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Proteases  |
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Aminopeptidase M, also known as Aminopeptidase N, is an ideal protease to remove amino acids sequentially from the amino terminus of peptides in peptide sequencing applications.
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Carboxypeptidase Y has a broad amino acid specificity, and is able to release every amino acid including proline from the carboxyl-terminus of peptides. It retains activity under the denaturing conditions used for peptide sequencing.
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Factor Xa is often used to remove histidine fusion tags from expressed proteins. By treating a purified, 6xHis-tagged protein expressed with a factor Xa cleavage site, it is possible to obtain the protein in its native form.
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Immobilized ficin is used primarily to generate Fab and F(ab’)2 fragments from mouse IgG1 antibodies, and immobilization virtually eliminates autolysis of the enzyme and allows tight control of the digestion by removing the ficin at any time.
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Immobilized papain is used primarily to generate Fab and Fc fragments from antibodies, and immobilization virtually eliminates autolysis and protease contamination of the sample and allows tight control of the digestion by removing the papain at any time.
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Immobilized pepsin is used primarily to generate F(ab’)2 fragments from antibodies, and immobilization virtually eliminates autolysis and protease contamination of the sample and allows tight control of the digestion by removing the pepsin at any time.
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In-Gel Tryptic Digestion Kit provides a complete set of reagents to perform ~150 digestions on colloidal coomassie or fluorescent dye-stained protein bands.
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The highest quality trypsin along with an optimized protocol to perform 90 protein digests and guanidations to improve sequence coverage.
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Effective protein characterization and identification by mass spectrometry (MS) begins with protein digestion, thus generating peptide fragments.
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Proteinase K, also known as peptidase K, cleaves proteins at the carboxyl side of aliphatic, aromatic or hydrophobic amino acid residues across a wide range of conditions.
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Staphylococcus aureus V-8 protease is specific for the cleavage at the carboxyl side of glutamic and aspartic acid residues. This protease is specific for only glutamate in buffers which do not contain phosphate.
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Submaxillary protease, also known as arginylendopeptidase, cleaves peptide bonds specifically at the carboxyl side of arginine residues of proteins and peptides.
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Trypsin is a pancreatic serine protease with a wide range of applications including amino acid analysis and protein sequencing, mapping and structural studies. Immobilized trypsin allows easy removal of the protease following digestion.
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