Recombinant human Cathepsin L/MEP protein
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(2 Publications)
Recombinant human Cathepsin L/MEP protein is a Human Full Length protein, in the 18 to 333 aa range, expressed in Mammalian, with >80%, suitable for SDS-PAGE, FuncS.
View Alternative Names
CTSL1, CTSL, Procathepsin L, Cathepsin L1, Major excreted protein, MEP
- FuncS
Supplier Data
Functional Studies - Recombinant human Cathepsin L/MEP protein (AB198444)
Functional studies of ab198444. Specific Activity : 990 pmol/min/μg. Assay condition : Z-Leu-Arg-AMC (20 μM) was used as a substrate.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human Cathepsin L/MEP protein (AB198444)
10% SDS-PAGE of 2.5μg ab198444.
Reactivity data
Product details
Expressed in FreeStyle 293-F cells.
Useful for activation of DPP1 (Cathepsin C). Suitable for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Cathepsin L links to cellular homeostasis and extracellular matrix remodeling. It often acts in protein turnover and antigen processing within endolysosomal compartments making it essential for major histocompatibility complex class II presentation. Cathepsin L forms complexes in certain conditions playing roles in interacting and modifying other proteins. It controls processes essential for cell survival differentiation and apoptosis.
Pathways
Cathepsin L plays significant roles in pathways like apoptosis and autophagy. It coordinates with other proteases and proteins such as cathepsin B and cathepsin S to regulate cell death and survival. In apoptosis cathepsin L mediates the breakdown of cellular components working alongside caspases. Its interaction with autophagy involves degradation of long-lived proteins highlighting its role in recycling amino acids during stress conditions.
Specifications
Form
Liquid
General info
Function
Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells (By similarity). Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (PubMed : 10716919). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity).. (Microbial infection) In cells lacking TMPRSS2 expression, facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via a slow acid-activated route with the proteolysis of coronavirus spike (S) glycoproteins in lysosome for entry into host cell (PubMed : 16339146, PubMed : 18562523, PubMed : 32142651, PubMed : 32221306, PubMed : 37990007). Proteolysis within lysosomes is sufficient to activate membrane fusion by coronaviruses SARS-CoV and EMC (HCoV-EMC) S as well as Zaire ebolavirus glycoproteins (PubMed : 16081529, PubMed : 18562523, PubMed : 26953343).. Isoform 2. Functions in the regulation of cell cycle progression through proteolytic processing of the CUX1 transcription factor (PubMed : 15099520). Translation initiation at downstream start sites allows the synthesis of isoforms that are devoid of a signal peptide and localize to the nucleus where they cleave the CUX1 transcription factor and modify its DNA binding properties (PubMed : 15099520).
Sequence similarities
Belongs to the peptidase C1 family.
Post-translational modifications
During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (By similarity). Autocleavage; produces the single-chain CTSL after cleavage of the propeptide. The cleavage can be intermolecular (PubMed:9468501).
Subcellular localisation
Lysosome
Target data
Publications (2)
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International journal of biological sciences 20:3863-3880 PubMed39113716
2024
Applications
Unspecified application
Species
Unspecified reactive species
Cell proliferation 57:e13526 PubMed37417221
2023
Applications
Unspecified application
Species
Unspecified reactive species
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