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p120gap  (BPS Bioscience)


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    Structured Review

    BPS Bioscience p120gap
    P120gap, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/100518-1/p120GAP%2C+His-Tag+Recombinant/pm37762480-394-42-43
    Average 92 stars, based on 2 article reviews
    p120gap - by Bioz Stars, 2026-10
    92/100 stars

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    Related Articles

    Activity Assay:

    Article Title: Identification of SH2 Domain-Containing Protein 3C as a Novel, Putative Interactor of Dipeptidyl Peptidase 3.
    Article Snippet: Guanine Nucleotide Exchange (GEF) Activity Test The putative GEF activity of SH2D3C with or without DPP3 was analyzed using the GTPase-Glo Assay kit (Promega, Madison, WI, USA) according to the manufacturer’s instructions. .. To test SH2D3C GEF activity toward RRAS, GTPase activity of 2 μM RRAS was determined in the absence and presence of purified 1 μM SH2D3C-isoform 2 and purified 1 μM DPP3 in the GEF buffer containing 5 μM GTP and 1 μM p120GAP (BPS biosciences, San Diego, CA, USA) in 384-well, flat-bottom white plates (Greiner Bio-one, Kremsmünster, Austria). ..

    Article Title: Identification of SH2 Domain-Containing Protein 3C as a Novel, Putative Interactor of Dipeptidyl Peptidase 3
    Article Snippet: The putative GEF activity of SH2D3C with or without DPP3 was analyzed using the GTPase-Glo Assay kit (Promega, Madison, WI, USA) according to the manufacturer’s instructions. .. To test SH2D3C GEF activity toward RRAS, GTPase activity of 2 μM RRAS was determined in the absence and presence of purified 1 μM SH2D3C-isoform 2 and purified 1 μM DPP3 in the GEF buffer containing 5 μM GTP and 1 μM p120GAP (BPS biosciences, San Diego, CA, USA) in 384-well, flat-bottom white plates (Greiner Bio-one, Kremsmünster, Austria). ..

    Purification:

    Article Title: Identification of SH2 Domain-Containing Protein 3C as a Novel, Putative Interactor of Dipeptidyl Peptidase 3.
    Article Snippet: Guanine Nucleotide Exchange (GEF) Activity Test The putative GEF activity of SH2D3C with or without DPP3 was analyzed using the GTPase-Glo Assay kit (Promega, Madison, WI, USA) according to the manufacturer’s instructions. .. To test SH2D3C GEF activity toward RRAS, GTPase activity of 2 μM RRAS was determined in the absence and presence of purified 1 μM SH2D3C-isoform 2 and purified 1 μM DPP3 in the GEF buffer containing 5 μM GTP and 1 μM p120GAP (BPS biosciences, San Diego, CA, USA) in 384-well, flat-bottom white plates (Greiner Bio-one, Kremsmünster, Austria). ..

    Article Title: Identification of SH2 Domain-Containing Protein 3C as a Novel, Putative Interactor of Dipeptidyl Peptidase 3
    Article Snippet: The putative GEF activity of SH2D3C with or without DPP3 was analyzed using the GTPase-Glo Assay kit (Promega, Madison, WI, USA) according to the manufacturer’s instructions. .. To test SH2D3C GEF activity toward RRAS, GTPase activity of 2 μM RRAS was determined in the absence and presence of purified 1 μM SH2D3C-isoform 2 and purified 1 μM DPP3 in the GEF buffer containing 5 μM GTP and 1 μM p120GAP (BPS biosciences, San Diego, CA, USA) in 384-well, flat-bottom white plates (Greiner Bio-one, Kremsmünster, Austria). ..



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    Image Search Results


    Western blot of the AKR1B1, AKR1A1, AKR1C3, CBR1, and CBR3 in HepG2, MCF-7, and HEK293 cells. β-actin served as a loading control. Depicted is one blot of a series of three for each protein investigated

    Journal: Archives of Toxicology

    Article Title: In vitro evaluation of the reductive carbonyl idarubicin metabolism to evaluate inhibitors of the formation of cardiotoxic idarubicinol via carbonyl and aldo–keto reductases

    doi: 10.1007/s00204-023-03661-7

    Figure Lengend Snippet: Western blot of the AKR1B1, AKR1A1, AKR1C3, CBR1, and CBR3 in HepG2, MCF-7, and HEK293 cells. β-actin served as a loading control. Depicted is one blot of a series of three for each protein investigated

    Article Snippet: The mouse monoclonal antibodies against β-actin (sc-47778), AKR1B1 (aldose reductase (H-6, sc-166918)), CBR1 (B-11, sc-390554), and CBR3 (E-12, sc-374393) were obtained from Santa Cruz (Heidelberg, Germany), the rabbit monoclonal antibody against AKR1C3 (ab209899) and the rabbit polyclonal antibody against AKR1A1 (ab125878) were from Abcam (Cambridge, United Kingdom).

