Column is designed for direct lysis of bacterial culture.February 20, 2006 -
HIS-Select(TM) iLAP(TM) 5 ml column combines cell lysis and histidine-tagged protein purification into one step, allowing non-denaturing protein extraction. Single-use, disposable column contains HIS-Select(TM) nickel chelate matrix and CelLytic(TM) Express in tablet format, and high capacity feature of columns enables capture of 1-2 mg of histidine-tagged protein per column. Purified protein is compatible with protein assays, SDS-PAGE, Western blotting, and MALDI.
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Original Press release
Sigma Aldrich Corp.
3050 Spruce St.
St. Louis, MO, 63103
USA
Sigma Introduces New Integrated Lysis and Affinity Purification (iLAP) Columns
ST. LOUIS, Jan. 11 - Sigma, a division of Sigma-Aldrich Corporation (NASDAQ:SIAL), has launched a new HIS-Select(TM) iLAP(TM) 5 ml Column (Product code H9913). The HIS-Select iLAP column is an innovative, patent-pending method that combines cell lysis and histidine- tagged protein purification steps into one step, allowing fast, efficient and non-denaturing protein extraction directly from microbial cultures.
The HIS-Select iLAP column consists of a novel single-use, disposable column designed for the one-step purification of histidine-tagged proteins directly from a 5 ml bacterial culture. This product maximizes the speed and efficiency of recombinant protein extraction while eliminating sample loss. The column contains highly specific HIS-Select(TM) nickel chelate matrix and highly efficient CelLytic(TM) Express, both present in a convenient tablet format. The column is designed for the simultaneous, direct lysis of a 5 ml bacterial culture and affinity capture of the target histidine-tagged protein without any additional manipulation required (such as centrifugation). As the culture is lysed in the column, the target protein is captured on the same highly selective HIS-Select Affinity Gel. The relatively high capacity feature of these columns enables capture of at least 1-2 mg of histidine-tagged protein per column, making them ideal for confirming expression of a histidine-tagged target protein, for performing protein:protein interaction assays, or for rapidly screening colonies or multiple constructs (cultures). The resulting purified protein is compatible with protein assays, SDS-PAGE, Western blotting and MALDI.
"The HIS-Select iLAP technology has dramatically simplified purification of histidine-tagged recombinant proteins directly from bacterial cultures," said Michael Hadjisavas, Global Strategic Marketing Manager, Proteomics, at Sigma-Aldrich Corporation. "This new 5 ml column format allows for the rapid screening of recombinant clones for protein expression and subsequent protein characterization," he added. "Since this technology allows for simultaneous cell lysis and protein purification, it will significantly reduce purification time as well as sample handling, minimizing the potential for protein loss or damage. As a leader in protein purification, we have taken efficiency one step further by introducing a technology which improves the speed and efficiency by which recombinant proteins can be purified."
Sigma-Aldrich is a leading Life Science and High Technology company. Our biochemical and organic chemical products and kits are used in scientific and genomic research, biotechnology, pharmaceutical development, the diagnosis of disease and as key components in pharmaceutical and other high technology manufacturing. We have customers in life science companies, university and government institutions, hospitals, and in industry. Over one million scientists and technologists use their products. Sigma-Aldrich operates in 35 countries and has 6,800 employees providing excellent service worldwide. We are committed to accelerating Customer's success through leadership in Life Science, High Technology and Service. For more information about Sigma- Aldrich, please visit its award-winning web site at http://sigma-aldrich.com/.
CONTACT: Michael Hadjisavas of Sigma-Aldrich, +1-314-286-7431
Web site: http://www.sigma-aldrich.com/
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