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Functional analysis of the Drosophila Dnop5 gene using targeted RNA interference
Functional analysis of the Drosophila Dnop5 gene using targeted RNA interference

... Drosophila. Dnop5, a novel gene in Drosophila, is the member of the conserved nop5/sik1 gene family. As other Nop5/Sik1 family members, DNop5 contains multiple KKX motifs at the carboxy terminus, and is the closest relative of Nop5 of Caenorhabditis elegans. Dnop5 cDNA codes for a transcript of appr ...
Exam 3 Stats
Exam 3 Stats

... The bonds creating the primary structure of a protein are called 1)___________ and form between a 2)___ atom in one amino acid and a 3)____ atom in another amino acid. The bonds creating the secondary structure of a protein are called 4)__________ and form between 5)___________. The bonds creating t ...
View PDF - e-Science Central
View PDF - e-Science Central

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General Biology 115 Summer 2014
General Biology 115 Summer 2014

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Thiol regulation of pro-inflammatory cytokines and innate immunity

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... cotyledons, and in the isolated peroxisomes, respectively, indicating that the antibody was monospecific. We concluded that the antibody cross-reacted with not only AtPMP38 but also PmPMP38, although it was indicated that the molecular mass of PmPMP38 was slightly higher than that of AtPMP38. Subcel ...
Protein Synthesis:
Protein Synthesis:

... 3. This procedure repeats until the ribosome encounters one of three possible stop codons, where translation is terminated. This stalls protein growth, and release factors, proteins which mimic tRNA, enter the A site and release the protein in to the cytoplasm. Synthesis of proteins can take place e ...
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Protein Synthesis:
Protein Synthesis:

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Protein Digestion by Enzymes

... The enzyme above (denoted as E) catalyzes the cutting of another protein, which is its substrate (S). The enzyme first binds to the protein to form an enzyme–substrate complex (ES) and then catalyzes the cleavage of a specific bond in the protein, forming an enzyme–product complex (EP) that rapidly ...
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Molecular Biology Databases

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Western blot



The western blot (sometimes called the protein immunoblot) is a widely used analytical technique used to detect specific proteins in a sample of tissue homogenate or extract. It uses gel electrophoresis to separate native proteins by 3-D structure or denatured proteins by the length of the polypeptide. The proteins are then transferred to a membrane (typically nitrocellulose or PVDF), where they are stained with antibodies specific to the target protein. The gel electrophoresis step is included in western blot analysis to resolve the issue of the cross-reactivity of antibodies.There are many reagent companies that specialize in providing antibodies (both monoclonal and polyclonal antibodies) against tens of thousands of different proteins. Commercial antibodies can be expensive, although the unbound antibody can be reused between experiments. This method is used in the fields of molecular biology, immunogenetics and other molecular biology disciplines. A number of search engines, such as CiteAb, Antibodypedia, and SeekProducts, are available that can help researchers find suitable antibodies for use in western blotting.Other related techniques include dot blot analysis, immunohistochemistry and immunocytochemistry where antibodies are used to detect proteins in tissues and cells by immunostaining, and enzyme-linked immunosorbent assay (ELISA).The method originated in the laboratory of Harry Towbin at the Friedrich Miescher Institute. The name western blot was given to the technique by W. Neal Burnette and is a play on the name Southern blot, a technique for DNA detection developed earlier by Edwin Southern. Detection of RNA is termed northern blot and was developed by George Stark at Stanford.
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