Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species
Yamada, Ishimaru, Arakaki, Katunuma, Hayashi: Cathepsin L inhibition prevents murine autoimmune diabetes via suppression of CD8(+) T cell activity. in PLoS ONE 2010
Show all 3 references for ABIN411884
Human Cathepsin L1 ELISA Kit for Sandwich ELISA - ABIN414965
Zhang, Wang, Huang, Li, Zhu, Luo, Shi, Li: Plasma cathepsin L and its related pro/antiangiogenic factors play useful roles in predicting rich coronary collaterals in patients with coronary heart disease. in The Journal of international medical research 2010
Show all 2 references for ABIN414965
Rat (Rattus) Cathepsin L1 ELISA Kit for Sandwich ELISA - ABIN416447
Bauer, Hess, Qiu, Klenk, Renault, Wanner, Studer, Killer, Stalder, Stritt, Strasser, Farine, Kauser, Clozel, Fischli, Nayler: Identification of cathepsin L as a potential sex-specific biomarker for renal damage. in Hypertension 2011
These results suggest that an antipain-sensitive protease or cathepsin L (or a related protease) is a candidate for pp25 degradation.
Results showed an increase level of CTSL, and CTSB (show CTSB ELISA Kits) in dilated cardiomyopathy patients which correlates with reduced left ventricular ejection fraction.
endothelial CTSL up-regulation partially due to Fli1 (show FLI1 ELISA Kits) 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
cathepsin L activity was decreased in p53 (show TP53 ELISA Kits) positive cells after adriamycin treatment, but not in p53 (show TP53 ELISA Kits) 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 ELISA Kits) fragment is also shown to reduce the secretion of interleukin-12 (IL-12 (show IL12A ELISA Kits)/p70 (show ANXA6 ELISA Kits)) during the subsequent maturation of treated dendritic cells.
findings suggest that single chain-cathepsin L is biologically active in promoting Th17 generation and is counter-regulated by serpinB1 (show SERPINB1 ELISA Kits) 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 ELISA Kits)+ T cell in thymus.
genetic blockade of cathepsin L activity is inferred to retard Myc (show MYC ELISA Kits)-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 ELISA Kits), and TINAGL1 (show TINAGL1 ELISA Kits) in placenta.
CtsB (show CTSB ELISA Kits) 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 ELISA Kits) 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 ELISA Kits) deserves further evaluation as therapeutic targets to develop disease modifying drugs to treat Alzheimer's disease.
Cathepsin L (show CTSL ELISA Kits) has an previously uncharacterized biological role in the production of [Met]enkephalin, an endogenous peptide neurotransmitter
Secretory vesicle function of cathepsin L (show CTSL ELISA Kits) 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