Recombinant Borrelia burgdorferi ATP-dependent Clp protease proteolytic subunit 2(clpP2) CSB-EP528713BUD
Specifications
| 20ug / 100ug price = 20ug |
Alternative Name(s):
Endopeptidase Clp 2
Species: (Organism)
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Gene Names:
clpP2
Tag info:
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Target Protein AA Sequence:
MTGKEDNDACVLHDKSLKLVLKSRSIVIAGEITKDVSRLFQEKILLLEALDFKKPIFVYIDSEGGDIDAGFAIFNMIRFVKPKVFTVGVGLVASAAALIFLAAKLENRFSLPFARYLLHQPLSGFKGVATDIEIYTNELNKVKKELNNIISKETGQKISKIEKDTDRDFWLDSSAAKKYGLVFEVVETKYQLEEFISA
Expression Region:
1-198aa
Subcellular Location:
Cytoplasm
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
27.2 kDa
Purity:
Greater than 85% as determined by SDS-PAGE.
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.
Research Areas:
Others
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.
Involvement in disease:
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.
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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Peptidase S14 family
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)
