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Proteases and Protein-Cleaving Reagents  |
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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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A labeling reagent and artificial protease as a complete Protein Interaction Mapping Kit; contains the Fe-BABE protein cutting reagent, very useful in mapping interaction sites of known proteins.
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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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A complete kit for in-gel trypsin digestion and recovery of excised protein bands for proteomics mass spectrometry of proteins that have been separated by SDS-PAGE and stained with coomassie, silver or fluorescent stains.
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A complete kit for reduction, alkylation, trypsin digestion and guanidination of protein samples for reliable proteomics analysis by mass spectrometry (MS).
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Individual MS-grade proteases purified and optimized for protein digestion and peptide fragmentation for protein characterization and identification by mass spectrometry (MS) and sequencing; includes trypsin, LysC, AspN, GluC and chymotrypsin.
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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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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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