|Synonyms||Cathepsin L; CTSL; CTSL1|
|Description||Cathepsin L, also known as Aldrichina grahami cysteine proteinase, is an important lysosomal endopeptidase enzyme which is involved in the initiation of protein degradation. It is a member of the Peptidase C1 family, which play an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis. Cathepsin L has also been shown to proteolytically inactivate α-1-antitrypsin and secretory leucoprotease inhibitor, two major protease inhibitors of the respiratory tract. Cathepsin L expression has been reported in many organisms including fish, birds and mammals.
Recombinant Human Cathepsin L produced in CHO cells is a polypeptide chain containing 227 amino acids. A fully biologically active molecule, rhCathepsin L has a molecular mass of 40 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.
|Biological Activity||The Specific Activity is > 2000 pmol/min/μg, measured by Cathepsin L’s ability to cleave the fluorogenic peptide substrate Z-FR-AMC (Enzo, Catalog: P139).
Assay buffer: 400 mM sodium acetate, pH5.5,4 mM EDTA, 8 mM DTT
EAPRSVDWRE KGYVTPVKNQ GQCGSCWAFS ATGALEGQMF
RKTGRLISLS EQNLVDCSGP QGNEGCNGGL MDYAFQYVQD
NGGLDSEESY PYEATEESCK YNPKYSVAND TGFVDIPKQE
KALMKAVATV GPISVAIDAG HESFLFYKEG IYFEPDCSSE
DMDHGVLVVG YGFESTESDN NKYWLVKNSW GEEWGMGGYV
KMAKDRRNHC GIASAASYPT VHHHHHH
|Measured Molecular Weight||40 kDa, observed by reducing SDS-PAGE.|
|Purity||> 95% as analyzed by SDS-PAGE & HPLC.|
|Formulation||Liquid after a 0.2 μm filtered solution in 50 mM NaOAc, 50 mM NaCl, 20% Glycerol, pH 6.0.|
|Endotoxin Level||< 0.2 EU/μg, determined by LAL method.|
|Storage||Recombinant Human Cathepsin L remains stable up to 6 months at lower than -70°C from date of receipt under sterile conditions. Up to 3 months at lower than -70°C under sterile conditions after opening. Avoid repeated freeze-thaw cycles.|
|Note||For research use only|
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