Cathepsin K (Ctsk), mouse, recombinant

Organism: Mus musculus (Mouse). Source: E.coli. Expression Region: 115-329aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-tagged. Target Protein Sequence: VPDSIDYRKK GYVTPVKNQG QCGSCWAFSS AGALEGQLKK KTGKLLALSP QNLVDCVTEN YGCGGGYMTT AFQYVQQNGG IDSEDAYPYV GQDESCMYNA TAKAAKCRGY REIPVGNEKA LKRAVARVGP ISVSIDASLA SFQFYSRGVY YDENCDRDNV NHAVLVVGYG TQKGSKHWII KNSWGESWGN KGYALLARNK NNACGITNMA SFPKM. Purity: Greater than 90% 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: Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone rodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in Extracellular domain matrix degradation . Reference: Complete genomic structure of the mouse cathepsin K gene (Ctsk) and its localization next to the Arnt gene on mouse chromosome 3.Rantakokko J.A., Kiviranta R., Eerola R., Aro H.T., Vuorio E.Matrix Biol. 18:155-161(1999). Function: Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation (By similarity).