Bio-Scale CHT20-I Column from Bio-Rad

Product Specs
ItemBio-Scale CHT20-I Column
CompanyBio-Rad
Price $4,997.00Supplier Page View Company Product Page
Catalog Number7510027

Add to Compare List

Bio-Rad

Bio-Rad Laboratories, Inc. Life Science Research Group 2000 Alfred Nobel Drive

Hercules, California 94547

United States

Phone: 800-424 6723
800-879 2289

Company Profile

Website: http://discover.bio-rad.com

(1) Crystal structure of SAM-dependent methyltransferase from Pyrococcus horikoshiiActa Crystallographica Section F Structural Biology CommunicationsDecember 1, 2017K. J. Pampa, S. Madan Kumar, M. K. Hema, Karthik Kumara, S. Naveen, Naoki Kunishima, N. K. Lokanathwere desalted on a HiPrep 26/10 desalting column with 10 mM sodium phosphate pH 7.0 and applied onto a Bio-Scale CHT20-I column (Bio-Rad) equilibrated with 10 mM sodium phosphate pH 7.0. The proteins were again eluted with a linear

(2) The first crystal structure of NAD-dependent 3-dehydro-2-deoxy-D-gluconate dehydrogenase from Thermus thermophilus HB8Acta Crystallographica Section D Biological CrystallographyApril 1, 2014Kudigana J. Pampa, Neratur K. Lokanath, Naoki Kunishima, Ravishankar Vittal Raidesalted using a HiPrep 26/10 desalting column with 10 mM sodium phosphate pH 7.0 and applied onto a Bio-Scale CHT20-I column (BioRad) equilibrated with 10 mM sodium phosphate pH 7.0. DDGDH was eluted with a linear gradient of

(3) Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5Acta Crystallographica Section F Structural Biology and Crystallization CommunicationsFebruary 1, 2010Jeyaraman Jeyakanthan, Subbiah Thamotharan, Santosh Panjikar, Yoshiaki Kitamura, Noriko Nakagawa, Akeo Shinkai, Seiki Kuramitsu, Shigeyuki Yokoyamaprotein was subjected to buffer exchange with 10 mM potassium phosphate buffer pH 7.0 and loaded onto a Bio-Scale CHT20-I column (Bio-Rad) preequilibrated with the same buffer. The protein bound to the column and eluted at 99.8 mM

(4) Crystallization and preliminary X-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensisActa Crystallographica Section F Structural Biology and Crystallization CommunicationsFebruary 1, 2007Ryota Katsumi, Yuichi Koga, Dong-Ju You, Hiroyoshi Matsumura, Kazufumi Takano, Shigenori Kanayafractions containing the protein were collected, dialyzed against 5 mM sodium phosphate pH 6.8 and applied onto a Bio-Scale CHT20-I column (Bio-Rad) equilibrated with the same buffer. The protein was eluted from the column with a linear gradient

(5) Purification, crystallization and preliminary crystallographic analysis of the putative thiamine-biosynthesis protein PH1313 from Pyrococcus horikoshii OT3Acta Crystallographica Section F Structural Biology and Crystallization CommunicationsJanuary 1, 2007Michihiro Sugahara, Satoko Murai, Mitsuaki Sugahara, Naoki KunishimaB and eluted with a linear gradient of 0–0.4 M NaCl in buffer B. The sample was then applied onto a Bio-Scale CHT20-I column (Bio-Rad) equilibrated with 10 mM potassium phosphate pH 7.0 and eluted with a linear gradient of 10–400

(6) Crystallization and preliminary crystallographic analysis of type 1 RNase H from the hyperthermophilic archaeon Sulfolobus tokodaii 7Acta Crystallographica Section F Structural Biology and Crystallization CommunicationsAugust 1, 2006Dong-Ju You, Hyongi Chon, Yuichi Koga, Kazufumi Takano, Shigenori KanayaSto-RNase HI were combined, dialyzed against buffer C (5 mM sodium phosphate pH 6.8) and loaded onto a Bio-Scale CHT20-I column (Bio-Rad) equilibrated with buffer C. The protein was eluted from the column with a linear gradient

Be the First to Write a Review!