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Rat Anti-CTSL Recombinant Antibody (CBFYC-2456) (CBMAB-C2529-FY)

This product is rat antibody that recognizes CTSL. The antibody CBFYC-2456 can be used for immunoassay techniques such as: IHC, IP, WB.
See all CTSL antibodies

Summary

Host Animal
Rat
Specificity
Human, Mouse
Clone
CBFYC-2456
Antibody Isotype
IgG2a
Application
IHC, IP, WB

Basic Information

Immunogen
Mouse myeloma cell line NS0-derived recombinant human Cathepsin L Glu113-Val333
Specificity
Human, Mouse
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 5% trehalose
Concentration
0.5 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Cathepsin L
Introduction
CTSL (Cathepsin L) is a Protein Coding gene. Diseases associated with CTSL include Tracheal Cancer and Eccrine Acrospiroma. Among its related pathways are Bacterial infections in CF airways and Primary Focal Segmental Glomerulosclerosis FSGS. Gene Ontology (GO) annotations related to this gene include histone binding and cysteine-type peptidase activity. An important paralog of this gene is CTSV.
Entrez Gene ID
Human1514
Mouse13039
UniProt ID
HumanP07711
MouseP06797
Alternative Names
Cathepsin L; Major Excreted Protein; Cathepsin L1; EC 3.4.22.15; CTSL1; MEP; EC 3.4.22; CATL
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).

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).

(Microbial infection) Facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via proteolysis of coronavirus spike (S) glycoproteins in lysosome for entry into host cell (PubMed:32142651, PubMed:32221306, PubMed:16339146, PubMed:18562523).

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:26953343, PubMed:18562523).
Biological Process
Adaptive immune response Source: UniProtKB
Antigen processing and presentation Source: UniProtKB
Antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
Antigen processing and presentation of peptide antigen Source: UniProtKB
CD4-positive, alpha-beta T cell lineage commitment Source: UniProtKB
Cellular response to thyroid hormone stimulus Source: UniProtKB
Collagen catabolic process Source: UniProtKB
Elastin catabolic process Source: UniProtKB
Enkephalin processing Source: UniProtKB
Extracellular matrix disassembly Source: Reactome
Fusion of virus membrane with host endosome membrane Source: UniProtKB
Fusion of virus membrane with host plasma membrane Source: UniProtKB
Immune response Source: GO_Central
Macrophage apoptotic process Source: BHF-UCL
Protein autoprocessing Source: UniProtKB
Proteolysis Source: UniProtKB
Proteolysis involved in cellular protein catabolic process Source: BHF-UCL
Receptor-mediated endocytosis of virus by host cell Source: UniProtKB
Regulation of keratinocyte differentiation Source: Reactome
Toll-like receptor signaling pathway Source: Reactome
Viral entry into host cell Source: UniProtKB
Zymogen activation Source: UniProtKB
Cellular Location
Extracellular space; Secreted; Lysosome; Apical cell membrane; Chromaffin granule. Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages.
Isoform 2: Nucleus. Translation initiation at downstream start sites allows the synthesis of isoforms that are devoid of a signal peptide and do not transit through the endoplasmic reticulum to localize to the nucleus (PubMed:15099520). Nuclear location varies during the cell cycle, whith higher levels during S phase (PubMed:15099520).
PTM
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).

Zhao, M. M., Yang, W. L., Yang, F. Y., Zhang, L., Huang, W. J., Hou, W., ... & Yang, J. K. (2021). Cathepsin L plays a key role in SARS-CoV-2 infection in humans and humanized mice and is a promising target for new drug development. Signal transduction and targeted therapy, 6(1), 1-12.

Thirusangu, P., Pathoulas, C. L., Ray, U., Xiao, Y., Staub, J., Jin, L., ... & Shridhar, V. (2021). Quinacrine-induced autophagy in ovarian cancer triggers cathepsin-l mediated lysosomal/mitochondrial membrane permeabilization and cell death. Cancers, 13(9), 2004.

Wang, Z., Xiang, Z., Zhu, T., Chen, J., Zhong, M. Z., Huang, J., ... & Zhou, W. B. (2020). Cathepsin L interacts with CDK2‑AP1 as a potential predictor of prognosis in patients with breast cancer. Oncology letters, 19(1), 167-176.

Chen, J., Zhang, L., Yang, N., Cao, M., Tian, M., Fu, Q., ... & Li, C. (2020). Characterization of the immune roles of cathepsin L in turbot (Scophthalmus maximus L.) mucosal immunity. Fish & Shellfish Immunology, 97, 322-335.

Fei, Y., Xiong, Y., Shen, X., Zhao, Y., Zhu, Y., Wang, L., & Liang, Z. (2018). Cathepsin L promotes ionizing radiation-induced U251 glioma cell migration and invasion through regulating the GSK-3β/CUX1 pathway. Cellular signalling, 44, 62-71.

Zhao, Y. F., Han, M. L., Xiong, Y. J., Wang, L., Fei, Y., Shen, X., ... & Liang, Z. Q. (2018). A miRNA-200c/cathepsin L feedback loop determines paclitaxel resistance in human lung cancer A549 cells in vitro through regulating epithelial–mesenchymal transition. Acta pharmacologica Sinica, 39(6), 1034-1047.

Xu, S., Zhang, H., Yang, X., Qian, Y., & Xiao, Q. (2018). Inhibition of cathepsin L alleviates the microglia-mediated neuroinflammatory responses through caspase-8 and NF-κB pathways. Neurobiology of Aging, 62, 159-167.

Pandey, G., Bakhshi, S., Thakur, B., Jain, P., & Chauhan, S. S. (2018). Prognostic significance of cathepsin L expression in pediatric acute myeloid leukemia. Leukemia & Lymphoma, 59(9), 2175-2187.

Manchanda, M., Das, P., Gahlot, G. P., Singh, R., Roeb, E., Roderfeld, M., ... & Chauhan, S. S. (2017). Cathepsin L and B as potential markers for liver fibrosis: insights from patients and experimental models. Clinical and translational gastroenterology, 8(6), e99.

Mehra, S., Kumar, M., Manchanda, M., Singh, R., Thakur, B., Rani, N., ... & Chauhan, S. S. (2017). Clinical significance of cathepsin L and cathepsin B in dilated cardiomyopathy. Molecular and cellular biochemistry, 428(1), 139-147.

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For research use only. Not intended for any clinical use.

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