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Arhgap1 cdc42gap

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Arhgap1/Cdc42gap is a protein that functions as a GTPase-activating protein (GAP) for the Rho family GTPase Cdc42. It promotes the hydrolysis of GTP bound to Cdc42, thereby inactivating Cdc42 signaling. Arhgap1/Cdc42gap is involved in the regulation of actin cytoskeleton organization and cell morphology.

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Lab products found in correlation

Ubiquitin, by Santa Cruz Biotechnology (2 mentions) Protein a g plus beads, by Santa Cruz Biotechnology (2 mentions) Traf6, by Santa Cruz Biotechnology (2 mentions) Myc tag, by Cell Signaling Technology (2 mentions) Gapdh, by Cell Signaling Technology (2 mentions) β actin, by Cell Signaling Technology (2 mentions)

2 protocols using arhgap1 cdc42gap

1

Protein Fractionation and Immunoprecipitation Analysis

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Cells were lysed in cold RIPA buffer in the presence of PMSF, sodium orthovanadate, protease and phosphatase inhibitors. Protein concentration was evaluated by a BCA assay (32106, Pierce). For cytosol and nuclei protein fractionation, cytosol proteins were recovered in 10 mM Hepes pH 7.9, 10 mM KCl, 0,1 mM EDTA, 0,1 mM EGTA, 0,4 % NP40, 1 mM DTT, 0,1 mM PMSF, 10 µg/ml aprotonin, 1 mM OVA. For immunoprecipitation, TRAF6, hnRNPA1 or M2 antibodies (2µg) were added to cell lysates (1–5 mg) for 3 h at 4°C and captured by the addition of Protein A/G Plus beads (sc-2003; Santa Cruz) as described before51 (link). The immune complexes were recovered and detected by immunoblotting. Western blot analysis was performed with the following antibodies: TRAF6 (sc-7221; Santa Cruz)52 , ubiquitin (sc-8017; Santa Cruz), Myc-tag (2278; Cell Signaling), M2 (F3105; Sigma), Arhgap1/Cdc42gap (discontinued; BD Laboratories)29 (link),53 (link), Cdc42 (ab64533; Abcam), hnRNPA1 (sc-10030; Santa Cruz), Tubulin (ab6160; Abcam), β-actin (4968; Cell Signaling), GAPDH (5174; Cell Signaling).
Fang J., Bolanos L., Choi K., Liu X., Christie S., Akunuru S., Kumar R., Wang D., Chen X., Greis K.D., Stoilov P., Filippi M.D., Maciejewski J.P., Garcia-Manero G., Weirauch M.T., Salamonis N., Geiger H., Zheng Y, & Starczynowski D.T. (2016). Ubiquitination of the spliceosome auxiliary factor hnRNPA1 by TRAF6 links chronic innate immune signaling with hematopoietic defects and myelodysplasia. Nature immunology, 18(2), 236-245.
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2

Protein Fractionation and Immunoprecipitation Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Cells were lysed in cold RIPA buffer in the presence of PMSF, sodium orthovanadate, protease and phosphatase inhibitors. Protein concentration was evaluated by a BCA assay (32106, Pierce). For cytosol and nuclei protein fractionation, cytosol proteins were recovered in 10 mM Hepes pH 7.9, 10 mM KCl, 0,1 mM EDTA, 0,1 mM EGTA, 0,4 % NP40, 1 mM DTT, 0,1 mM PMSF, 10 µg/ml aprotonin, 1 mM OVA. For immunoprecipitation, TRAF6, hnRNPA1 or M2 antibodies (2µg) were added to cell lysates (1–5 mg) for 3 h at 4°C and captured by the addition of Protein A/G Plus beads (sc-2003; Santa Cruz) as described before51 (link). The immune complexes were recovered and detected by immunoblotting. Western blot analysis was performed with the following antibodies: TRAF6 (sc-7221; Santa Cruz)52 , ubiquitin (sc-8017; Santa Cruz), Myc-tag (2278; Cell Signaling), M2 (F3105; Sigma), Arhgap1/Cdc42gap (discontinued; BD Laboratories)29 (link),53 (link), Cdc42 (ab64533; Abcam), hnRNPA1 (sc-10030; Santa Cruz), Tubulin (ab6160; Abcam), β-actin (4968; Cell Signaling), GAPDH (5174; Cell Signaling).
Fang J., Bolanos L., Choi K., Liu X., Christie S., Akunuru S., Kumar R., Wang D., Chen X., Greis K.D., Stoilov P., Filippi M.D., Maciejewski J.P., Garcia-Manero G., Weirauch M.T., Salamonis N., Geiger H., Zheng Y, & Starczynowski D.T. (2016). Ubiquitination of the spliceosome auxiliary factor hnRNPA1 by TRAF6 links chronic innate immune signaling with hematopoietic defects and myelodysplasia. Nature immunology, 18(2), 236-245.
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