Detection of Dnaic1 protein by Western blotting was performed using a mouse monoclonal antibody generated against a synthetic peptide from the human DNAI1 protein 18 (link) using standard procedures. For analysis of mouse tracheal epithelial cells, total cell lysates were prepared in Mammalian Protein Extraction Reagent (Pierce, Rockford, IL). Ciliary axonemes were isolated from cultured mouse tracheal epithelial cells as previously described 32 (link) and prepared in gel-loading buffer. For studies of protein turnover, both the soluble (cytoplasmic) and pellet (axonemal) fractions from individual cultures were analyzed. Protein samples were fractionated on 4 to 12% Bis-Tris gradient gels (Invitrogen, Carlsbad, CA), transferred to nitrocellulose membranes, and probed using Amersham ECL Plus reagents (GE Healthcare, Buckinghamshire, UK), all according to manufacturer's instructions. For normalization of loading, Western blots of cytoplasmic extracts were reprobed with an antibody to GAPDH (Sigma, St. Louis, MO), and axonemal pellets were reprobed with mouse anti-acetylated α-tubulin (Invitrogen). Quantification of signals was performed on an Odyssey Imaging System (Licor, Lincoln, NB).
An antibody to gapdh
Manufactured by Merck Group
The Merck Group's antibody to GAPDH is a laboratory reagent used for the detection and quantification of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein in biological samples. GAPDH is a widely expressed enzyme involved in the glycolytic pathway. This antibody can be used in various analytical techniques, such as Western blotting, immunohistochemistry, and ELISA, to study the expression and localization of GAPDH in cells and tissues.
Automatically generated - may contain errors
2 protocols using an antibody to gapdh
1
DNAIC1 Protein Detection in Mouse Trachea
2
DNAIC1 Protein Detection in Mouse Trachea
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Detection of Dnaic1 protein by Western blotting was performed using a mouse monoclonal antibody generated against a synthetic peptide from the human DNAI1 protein 18 (link) using standard procedures. For analysis of mouse tracheal epithelial cells, total cell lysates were prepared in Mammalian Protein Extraction Reagent (Pierce, Rockford, IL). Ciliary axonemes were isolated from cultured mouse tracheal epithelial cells as previously described 32 (link) and prepared in gel-loading buffer. For studies of protein turnover, both the soluble (cytoplasmic) and pellet (axonemal) fractions from individual cultures were analyzed. Protein samples were fractionated on 4 to 12% Bis-Tris gradient gels (Invitrogen, Carlsbad, CA), transferred to nitrocellulose membranes, and probed using Amersham ECL Plus reagents (GE Healthcare, Buckinghamshire, UK), all according to manufacturer's instructions. For normalization of loading, Western blots of cytoplasmic extracts were reprobed with an antibody to GAPDH (Sigma, St. Louis, MO), and axonemal pellets were reprobed with mouse anti-acetylated α-tubulin (Invitrogen). Quantification of signals was performed on an Odyssey Imaging System (Licor, Lincoln, NB).
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