Cathepsin S (CTSS), human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 115-331aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-tagged. Target Protein Sequence: LPDSVDWREK GCVTEVKYQG SCGACWAFSA VGALEAQLKL KTGKLVSLSA QNLVDCSTEK YGNKGCNGGF MTTAFQYIID NKGIDSDASY PYKAMDQKCQ YDSKYRAATC SKYTELPYGR EDVLKEAVAN KGPVSVGVDA RHPSFFLYRS GVYYEPSCTQ NVNHGVLVVG YGDLNGKEYW LVKNSWGHNF GEEGYIRMAR NKGNHCGIAS FPSYPEI. 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: Thiol protease. Key protease responsible for the roval of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N. Reference: Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease.Shi G.-P., Munger J.S., Meara J.P., Rich D.H., Chapman H.A.J. Biol. Chem. 267:7258-7262(1992). Function: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.