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The protein encoded by CTSL1 is a lysosomal cysteine proteinase that plays a major role in intracellular protein catabolism. Additionally we are shipping Cathepsin L1 Antibodies (184) and Cathepsin L1 Kits (75) and many more products for this protein.
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Human Cathepsin L1 Protein expressed in Human Cells - ABIN2002949
Mason, Wilcox, Wikstrom, Shaw: The identification of active forms of cysteine proteinases in Kirsten-virus-transformed mouse fibroblasts by use of a specific radiolabelled inhibitor. in The Biochemical journal 1989
Show all 5 references for ABIN2002949
Mouse (Murine) Cathepsin L1 Protein expressed in Human Cells - ABIN2007149
Chauhan, Goldstein, Gottesman: Expression of cathepsin L in human tumors. in Cancer research 1991
Show all 5 references for ABIN2007149
Human Cathepsin L1 Protein expressed in HEK-293 Cells - ABIN2180948
Goretzki, Schmitt, Mann, Calvete, Chucholowski, Kramer, Günzler, Jänicke, Graeff: Effective activation of the proenzyme form of the urokinase-type plasminogen activator (pro-uPA) by the cysteine protease cathepsin L. in FEBS letters 1992
Show all 2 references for ABIN2180948
These results suggest that an antipain-sensitive protease or cathepsin L (or a related protease) is a candidate for pp25 degradation.
Cathepsin L targeting in cancer treatment
cathepsin L activity was decreased in p53 (show TP53 Proteins) positive cells after adriamycin treatment, but not in p53 (show TP53 Proteins) negative cells.
these data indicate that the CTSL inhibitor KGP94 has the potential to alleviate metastatic disease progression and associated skeletal morbidities and hence may have utility in the treatment of advanced prostate cancer patients
p41 (show EPB41 Proteins) fragment is also shown to reduce the secretion of interleukin-12 (IL-12 (show IL12A Proteins)/p70 (show ANXA6 Proteins)) during the subsequent maturation of treated dendritic cells.
Our findings highlight the potential role of CTSL in the cross talk between autophagy and apoptosis, which might be considered a therapeutic strategy for treatment of pathologic conditions associated with neurodegeneration.
Knockdown of Cathepsin L promotes radiosensitivity of glioma stem cells both in vivo and in vitro.
shedding of surface proteins by extracellular cathepsins impacts intracellular signaling as demonstrated for regulation of Ras GTPase (show RACGAP1 Proteins) activity.
Cathepsins in Rotator Cuff Tendinopathy: Identification in Human Chronic Tears and Temporal Induction in a Rat Model.
In addition, cathepsin L positively correlates with MMP2 (show MMP2 Proteins). PRACTICE: The cathepsin L may be used as a monitoring index in age-related diseases.
TGFbetainduced epithelialmesenchymal transition was associated with increased cathepsin L in A549 and MCF7 cells. CATL may be involved in the regulation of EMT (show ITK Proteins). CATL knockdown in A549 cells inhibited xenograft tumor growth and EMT (show ITK Proteins) in vivo
findings suggest that single chain-cathepsin L is biologically active in promoting Th17 generation and is counter-regulated by serpinB1 (show SERPINB1 Proteins) 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 Proteins)+ T cell in thymus.
genetic blockade of cathepsin L activity is inferred to retard Myc (show MYC Proteins)-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 Proteins), and TINAGL1 (show TINAGL1 Proteins) in placenta.
CtsB (show CTSB Proteins) 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 Proteins) 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 Proteins) deserves further evaluation as therapeutic targets to develop disease modifying drugs to treat Alzheimer's disease.
Cathepsin L (show CTSL Proteins) has an previously uncharacterized biological role in the production of [Met]enkephalin, an endogenous peptide neurotransmitter
Secretory vesicle function of cathepsin L (show CTSL Proteins) 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