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Showing 1-6 of 6 results for "hitrap™ hp columns" within Papers
Qing-Guo Zhao et al.
Yi chuan xue bao = Acta genetica Sinica, 33(1), 49-55 (2006-02-03)
Fanconi anemia complementation group L (FANCL) is a novel Fanconi anemia protein, which mono-ubiquitinates FANCD2 as a ubiquitin E3 ligase, and plays a crucial role in DNA damage repair and chromosome stability maintenance. FANCL is involved in the proliferation of
Kaiying Jia et al.
International journal of biological macromolecules, 128, 710-717 (2018-12-31)
In this study exopolysaccharide (EPS) of Enterococcus faecium WEFA23 from healthy infant's feces was yielded as high as 130 mg/L by fermentation. By purification the EPS was further fractioned into A23-1, A23-2, A23-3 and A23-4 on HiTrap Q HP and Superdex
Jing Zhao et al.
Peptides, 33(2), 206-211 (2012-01-17)
A novel antimicrobial peptide, with molecular mass of 1602.0469Da, produced by Brevibacillus laterosporus strain A60 was isolated and purified from the soil of mango plants. The purification procedure consisted of ammonium sulfate precipitation, cation exchange chromatography on an HiTrap SP
Antonella Di Poto et al.
Applied microbiology and biotechnology, 99(13), 5593-5603 (2015-02-17)
Staphylococcus epidermidis is the leading etiologic agent of device-related infections. S. epidermidis is able to bind, by means of the adhesins of its cell wall, the host matrix proteins filming the artificial surfaces. Thence, bacteria cling to biomaterials and infection
Yao-li Wu et al.
Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology, 27(12), 1335-1338 (2011-12-14)
To obtain purificated his-XCL1 recombinant protein of porcine in vitro and prepare the associated polyclonal antibody; To study how the recombinant protein affects on lymphocytes proliferation. Purify the recombinant protein using HiTrap(TM); Chelating HP chromatographic column; Check the purified product
Kyoung-Hwa Choi et al.
Journal of bioscience and bioengineering, 108(6), 455-459 (2009-11-17)
The genes encoding beta-N-acetylglucosaminidase (nagA and cbsA) from Thermotoga maritima and Thermotoga neapolitana were cloned and expressed in Escherichia coli in order to investigate whether Thermotoga sp. is capable of utilizing chitin as a carbon source. NagA and CbsA were
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