads. Purified TrkA-HA was incubated with DMSO (blue circles and hatched line), ACD855 (5 µM) (black triangles and solid line), or ACD856 (1 µM) (red squares and solid line) for approx. 5 min. Thereafter, ATP was added to yield the indicated concentration. Each data point is the mean ± SEM ( n = 3). The solid lines are the curve-fit using the Michaelis–Menten equation used to calculate the apparent Vmax(app) and km(app), and the dotted lines are the 95% confidence band for each curve fit. ( b – d ) Affinity labeling and streptavidin adsorption of Trka. ( b ) Western blot of streptavidin adsorbed TrkA-HA non-covalent labeled with NHS-biotinylated triazinetrione compound (lane 2) or covalent labeled by UV-crosslinking of 100 µM sulfo-SBED biotinylated compound (lane 3). Detection of immunoreactive band was performed with anti-TrkA antibody. Supernatant loaded to the left (lane 1) was used as positive control for the Western blot. Arrows on the left indicate the migration of molecular weight markers corresponding to 198, 98, and 62 kDa. ( c ) Anti-HA agarose immunoprecipitation of cross-linked or non-crosslinked sulfo-SBED compound (AC27019-SBED) from cell lysate incubated with 100 µM AC27019-SBED. Lane 1, non-UV-crosslinking, and lane 2, UV-crosslinking of sulfo-SBED labeled TrkA-HA, both detected with streptavidin-HRP. Lanes 3 and 4 are loading controls of lanes 1 and 2, respectively, were TrkA-HA was detected by immunoblotting using the anti-TrkA antibody. Both blots were part of the same gel, but the membrane was cut in two pieces, and the proteins were detected by streptavidin-HRP (left panel) or by an anti-TrkA antibody (right panel). ( d ) Streptavidin adsorption of biotinylated compound bound to TrkA-HA. Lane 1, cell lysate used for positive control of immunodetection; lane 3, cell lysate without biotinylated compound was adsorbed to streptavidin-agarose as negative control; lanes 5 and 7, cell lysates containing sulfo-SBED compound UV-crosslinked to TrkA (from two different experiments) were adsorbed to streptavidin-agarose and immunoblotted using anti-TrkA antibody. Lanes 2, 4, and 6 are empty lanes to avoid cross-contamination between lanes.

    Techniques Used: Purification, Immunoprecipitation, Incubation, Concentration Assay, Labeling, Adsorption, Western Blot, Positive Control, Migration, Molecular Weight, Membrane, Immunodetection, Negative Control



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    non activated trka  (Carna Inc)
    93
    Carna Inc non activated trka
    Mechanism of action of triazinetriones on <t>TrkA.</t> ( a ) Full-length TrkA with a HA-tag (TrkA-HA) fused to the C -terminus was purified through immunoprecipitation using anti-HA agarose beads. Purified TrkA-HA was incubated with DMSO (blue circles and hatched line), ACD855 (5 µM) (black triangles and solid line), or ACD856 (1 µM) (red squares and solid line) for approx. 5 min. Thereafter, ATP was added to yield the indicated concentration. Each data point is the mean ± SEM ( n = 3). The solid lines are the curve-fit using the Michaelis–Menten equation used to calculate the apparent Vmax(app) and km(app), and the dotted lines are the 95% confidence band for each curve fit. ( b – d ) Affinity labeling and streptavidin adsorption of Trka. ( b ) Western blot of streptavidin adsorbed TrkA-HA non-covalent labeled <t>with</t> <t>NHS-biotinylated</t> triazinetrione compound (lane 2) or covalent labeled by UV-crosslinking of 100 µM sulfo-SBED biotinylated compound (lane 3). Detection of immunoreactive band was performed with anti-TrkA antibody. Supernatant loaded to the left (lane 1) was used as positive control for the Western blot. Arrows on the left indicate the migration of molecular weight markers corresponding to 198, 98, and 62 kDa. ( c ) Anti-HA agarose immunoprecipitation of cross-linked or non-crosslinked sulfo-SBED compound (AC27019-SBED) from cell lysate incubated with 100 µM AC27019-SBED. Lane 1, non-UV-crosslinking, and lane 2, UV-crosslinking of sulfo-SBED labeled TrkA-HA, both detected with streptavidin-HRP. Lanes 3 and 4 are loading controls of lanes 1 and 2, respectively, were TrkA-HA was detected by immunoblotting using the anti-TrkA antibody. Both blots were part of the same gel, but the membrane was cut in two pieces, and the proteins were detected by streptavidin-HRP (left panel) or by an anti-TrkA antibody (right panel). ( d ) Streptavidin adsorption of biotinylated compound bound to TrkA-HA. Lane 1, cell lysate used for positive control of immunodetection; lane 3, cell lysate without biotinylated compound was adsorbed to streptavidin-agarose as negative control; lanes 5 and 7, cell lysates containing sulfo-SBED compound UV-crosslinked to TrkA (from two different experiments) were adsorbed to streptavidin-agarose and immunoblotted using anti-TrkA antibody. Lanes 2, 4, and 6 are empty lanes to avoid cross-contamination between lanes.
    Non Activated Trka, supplied by Carna Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/non+activated+trka/pmc08391421-38-14-20?v=Carna+Inc
    Average 93 stars, based on 1 article reviews
    non activated trka - by Bioz Stars, 2026-07
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Mechanism of action of triazinetriones on TrkA. ( a ) Full-length TrkA with a HA-tag (TrkA-HA) fused to the C -terminus was purified through immunoprecipitation using anti-HA agarose beads. Purified TrkA-HA was incubated with DMSO (blue circles and hatched line), ACD855 (5 µM) (black triangles and solid line), or ACD856 (1 µM) (red squares and solid line) for approx. 5 min. Thereafter, ATP was added to yield the indicated concentration. Each data point is the mean ± SEM ( n = 3). The solid lines are the curve-fit using the Michaelis–Menten equation used to calculate the apparent Vmax(app) and km(app), and the dotted lines are the 95% confidence band for each curve fit. ( b – d ) Affinity labeling and streptavidin adsorption of Trka. ( b ) Western blot of streptavidin adsorbed TrkA-HA non-covalent labeled with NHS-biotinylated triazinetrione compound (lane 2) or covalent labeled by UV-crosslinking of 100 µM sulfo-SBED biotinylated compound (lane 3). Detection of immunoreactive band was performed with anti-TrkA antibody. Supernatant loaded to the left (lane 1) was used as positive control for the Western blot. Arrows on the left indicate the migration of molecular weight markers corresponding to 198, 98, and 62 kDa. ( c ) Anti-HA agarose immunoprecipitation of cross-linked or non-crosslinked sulfo-SBED compound (AC27019-SBED) from cell lysate incubated with 100 µM AC27019-SBED. Lane 1, non-UV-crosslinking, and lane 2, UV-crosslinking of sulfo-SBED labeled TrkA-HA, both detected with streptavidin-HRP. Lanes 3 and 4 are loading controls of lanes 1 and 2, respectively, were TrkA-HA was detected by immunoblotting using the anti-TrkA antibody. Both blots were part of the same gel, but the membrane was cut in two pieces, and the proteins were detected by streptavidin-HRP (left panel) or by an anti-TrkA antibody (right panel). ( d ) Streptavidin adsorption of biotinylated compound bound to TrkA-HA. Lane 1, cell lysate used for positive control of immunodetection; lane 3, cell lysate without biotinylated compound was adsorbed to streptavidin-agarose as negative control; lanes 5 and 7, cell lysates containing sulfo-SBED compound UV-crosslinked to TrkA (from two different experiments) were adsorbed to streptavidin-agarose and immunoblotted using anti-TrkA antibody. Lanes 2, 4, and 6 are empty lanes to avoid cross-contamination between lanes.

