THIOPROPYL-ACTIVATED MATRIX
THIOPROPYL-ACTIVATED MATRIX结构式
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常用名 | THIOPROPYL-ACTIVATED MATRIX | 英文名 | THIOPROPYL-ACTIVATED MATRIX |
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| CAS号 | 68517-67-9 | 分子量 | N/A | |
| 密度 | N/A | 沸点 | N/A | |
| 分子式 | N/A | 熔点 | N/A | |
| MSDS | 美版 | 闪点 | N/A |
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Robust methods for purification of histones from cultured mammalian cells with the preservation of their native modifications.
Nucleic Acids Res. 37(11) , e81, (2009) Post-translational modifications (PTMs) of histones play a role in modifying chromatin structure for DNA-templated processes in the eukaryotic nucleus, such as transcription, replication, recombination and repair; thus, histone PTMs are considered major playe... |
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High efficiency immunoaffinity purification of anti-peptide antibodies on thiopropyl sepharose immunoadsorbants.
Pept. Res. 2(3) , 249-52, (1989) Antibodies to peptides are routinely made by immunizing animals with peptide linked to a carrier protein such as keyhole limpet hemocyanin (KLH) or bovine serum albumin (BSA) via a disulfide bond. The majority of such a polyclonal antibody response is directe... |
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Purification and site-specific immobilization of genetically engineered glucose dehydrogenase on thiopropyl-Sepharose.
FEBS Lett. 270(1-2) , 41-4, (1990) The gene encoding glucose dehydrogenase (EC 1.1.1.47) from Bacillus subtilis was inserted in a plasmid 1.0 kb downstream from a lac promoter, resulting in a 70-fold higher production of the enzyme when expressed in Escherichia coli. A glucose dehydrogenase mu... |
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Site-specific analysis of protein S-acylation by resin-assisted capture.
J. Lipid Res. 52(2) , 393-8, (2011) Protein S-acylation is a major posttranslational modification whereby a cysteine thiol is converted to a thioester. A prototype is S-palmitoylation (fatty acylation), in which a protein undergoes acylation with a hydrophobic 16 carbon lipid chain. Although th... |
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Apolipoproteins A-I, A-II and E are independently distributed among intracellular and newly secreted HDL of human hepatoma cells
Biochim. Biophys. Acta 1791(12) , 1125-32, (2009) Whereas hepatocytes secrete the major human plasma high density lipoproteins (HDL)-protein, apo A-I, as lipid-free and lipidated species, the biogenic itineraries of apo A-II and apo E are unknown. Human plasma and HepG2 cell-derived apo A-II and apo E occur ... |
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A convenient and rapid method for the complete removal of CoA from butyryl-CoA dehydrogenase.
Biochim. Biophys. Acta 706(2) , 245-8, (1982) The commercially available gel, 2-pyridyl disulphide hydroxypropyl ether-Sepharose (thiopropyl-Sepharose 6B), can be used to remove bound ligand completely from butyryl-CoA dehydrogenase (EC 1.399.2) in two simple operations. The resultant enzyme forms normal... |
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Protein purification using combined streptavidin (or avidin)-Sepharose and thiopropyl-Sepharose affinity chromatography.
J. Chromatogr. A. 603(1-2) , 95-104, (1992) The major problem usually encountered in the application of the (strept)avidin-biotin system to the purification of proteins (or other biological molecules) lies in the difficult reversion of the interaction between immobilized (strept)avidin and the adsorbed... |
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Characterization of the covalent chromatography of thymidylate synthase on thiopropyl-Sepharose 6B.
Biochim. Biophys. Acta 1163(2) , 165-75, (1993) We have examined the covalent chromatography of Lactobacillus casei thymidylate synthase on thiopropyl-Sepharose 6B resin. This enzyme is a dimer of identical subunits, each of which contains one active site that features a catalytic sulfhydryl group (Cys-198... |
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Use of thiopropyl sepharose for the synthesis of an adsorbent for the affinity chromatography of glutathione S-transferase.
J. Chromatogr. B. Biomed. Sci. Appl. 688(2) , 239-43, (1997) Thiopropyl Sepharose 6B in the 2-thiopyridyl-activated form was used for the reversible immobilisation of reduced glutathione (GSH). The resulting affinity matrix was successfully tested as a sorbent for the partial purification of glutathione S-transferase (... |
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Reference map for liquid chromatography-mass spectrometry-based quantitative proteomics.
Anal. Biochem. 393(2) , 155-62, (2009) The accurate mass and time (AMT) tag strategy has been recognized as a powerful tool for high-throughput analysis in liquid chromatography-mass spectrometry (LC-MS)-based proteomics. Due to the complexity of the human proteome, this strategy requires highly a... |