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Structures of GRP94-Nucleotide Complexes Reveal Mechanistic
Structures of GRP94-Nucleotide Complexes Reveal Mechanistic

... Life depends on the biochemical activity of the thousands of proteins that inhabit and decorate the surface of every one of our cells. Proteins themselves, although simple linear combinations of the twenty amino acids, derive their remarkable properties from the complex three-dimensional structures ...
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... non-polar molecule is formed when the atoms in a covalent bond equally share electrons so that no region within it has a charge.  What is the most common polar substance on Earth? Water is the most common polar substance on Earth  What is the difference between a hydrophilic and hydrophobic substa ...
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... P-40. The BiP antibodies (anti-rabbit) (43) and monoclonal p67 antibodies (44) were diluted 1:200 and 1:1000, respectively. The CRAM (45) antibodies and the anti-EP monoclonal antibodies (Cedarline) were diluted 1:300 and 1:500, respectively. Antibodies from a rabbit chronically infected with trypan ...
Advances in Amino Acid Analysis
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... 1960s, Pehr Edman developed the first workable chemical process for sequencing a protein. At about the same time, Stein and Moore devised the automatic amino acid analyzer for describing proteins, earning them the 1972 Nobel Prize in chemistry (4). The underlying protein chemistry of those ...
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Acetylcholine Receptor-associated 43K Protein Contains Covalently

... Three 60-ram cultures of BC3Ht cells were labeled for 4 h with [3H]myristate and 43K protein was immunoprecipitated from the cell lysate with anti-43K serum. Immunoprecipitated proteins were resolved by SDS-PAGE and the region of the unfixed, undried gel containing 43K protein excised using prestain ...
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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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