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anti-Human Cathepsin L1 Antibodies:
anti-Mouse (Murine) Cathepsin L1 Antibodies:
anti-Rat (Rattus) Cathepsin L1 Antibodies:
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Human Monoclonal Cathepsin L1 Primary Antibody for ICC, IHC (fro) - ABIN151302
Igdoura, Morales, Hermo: Differential expression of cathepsins B and D in testis and epididymis of adult rats. in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society 1995
Show all 13 references for ABIN151302
Human Monoclonal Cathepsin L1 Primary Antibody for EIA, IHC (p) - ABIN317508
Klionsky: The molecular machinery of autophagy: unanswered questions. in Journal of cell science 2004
Show all 4 references for ABIN317508
Human Monoclonal Cathepsin L1 Primary Antibody for IF, WB - ABIN968359
Ishidoh, Kominami: Procathepsin L degrades extracellular matrix proteins in the presence of glycosaminoglycans in vitro. in Biochemical and biophysical research communications 1996
Show all 3 references for ABIN968359
Human Polyclonal Cathepsin L1 Primary Antibody for IHC, WB - ABIN222981
Song, Spencer, Bazer: Cathepsins in the ovine uterus: regulation by pregnancy, progesterone, and interferon tau. in Endocrinology 2005
Show all 2 references for ABIN222981
Mouse (Murine) Polyclonal Cathepsin L1 Primary Antibody for IP, ELISA - ABIN2000123
Dixit, Dixit, Sharma: Immunodiagnostic/protective role of cathepsin L cysteine proteinases secreted by Fasciola species. in Veterinary parasitology 2008
Human Polyclonal Cathepsin L1 Primary Antibody for IF (cc), IF (p) - ABIN687532
Hernáez, Guerra, Salas, Andrés: African Swine Fever Virus Undergoes Outer Envelope Disruption, Capsid Disassembly and Inner Envelope Fusion before Core Release from Multivesicular Endosomes. in PLoS pathogens 2016
These results suggest that an antipain-sensitive protease or cathepsin L (or a related protease) is a candidate for pp25 degradation.
interactions of human family 1 & 2 cystatins with cathepsin L1
cathepsin L and cathepsin B (show CTSB Antibodies) as the lysosomal cysteine proteases that activate the PEDV spike.
the crystal structure determined at 1.4 A revealed that the cathepsin L molecule is cleaved, with the cleaved region trapped in the active site cleft of the neighboring molecule.
Results showed an increase level of CTSL, and CTSB (show CTSB Antibodies) in dilated cardiomyopathy patients which correlates with reduced left ventricular ejection fraction.
endothelial CTSL up-regulation partially due to Fli1 (show FLI1 Antibodies) deficiency may contribute to the development of vasculopathy, while the decrease in dermal CTSL expression is likely associated with dermal fibrosis in systemic sclerosis
CTSL may contribute to gefitinib resistance in non-small-cell lung cancer
The study results indicate the A-allele of rs3118869 [of the human cathepsin Lgene] is a protective factor in hypertension.
Data suggest that nuclear cathepsin L accelerates cell cycle progression of HCT116 colorectal carcinoma cells.
Mechanistic studies showed that teicoplanin blocks Ebola virus entry by specifically inhibiting the activity of cathepsin L, opening a novel avenue for the development of additional glycopeptides as potential inhibitors of cathepsin L-dependent viruses.
Cathepsin L targeting in cancer treatment
findings suggest that single chain-cathepsin L is biologically active in promoting Th17 generation and is counter-regulated by serpinB1 (show SERPINB1 Antibodies) and secondarily by asparagine endopeptidase.
CTSL plays an important role in the MHC class II-mediated peptide presentation in thymic epithelial cells, acting both in the invariant chain degradation and in the generation of MHC class II-bound peptide ligands presented by cortical thymic epithelial cells. Consequently, CTSL plays an important role in the positive selection of CD4 (show CD4 Antibodies)+ T cell in thymus.
genetic blockade of cathepsin L activity is inferred to retard Myc (show MYC Antibodies)-driven tumor growth, encouraging the potential utility of pharmacological inhibitors of cysteine cathepsins in treating late stage tumors.
Double immunofluorescence analysis showed that CTLA-2alpha was co-localized with cathepsin L, cathepsin C (show CTSC Antibodies), and TINAGL1 (show TINAGL1 Antibodies) in placenta.
CtsB (show CTSB Antibodies) and CtsL are essential in alpha-syn lysosomal degradation
The phenotypes of cathepsin L deficiency can be fully assigned to lack of canonically targeted cathepsin L, while the biogenesis and functionality of nucleo-cytosolic cathepsin L remain elusive.
in vivo functional evidence for overexpressed CTSL as a promoter of lung metastasis, whereas high CTSL levels are maintained during tumor progression due to stress-resistant mRNA translation.
cathepsin L has a protective role in mouse skin carcinogenesis
Cathepsin L is involved in nociception in mice, whereas peripheral autophagy and cathepsin L contribute, at least in part, to the antinociceptive effect of dimethoxybenzylidene in mice.
a degradative Ctsl-MMP-2 axis, resulting in increased MMP-2 levels upon cathepsin deficiency with subsequent degradation of secreted proteins such as collagen alpha-1 (I).
Endosomal acidification and cathepsin L (show CTSL Antibodies) activity is required for porcine enteric calicivirus replication.
CTSL1 is expressed by endometrial epithelia, placental areolae, and neonatal intestine, and it may function in the transport of macromolecules across these epithelia.
These results, together with those previously reported for other genes of this family, suggest that cathepsin genes play a role in defining economically important traits in pigs.
The cathepsin L (show CTSL Antibodies) deserves further evaluation as therapeutic targets to develop disease modifying drugs to treat Alzheimer's disease.
Cathepsin L (show CTSL Antibodies) has an previously uncharacterized biological role in the production of [Met]enkephalin, an endogenous peptide neurotransmitter
Secretory vesicle function of cathepsin L (show CTSL Antibodies) for biosynthesis of active enkephalin opioid peptide contrasts with its function in lysosomes for protein degradation.
The protein encoded by this gene is a lysosomal cysteine proteinase that plays a major role in intracellular protein catabolism. Its substrates include collagen and elastin, as well as alpha-1 protease inhibitor, a major controlling element of neutrophil elastase activity. The encoded protein has been implicated in several pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. This protein, which is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. Multiple alternatively spliced transcript variants have been found for this gene.
, cathepsin L
, Cathepsin L1
, cathepsin L1-like
, major excreted protein
, Cat L
, p39 cysteine proteinase
, cyclic protein 2
, cathepsin L2 preproprotein