Columns for folding soluble proteins

Spin-Column Protein Folding Screen Kit  (Catalog #:  SFC01-10)                               

The Spin-Column Protein Folding Screen Kit is an easy-to-use and effective tool for optimization of protein folding conditions.  The screen kit includes reagents and 10 different protein folding spin-columns (Column #1 to Column #10). The 10 different columns represent the 10 most promising folding conditions.  Following is a list of publications using the protein folding columns.

 

Small-Scale Preparative Protein Folding Column Set

The Small-Scale Preparative Protein Folding Column Set  is designed for small-scale (0.6 - 1.2 mg) preparative protein folding experiments after the optimal folding condition has been identified from the Spin-Column Protein Folding Screen Kit (SFC01-10).  The column set  includes reagents and 10 identical protein folding spin-columns.  The columns are identical to one of the 10 columns in the screen kit.  The catalog numbers for different column numbers are:

SFC01  (column #1)   SFC02  (column #2)   SFC03  (column #3)  SFC04  (column #4)   SFC05  (column #5)              

SFC06  (column #6)   SFC07  (column #7)   SFC08  (column #8)  SFC09  (column #9)   SFC10  (column #10)

 

Large-Scale Preparative Protein Folding Column Set

The Large-Scale Preparative Protein Folding Column Set  is designed for large-scale (5 -10 mg) preparative protein folding experiments after the optimal folding condition has been identified by the Spin-Column Protein Folding Screen Kit (SFC01-10).  The column set includes 4 identical preparative protein folding columns and reagents.  The buffer condition of each column is identical to one of the 10 columns in the screen kit. The catalog numbers for different column numbers are:

PFC01  (column #1)   PFC02  (column #2)   PFC03  (column #3)   PFC04  (column #4)   PFC05 (column #5)                

PFC06  (column #6)   PFC07  (column #7)   PFC08  (column #8)   PFC09 (column #9)    PFC10  (column #10)

 

References:

  1. Kuznetsova VE et al, Genome-wide Analysis of Substrate Specificities of the Escherichia coli Haloacid Dehalogenase-like Phosphatase Family,  J. Biol. Chem. VOL.  281, NO. 47, pp. 36149–36161 (2006).
  2. Cha J et al, Characterization of the β-Lactam Antibiotic Sensor Domain of the MecR1 Signal Sensor/Transducer Protein from Methicillin-Resistant Staphylococcus aureus,  Biochemistry, 46 (26), pp 7822–7831 (2007).
  3. Hao X et al, Overexpression and Purif ication of Membrane Transport Protein with Native Functions,  Chinese J. Bioch. Mol. Biol. 23:12, 1051-1058 (2007).
  4. Thomas J et al, Acyl Carrier Protein Phosphodiesterase (AcpH) of Escherichia coli Is a Non-Canonical Member of the HD Phosphatase/Phosphodiesterase Family  Biochemistry, 46, 129-136 (2007).
  5. Cha J et al, Lysine N-Decarboxylation in the BlaR1 Protein from Staphylococcus Aureus at the Root of Its Function As an Antibiotic Sensor J. Am. Chem. Soc., 129 (13), pp 3834–3835 (2007).
  6. Kuznetsova E. Activity-based functional annotation of unknown proteins: HAD-like hydrolases, University of Toronto, Graduate thesis, (2009).
  7. Miller PS. Kinetic and Structural Studies on the First Three Enzymes in Bacillus Anthracis Isoprenoid Biosynthesis, ProQuest LLC, Ann Arber, P133 (2009).
  8. Duk-Hee  K et al, Novel dual-binding function of a poly (C)-binding protein 3, transcriptional factor which binds the double-strand and single-stranded DNA sequence, Gene, 501 (1), p.33-38, (2012).
  9. Copeland DL. Production of Recombinant Carp Leptin And its Effects on Lipid Metabolism in the Common Carp (Cyprinus Carpio), Thesis, The University of Akron (2012).
  10. Morrow KJ. The New Generation of Antibody Therapeutics:Current Status and Future Prospects,Insight Reports, Cambridge Healthtech Institute, Page 84, (2012)
  11. Kang DH. Novel function of the poly(c)-binding protein α-CP2 as a transcriptional activator that binds to single-stranded DNA sequences, International Journal of Molecular Medicine, Vol 32 (5): 1187-1194 (2013).
  12. Lee DS et al, Differential regulation of mouse and human Mu opioid receptor gene depends on the single stranded DNA structure of its promoter and α-complex protein 1. Biomedical Reports (2017).