    Journal: Cells

    Article Title: Identification of Novel Positive Allosteric Modulators of Neurotrophin Receptors for the Treatment of Cognitive Dysfunction

    doi: 10.3390/cells10081871

    Figure Lengend Snippet: Mechanism of action of triazinetriones on TrkA. ( a ) Full-length TrkA with a HA-tag (TrkA-HA) fused to the C -terminus was purified through immunoprecipitation using anti-HA agarose beads. Purified TrkA-HA was incubated with DMSO (blue circles and hatched line), ACD855 (5 µM) (black triangles and solid line), or ACD856 (1 µM) (red squares and solid line) for approx. 5 min. Thereafter, ATP was added to yield the indicated concentration. Each data point is the mean ± SEM ( n = 3). The solid lines are the curve-fit using the Michaelis–Menten equation used to calculate the apparent Vmax(app) and km(app), and the dotted lines are the 95% confidence band for each curve fit. ( b – d ) Affinity labeling and streptavidin adsorption of Trka. ( b ) Western blot of streptavidin adsorbed TrkA-HA non-covalent labeled with NHS-biotinylated triazinetrione compound (lane 2) or covalent labeled by UV-crosslinking of 100 µM sulfo-SBED biotinylated compound (lane 3). Detection of immunoreactive band was performed with anti-TrkA antibody. Supernatant loaded to the left (lane 1) was used as positive control for the Western blot. Arrows on the left indicate the migration of molecular weight markers corresponding to 198, 98, and 62 kDa. ( c ) Anti-HA agarose immunoprecipitation of cross-linked or non-crosslinked sulfo-SBED compound (AC27019-SBED) from cell lysate incubated with 100 µM AC27019-SBED. Lane 1, non-UV-crosslinking, and lane 2, UV-crosslinking of sulfo-SBED labeled TrkA-HA, both detected with streptavidin-HRP. Lanes 3 and 4 are loading controls of lanes 1 and 2, respectively, were TrkA-HA was detected by immunoblotting using the anti-TrkA antibody. Both blots were part of the same gel, but the membrane was cut in two pieces, and the proteins were detected by streptavidin-HRP (left panel) or by an anti-TrkA antibody (right panel). ( d ) Streptavidin adsorption of biotinylated compound bound to TrkA-HA. Lane 1, cell lysate used for positive control of immunodetection; lane 3, cell lysate without biotinylated compound was adsorbed to streptavidin-agarose as negative control; lanes 5 and 7, cell lysates containing sulfo-SBED compound UV-crosslinked to TrkA (from two different experiments) were adsorbed to streptavidin-agarose and immunoblotted using anti-TrkA antibody. Lanes 2, 4, and 6 are empty lanes to avoid cross-contamination between lanes.

    Article Snippet: Recombinant intracellular domain (ICD) of TrkA (08-186) and single site biotinylated activated (08-486-20N) or non-activated TrkA (08-486-23N) were obtained from Carna Biosciences, Odense, Denmark.

    Techniques: Purification, Immunoprecipitation, Incubation, Concentration Assay, Labeling, Adsorption, Western Blot, Positive Control, Migration, Molecular Weight, Membrane, Immunodetection, Negative Control