    Techniques: Western Blot, Control

    Inhibition of idarubicinol formation by different inhibitors in HEK293, HepG2, and MCF-7 cells

    Journal: Archives of Toxicology

    Article Title: In vitro evaluation of the reductive carbonyl idarubicin metabolism to evaluate inhibitors of the formation of cardiotoxic idarubicinol via carbonyl and aldo–keto reductases

    doi: 10.1007/s00204-023-03661-7

    Figure Lengend Snippet: Inhibition of idarubicinol formation by different inhibitors in HEK293, HepG2, and MCF-7 cells

    Article Snippet: The mouse monoclonal antibodies against β-actin (sc-47778), AKR1B1 (aldose reductase (H-6, sc-166918)), CBR1 (B-11, sc-390554), and CBR3 (E-12, sc-374393) were obtained from Santa Cruz (Heidelberg, Germany), the rabbit monoclonal antibody against AKR1C3 (ab209899) and the rabbit polyclonal antibody against AKR1A1 (ab125878) were from Abcam (Cambridge, United Kingdom).

    Techniques: Inhibition

    Expression of the mRNA of the five reductases in human liver samples and HepG2 cells. mRNA expression of AKR1A1, AKR1B1, AKR1C3, CBR1 , and CBR3 was quantified in 7 human liver samples and HepG2 cells via real-time RT-PCR and normalized to the expression of the two housekeeping genes HUPO and RPL13 . Each data point for the liver samples represents the mean of a technical duplicate and the data for the HepG2 cells represent the mean ± S.E.M. for n = 7

    Journal: Archives of Toxicology

    Article Title: In vitro evaluation of the reductive carbonyl idarubicin metabolism to evaluate inhibitors of the formation of cardiotoxic idarubicinol via carbonyl and aldo–keto reductases

    doi: 10.1007/s00204-023-03661-7

    Figure Lengend Snippet: Expression of the mRNA of the five reductases in human liver samples and HepG2 cells. mRNA expression of AKR1A1, AKR1B1, AKR1C3, CBR1 , and CBR3 was quantified in 7 human liver samples and HepG2 cells via real-time RT-PCR and normalized to the expression of the two housekeeping genes HUPO and RPL13 . Each data point for the liver samples represents the mean of a technical duplicate and the data for the HepG2 cells represent the mean ± S.E.M. for n = 7

    Article Snippet: The mouse monoclonal antibodies against β-actin (sc-47778), AKR1B1 (aldose reductase (H-6, sc-166918)), CBR1 (B-11, sc-390554), and CBR3 (E-12, sc-374393) were obtained from Santa Cruz (Heidelberg, Germany), the rabbit monoclonal antibody against AKR1C3 (ab209899) and the rabbit polyclonal antibody against AKR1A1 (ab125878) were from Abcam (Cambridge, United Kingdom).

    Techniques: Expressing, Quantitative RT-PCR

    Primers for the qRT-PCR.

    Journal: Toxicology in vitro : an international journal published in association with BIBRA

    Article Title: Effects of cellular differentiation in human primary bronchial epithelial cells: Metabolism of 4-(methylnitrosamine)-1-(3-pyridyl)-1-butanone

    doi: 10.1016/j.tiv.2018.12.006

    Figure Lengend Snippet: Primers for the qRT-PCR.

    Article Snippet: Rabbit anti-carbonyl reductase 1 antibody and mouse anti-GAPDH were purchased from Santa Cruz Biotechnology (Dallas, TX).

    Techniques: Amplification

    Protein expression of the major metabolic enzymes implicated in NNK metabolism. Protein expressions of CYP2A6/2A13 and carbonyl reductase 1 were analyzed using immunoblotting in NHBE cells and ALI cultures. β-Actin was used as the loading control.

    Journal: Toxicology in vitro : an international journal published in association with BIBRA

    Article Title: Effects of cellular differentiation in human primary bronchial epithelial cells: Metabolism of 4-(methylnitrosamine)-1-(3-pyridyl)-1-butanone

    doi: 10.1016/j.tiv.2018.12.006

    Figure Lengend Snippet: Protein expression of the major metabolic enzymes implicated in NNK metabolism. Protein expressions of CYP2A6/2A13 and carbonyl reductase 1 were analyzed using immunoblotting in NHBE cells and ALI cultures. β-Actin was used as the loading control.

    Article Snippet: Rabbit anti-carbonyl reductase 1 antibody and mouse anti-GAPDH were purchased from Santa Cruz Biotechnology (Dallas, TX).

    Techniques: Expressing, Western Blot