ATP-dependent Clp protease proteolytic subunit 2 (clpP2), Borrelia burgdorferi, recombinant

Organism: Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680). Source: E.coli. Expression Region: 1-198aa. Protein Length: Full Length. Tag Info: N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged. Target Protein Sequence: MTGKEDNDAC VLHDKSLKLV LKSRSIVIAG EITKDVSRLF QEKILLLEAL DFKKPIFVYI DSEGGDIDAG FAIFNMIRFV KPKVFTVGVG LVASAAALIF LAAKLENRFS LPFARYLLHQ PLSGFKGVAT DIEIYTNELN KVKKELNNII SKETGQKISK IEKDTDRDFW LDSSAAKKYG LVFEVVETKY QLEEFISA. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Reference: "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. Venter J.C. Nature 390:580-586(1997). Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.