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Ha, Martins, Khazaie, Han, Chan, Kim: Cathepsin B is involved in the trafficking of TNF-alpha-containing vesicles to the plasma membrane in macrophages. in Journal of immunology (Baltimore, Md. : 1950) 2008
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Unno, Wakamori, Koike, Uchiyama, Ishikawa, Kubota, Yoshida, Sasakawa, Peters, Mizusawa, Watase: Development of Purkinje cell degeneration in a knockin mouse model reveals lysosomal involvement in the pathogenesis of SCA6. in Proceedings of the National Academy of Sciences of the United States of America 2012
Vidal, Aguiar, Phansalkar, McAlpine, Napolitano, Chen, Araújo, Pauli, Bedran-Russo: Galloyl moieties enhance the dentin biomodification potential of plant-derived catechins. in Acta biomaterialia 2014
Human Cathepsin B ELISA Kit for Sandwich ELISA - ABIN2683959
Mueller-Steiner, Zhou, Arai, Roberson, Sun, Chen, Wang, Yu, Esposito, Mucke, Gan: Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease. in Neuron 2006
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Mouse (Murine) Cathepsin B ELISA Kit for Sandwich ELISA - ABIN2683961
Chan, San Segundo, McCormick, Steiner: Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. in Proceedings of the National Academy of Sciences of the United States of America 1986
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Cathepsin B is involved in the programmed cell death of the fat body during B. mori metamorphosis, and that cathepsin B and cathepsin B contribute to B (show TDO2 ELISA Kits). mori metamorphosis.
in CTSB knockout (KO) mice, running did not enhance adult hippocampal neurogenesis and spatial memory function. Interestingly, in Rhesus monkeys and humans, treadmill exercise elevated CTSB in plasma.
Increasing cystatin C (show CST3 ELISA Kits) and cathepsin B reported in serum of colorectal cancer patients.
Interruption of either CCL2 (show CCL2 ELISA Kits)-CCR2 (show CCR2 ELISA Kits) signaling or cathepsin B function significantly impaired perineural invasion (PNI (show SERPINE2 ELISA Kits)).
Expression of CSTA (show CSTA ELISA Kits) was detected in some tumor tissues and many tumor-infiltrating immune cells. Cathepsin B expression was also observed in most tumor tissues and tumor-infiltrating immune cells
Data suggest that expression of CTSB in human glioblastoma cell line can be modulated by dietary factors; here, caffeine decreases tumor size and CTSB expression in mouse xenograft model of glioblastoma; note that caffeine, normally a dietary component, was administered via intraperitoneal injection in these studies.
These results indicate that CST1 (show CST1 ELISA Kits)-mediated extracellular CatB activity enhances tumor development by preventing cellular senescence.
SNPs in NLRP3 (show NLRP3 ELISA Kits) and CTSB, associated with an increased NLRP3 (show NLRP3 ELISA Kits)-inflammasome activation, are protective against the development of active pulmonary tuberculosis.
cathepsin B activity assays identified secreted cathepsin B as responsible for apoA-I (show APOA1 ELISA Kits) cleavage at Ser (show SIGLEC1 ELISA Kits)(228) Importantly
ctsB enhanced neutrophil migration though a putative effect on pseudopod retraction rates.
We have shown that keratolytic winter erythema in South African and Norwegian families is caused by two different tandem duplications in a non-coding genomic region upstream of CTSB.
CtsB/L as major regulators of lysosomal function and demonstrate that CtsB/L may play an important role in intracellular cholesterol trafficking and in degradation of the key AD proteins
Using quenched activity-based probes, we identified mouse cathepsin B (CtsB), which is expressed in the lower regions of the hair follicle, as an additional target of mouse Cst6 (show CST6 ELISA Kits)
After phagocytosis, particles can disrupt lysosomes, and inhibitor studies have suggested that the resulting release of a lysosomal protease-cathepsin B-into the cytosol somehow activates NLRP3 (show NLRP3 ELISA Kits).
the roles of CTSB/S and SIRT1 (show SIRT1 ELISA Kits) in the regulation of hepatic inflammation using primary parenchymal and non-parenchymal hepatic cell types and cell lines.
Mice and macrophages lacking cathepsin B activity had increased resistance to the cytosolic bacterial pathogen Francisella novicida Genetic deletion.
Exposure of J774A.1 cells to HOCl or HOSCN resulted in a significant decrease in the activity of the Cys (show DNAJC5 ELISA Kits)-dependent cathepsins B and L, but not the Asp (show C3 ELISA Kits)-dependent cathepsin D (show CTSD ELISA Kits).
cathepsin B (CTSB) inhibition or expression of a CTSB-resistant Dab2 (show DAB2 ELISA Kits) mutant maintains Dab2 (show DAB2 ELISA Kits) expression and shifts long-term TGF-beta (show TGFB1 ELISA Kits)-treated cells from autophagy to apoptosis
study brings forth a yet unappreciated role for Cathepsin B in regulating T cell responses during Leishmania major infection
Our results suggest that the Mucopolysaccharidosis type I mice have progressive heart failure and valve disease, which may be caused by cathepsin B overexpression.
The cathepsin B deserves further evaluation as therapeutic targets to develop disease modifying drugs to treat Alzheimer's disease.
evidence shows cathepsin B activity may not be redox regulated; however, the stability of the enzyme at neutral pH is dependent on redox potential, and on the presence of oxidising agents.
Overexpressing cathepsin B reduced the Vascular Endothelial Growth Factor-dependent tube response
The peptides, all of which contain a C-terminal free acid, were tested as inactivators of bovine cathepsin B, in an attempt at exploiting the known and, amongst the cysteine proteinases, unique carboxy dipeptidyl peptidase (show ACE ELISA Kits) activity of the protease.
Findings showed that CTSB facilitates adipogenesis, and its effect is associated with fibronectin degradation and Wnt/b-catenin signaling pathway.
CTSB may be required to remodel endometrial and placental tissues for close apposition between maternal and fetal vasculatures and to facilitate transplacental transport of gases, micronutrients (amino acids, glucose), and macromolecules (proteins).
The protein encoded by this gene is a lysosomal cysteine proteinase composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is also known as amyloid precursor protein secretase and is involved in the proteolytic processing of amyloid precursor protein (APP). Incomplete proteolytic processing of APP has been suggested to be a causative factor in Alzheimer disease, the most common cause of dementia. Overexpression of the encoded protein, which is a member of the peptidase C1 family, has been associated with esophageal adenocarcinoma and other tumors. At least five transcript variants encoding the same protein have been found for this gene.
, cathepsin B-2744
, cathepsin B-1674
, cathepsin B-84
, cathepsin B-3098
, cathepsin B-16D2
, cathepsin B-1874
, cathepsin B-3483
, cathepsin B-10270
, APP secretase
, amyloid precursor protein secretase
, cathepsin B1
, cysteine protease