Rabbit Recombinant Monoclonal Cathepsin L/MEP antibody - conjugated to Alexa Fluor® 647.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Application | Reactivity | Dilution info | Notes |
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Application Target Binding Affinity | Reactivity Expected | Dilution info - | Notes - |
Application Antibody Labelling | Reactivity Expected | Dilution info - | Notes - |
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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).
CTSL1, CTSL, Procathepsin L, Cathepsin L1, Major excreted protein, MEP
Rabbit Recombinant Monoclonal Cathepsin L/MEP antibody - conjugated to Alexa Fluor® 647.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
Cathepsins L V K and H are essential cysteine proteases that serve important functions in protein catabolism. These proteases participate in proteolytic processes by digesting proteins into shorter peptides and amino acids. Cathepsin L also known as CTSL typically has a molecular mass of about 25-35 kDa and is expressed in various tissues such as the liver spleen and placenta. Cathepsin K plays a similar role in bone resorption and is highly expressed in osteoclasts. Cathepsin V and Cathepsin H meanwhile have distinct tissue distributions with cathepsin V often found in the thymus and testis whereas cathepsin H's expression spans across different cell types contributing a vast array of biological functions.
Cathepsins regulate cellular homeostasis and modulate various physiological processes. These proteases perform their functions within the lysosomal compartment although they can also participate in extracellular matrix remodeling and other non-lysosomal roles. Cathepsin K for example is part of the cathepsin protein family and aids in degrading collagen therefore playing a pivotal role in bone turnover and resorption. Cathepsins can act independently or in some cases are part of larger enzyme complexes enhancing their proteolytic activity to handle different substrates driven by the physiological demand.
Cathepsins key in the lysosomal degradation pathway and influence other signaling cascades like the apoptotic pathway. The regulation of these pathways often involves interactions with other proteins such as pro-apoptotic members of the Bcl-2 family facilitating cell death under certain conditions. Cathepsin L contributes to the antigen processing pathway linking it to the immune response. Cathepsin K on the other hand acts closely with structural proteins like collagen in the bone metabolism pathway highlighting its significance in skeletal development and maintenance.
Altered cathepsin activity closely associates with conditions like osteoporosis and cancer. Cathepsin K upregulation can lead to excessive bone degradation seen in osteoporosis while aberrant cathepsin L expression relates to cancer progression and metastasis due to its role in degrading extracellular matrix components facilitating tumor invasion. In osteoporosis interactions with matrix metalloproteinases further enhance bone matrix breakdown exacerbating disease symptoms. In cancer the relationship between cathepsin L and the urokinase-type plasminogen activator system highlights its role in promoting malignancy and suggests potential therapeutic targets.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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