E. coli DnaK (Amino residues 508-638)

<strong>E. coli DnaK (Amino residues 508-638)</strong>_x000D_ <strong>Catalog number:</strong> B2015022_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 20 ug_x000D_ <strong>Molecular Weight or Concentration:</strong> 14.6 kDa_x000D_ <strong>Supplied as:</strong> Liquid_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20° C_x000D_ <strong>Keywords:</strong> Chaperone Protein DnaK, HSP70, Heat Shock 70 kDa Protein, Heat Shock Protein 70, DnaK, GroP, GrpF_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Knappe D, Goldbach T, Hatfield MP, Palermo NY, Weinert S, Sträter N, Hoffmann R, Lovas S. Proline-rich Antimicrobial Peptides Optimized for Binding to Escherichia coli Chaperone DnaK Protein Pept Lett. 2016;23(12):1061-1071._x000D_ 2: Yoshimune K, Galkin A, Kulakova L, Yoshimura T, Esaki N. DnaK from Vibrio proteolyticus: complementation of a dnaK-null mutant of Escherichia coli and the role of its ATPase domain J Biosci Bioeng. 2005 Feb;99(2):136-42._x000D_ 3: Paek KH, Walker GC. Escherichia coli dnaK null mutants are inviable at high temperature J Bacteriol. 1987 Jan;169(1):283-90._x000D_ 4: McCarty JS, Rüdiger S, Schönfeld HJ, Schneider-Mergener J, Nakahigashi K, Yura T, Bukau B. Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria J Mol Biol. 1996 Mar 15;256(5):829-37._x000D_ 5: Rockabrand D, Livers K, Austin T, Kaiser R, Jensen D, Burgess R, Blum P. Roles of DnaK and RpoS in starvation-induced thermotolerance of Escherichia coli J Bacteriol. 1998 Feb;180(4):846-54._x000D_ 6: James R, Dean DO, Debbage J. Five open reading frames upstream of the dnaK gene of E. coli DNA Seq. 1993;3(5):327-32._x000D_ 7: Zhao L, Vecchi G, Vendruscolo M, Körner R, Hayer-Hartl M, Hartl FU. The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli Cell Rep. 2019 Jul 30;28(5):1335-1345.e6._x000D_ 8: Fatima K, Naqvi F, Younas H. A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins Cell Biochem Biophys. 2021 Jun;79(2):153-174._x000D_ 9: Doyle SM, Hoskins JR, Kravats AN, Heffner AL, Garikapati S, Wickner S. Intermolecular Interactions between Hsp90 and Hsp70 J Mol Biol. 2019 Jul 12;431(15):2729-2746._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/2522091">10: Johnson C, Chandrasekhar GN, Georgopoulos C. Escherichia coli DnaK and GrpE heat shock proteins interact both in vivo and in vitro J Bacteriol. 1989 Mar;171(3):1590-6. </a>_x000D_ _x000D_ <strong>Products Related to E. coli DnaK (Amino residues 508-638) can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>