Recombinant human Cathepsin L/MEP protein is a Human Full Length protein, in the 18 to 333 aa range, expressed in Mammalian, with >80% purity and suitable for SDS-PAGE, FuncS.
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Key facts
- Purity
- >80% SDS-PAGE
- Expression system
- Mammalian
- Tags
- His tag C-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
Amino acid sequence
T L T F D H S L E A Q W T K W K A M H N R L Y G M N E E G W R R A V W E K N M K M I E L H N Q E Y R E G K H S F T M A M N A F G D M T S E E F R Q V M N G F Q N R K P R K G K V F Q E P L F Y E A P R S V D W R E K G Y V T P V K N Q G Q C G S C W A F S A T G A L E G Q M F R K T G R L I S L S E Q N L V D C S G P Q G N E G C N G G L M D Y A F Q Y V Q D N G G L D S E E S Y P Y E A T E E S C K Y N P K Y S V A N D T G F V D I P K Q E K A L M K A V A T V G P I S V A I D A G H E S F L F Y K E G I Y F E P D C S S E D M D H G V L V V G Y G F E S T E S D N N K Y W L V K N S W G E E W G M G G Y V K M A K D R R N H C G I A S A A S Y P T V
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Target data
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).
Alternative names
CTSL1, CTSL, Procathepsin L, Cathepsin L1, Major excreted protein, MEP
Recommended products
Recombinant human Cathepsin L/MEP protein is a Human Full Length protein, in the 18 to 333 aa range, expressed in Mammalian, with >80% purity and suitable for SDS-PAGE, FuncS.
Key facts
- Purity
- >80% SDS-PAGE
- Expression system
- Mammalian
- Tags
- His tag C-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
- Biological activity
- Specific Activity: ≥ 990 pmol/min/μg
- Accession
- P07711-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Preservative: 1.36% Imidazole
Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride
Sequence info
Amino acid sequence
- T L T F D H S L E A Q W T K W K A M H N R L Y G M N E E G W R R A V W E K N M K M I E L H N Q E Y R E G K H S F T M A M N A F G D M T S E E F R Q V M N G F Q N R K P R K G K V F Q E P L F Y E A P R S V D W R E K G Y V T P V K N Q G Q C G S C W A F S A T G A L E G Q M F R K T G R L I S L S E Q N L V D C S G P Q G N E G C N G G L M D Y A F Q Y V Q D N G G L D S E E S Y P Y E A T E E S C K Y N P K Y S V A N D T G F V D I P K Q E K A L M K A V A T V G P I S V A I D A G H E S F L F Y K E G I Y F E P D C S S E D M D H G V L V V G Y G F E S T E S D N N K Y W L V K N S W G E E W G M G G Y V K M A K D R R N H C G I A S A A S Y P T V
- Accession
- P07711
- Protein length
- Full Length
- Predicted molecular weight
- 36 kDa
- Amino acids
- 18 to 333
- Nature
- Recombinant
- Tags
- His tag C-Terminus
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).
- 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, Nucleus
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
- Storage information
- Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Notes
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.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Cathepsin L also known as CTSL is a protease enzyme that has a mass of approximately 29-30 kDa. It originates from the peptidase C1 family and undergoes activation in acidic environments. This protein carries out proteolytic processes by breaking down proteins through cleaving peptide bonds. Cathepsin L has various forms including MEP (a common alternate name) and MEP L and it expresses itself in organs such as the liver kidney and spleen as well as in tumors and immune cells. It has a significant functional role in lysosomes where it degrades proteins.
- 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.
- Associated diseases and disorders
Cathepsin L connects strongly to cancer and fibrotic diseases. It contributes to tumor progression and metastasis due to its ability to degrade the extracellular matrix and enable cancer cell invasion. In fibrosis cathepsin L modulates the turnover of fibrous tissue linking to the development of lung fibrotic diseases. Proteins like collagenases work in concert with cathepsin L during these pathological processes to remodel tissues underlining its implication in disease states.
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2 product images
SDS-PAGE - Recombinant human Cathepsin L/MEP protein (ab198444)
10% SDS-PAGE of 2.5μg ab198444.
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.
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