Abbreviation
Recombinant Human CTSL protein (Active)
Purity
Greater than 90% as determined by SDS-PAGE.
Endotoxin
Less than 1.0 EU/ug as determined by LAL method.
Activity
Measured by its ability to cleave the fluorogenic peptide substrate Z-LR-AMC, The specific activity is >32000 pmol/ min/μg.
Alternative Names
Procathepsin L; EC:3.4.22.15; Cathepsin L1; Major excreted protein (MEP); CTSL; CTSL1
Species
Homo sapiens (Human)
Expression Region
18-333aa
Target Protein Sequence
TLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV
Note: The complete
sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is
translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application,
please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
Full Length
Tag Info
C-terminal 10xHis-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
Lyophilized from a 0.2 μm sterile filtered 50 mM NaAc, 0.5 M NaCl, 6% Trehalose, pH 4.5
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 Condition
Store at -20°C/-81°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Lead Time
3-7 business days
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Shelf Life
The shelf life is related to many factors, storage state, storage temperature and the stability of the product itself. Generally, the shelf life of lyophilized form is 6 months at -20°C/-80°C from the date of receipt.
Datasheet & COA
Please contact us to get it.
Images
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(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Activity
Measured by its ability to cleave the fluorogenic peptide substrate Z-LR-AMC, The specific activity is >32000 pmol/ min/μg.
Description
Cathepsin L plays a central role in lysosomal protein degradation and has been implicated in neurodegeneration, autophagy dysregulation, and extracellular matrix remodeling. This full-length procathepsin L (aa 18–333) demonstrates robust proteolytic activity with a specific activity exceeding 32,000 pmol/min/μg against the fluorogenic substrate Z-LR-AMC, providing a quantitative benchmark for enzyme kinetics studies and inhibitor screening assays. Mammalian cell expression preserves native glycosylation and folding, which are critical for proper zymogen activation and substrate recognition in functional assays. With greater than 90% purity and endotoxin levels below 1.0 EU/μg, this preparation meets the quality thresholds commonly required for cell-based proteolysis assays, autophagy flux measurements, and biochemical characterization of cathepsin L activation mechanisms in neuroscience research.
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