Rabbit Polyclonal Cathepsin L/MEP antibody. Suitable for IHC - Wmt and reacts with Zebrafish samples. Immunogen corresponding to Recombinant Fragment Protein within Human CTSL aa 1 to C-terminus.
IgG
Rabbit
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 79.99% PBS, 20% Glycerol (glycerin, glycerine)
Liquid
Polyclonal
IHC - Wmt | |
---|---|
Zebrafish | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Zebrafish | Dilution info 1/100.00000 - 1/500.00000 | Notes - |
Select an associated product type
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 2Functions 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).
CTSL1, CTSL1, CTSL, Procathepsin L, Cathepsin L1, Major excreted protein, MEP
Rabbit Polyclonal Cathepsin L/MEP antibody. Suitable for IHC - Wmt and reacts with Zebrafish samples. Immunogen corresponding to Recombinant Fragment Protein within Human CTSL aa 1 to C-terminus.
IgG
Rabbit
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 79.99% PBS, 20% Glycerol (glycerin, glycerine)
Liquid
Polyclonal
Affinity purification Immunogen
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
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This supplementary information is collated from multiple sources and compiled automatically.
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.
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.
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.
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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Immunohistochemical analysis (whole mount) of paraformaldehyde-fixed Zebrafish embryo, labeling Cathepsin L/MEP with ab209708 at 1/200 dilution.
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