Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.Cathepsins: A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.Cathepsin B: A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.Cathepsin D: An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).Cathepsin K: A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.Cysteine Endopeptidases: ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.Cathepsin G: A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.Cathepsin E: An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.Cathepsin C: A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.Cystatins: A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.Fasciola hepatica: A species of helminth commonly called the sheep liver fluke. It occurs in the biliary passages, liver, and gallbladder during various stages of development. Snails and aquatic vegetation are the intermediate hosts. Occasionally seen in man, it is most common in sheep and cattle.DiazomethaneCathepsin Z: A ubiquitously-expressed cysteine peptidase that exhibits carboxypeptidase activity. It is highly expressed in a variety of immune cell types and may play a role in inflammatory processes and immune responses.Lysosomes: A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Cathepsin W: A cysteine endopeptidase found in NATURAL KILLER CELLS and CYTOTOXIC T-LYMPHOCYTES. It may have a specific function in the mechanism or regulation of cytolytic activity of immune cells.Papain: A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.Cystatin B: An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Dipeptides: Peptides composed of two amino acid units.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.Cystatin A: A cytastin subtype found at high levels in the SKIN and in BLOOD CELLS. Cystatin A incorporates into the cornified cell envelope of stratified squamous epithelial cells and may play a role in bacteriostatic properties of skin.Fascioliasis: Liver disease caused by infections with parasitic flukes of the genus FASCIOLA, such as FASCIOLA HEPATICA.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Cathepsin A: A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.Pepstatins: N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Cystatin M: A cystatin subtype that has a diverse tissue distribution, target specificity, and functions as an endogenous inhibitor of lysosomal cysteine proteases.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Pancreatic Elastase: A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.Cystatin C: An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.Secretory Vesicles: Vesicles derived from the GOLGI APPARATUS containing material to be released at the cell surface.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)T-Lymphocytes, Cytotoxic: Immunized T-lymphocytes which can directly destroy appropriate target cells. These cytotoxic lymphocytes may be generated in vitro in mixed lymphocyte cultures (MLC), in vivo during a graft-versus-host (GVH) reaction, or after immunization with an allograft, tumor cell or virally transformed or chemically modified target cell. The lytic phenomenon is sometimes referred to as cell-mediated lympholysis (CML). These CD8-positive cells are distinct from NATURAL KILLER CELLS and NATURAL KILLER T-CELLS. There are two effector phenotypes: TC1 and TC2.ElastinNK Cell Lectin-Like Receptor Subfamily K: An activating NK cell lectin-like receptor subfamily that regulates immune responses to INFECTION and NEOPLASMS. Members of this subfamily generally occur as homodimers.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Cytoplasmic Granules: Condensed areas of cellular material that may be bounded by a membrane.Rodenticides: Substances used to destroy or inhibit the action of rats, mice, or other rodents.Rodent Control: The reduction or regulation of the population of noxious, destructive, or dangerous rodents through chemical, biological, or other means.Rodent Diseases: Diseases of rodents of the order RODENTIA. This term includes diseases of Sciuridae (squirrels), Geomyidae (gophers), Heteromyidae (pouched mice), Castoridae (beavers), Cricetidae (rats and mice), Muridae (Old World rats and mice), Erethizontidae (porcupines), and Caviidae (guinea pigs).Social Work: The use of community resources, individual case work, or group work to promote the adaptive capacities of individuals in relation to their social and economic environments. It includes social service agencies.Laboratory Animal Science: The science and technology dealing with the procurement, breeding, care, health, and selection of animals used in biomedical research and testing.LondonReagent Kits, Diagnostic: Commercially prepared reagent sets, with accessory devices, containing all of the major components and literature necessary to perform one or more designated diagnostic tests or procedures. They may be for laboratory or personal use.Animal Welfare: The protection of animals in laboratories or other specific environments by promoting their health through better nutrition, housing, and care.Animals, Laboratory

Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. (1/644)

The lysosomal cysteine proteases cathepsins S and L play crucial roles in the degradation of the invariant chain during maturation of MHC class II molecules and antigen processing. The p41 form of the invariant chain includes a fragment which specifically inhibits cathepsin L but not S. The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges. The first subdomain is an alpha-helix-beta-strand arrangement, whereas the second subdomain has a predominantly beta-strand arrangement. The wedge shape and three-loop arrangement of the p41 fragment bound to the active site cleft of cathepsin L are reminiscent of the inhibitory edge of cystatins, thus demonstrating the first example of convergent evolution observed in cysteine protease inhibitors. However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites. This enables inhibitors based on the thyroglobulin type-1 domain fold, in contrast to the rather non-selective cystatins, to exhibit specificity for their target enzymes.  (+info)

Crystal structure of wild-type human procathepsin K. (2/644)

Cathepsin K is a lysosomal cysteine protease belonging to the papain superfamily. It has been implicated as a major mediator of osteoclastic bone resorption. Wild-type human procathepsin K has been crystallized in a glycosylated and a deglycosylated form. The latter crystals diffract better, to 3.2 A resolution, and contain four molecules in the asymmetric unit. The structure was solved by molecular replacement and refined to an R-factor of 0.194. The N-terminal fragment of the proregion forms a globular domain while the C-terminal segment is extended and shows substantial flexibility. The proregion interacts with the enzyme along the substrate binding groove and along the proregion binding loop (residues Ser138-Asn156). It binds to the active site in the opposite direction to that of natural substrates. The overall binding mode of the proregion to cathepsin K is similar to that observed in cathepsin L, caricain, and cathepsin B, but there are local differences that likely contribute to the specificity of these proregions for their cognate enzymes. The main observed difference is in the position of the short helix alpha3p (67p-75p), which occupies the S' subsites. As in the other proenzymes, the proregion utilizes the S2 subsite for anchoring by placing a leucine side chain there, according to the specificity of cathepsin K toward its substrate.  (+info)

Vaccination with cathepsin L proteinases and with leucine aminopeptidase induces high levels of protection against fascioliasis in sheep. (3/644)

The potential of different parasite proteinases for use as vaccine candidates against fascioliasis in sheep was studied by vaccinating animals with the cathepsin L proteinases CL1 and CL2 and with leucine aminopeptidase (LAP) purified from adult flukes. In the first trial, sheep were immunized with CL1 or CL2 and the mean protection levels obtained were 33 and 34%, respectively. Furthermore, a significant reduction in egg output was observed in sheep vaccinated either with CL1 (71%) or with CL2 (81%). The second trial was performed to determine the protective potential of the two cathepsin L proteinases assayed together, as well as in combination with LAP, and of LAP alone. The combination of CL1 and CL2 induced higher levels of protection (60%) than those produced when these enzymes were administered separately. Those sheep that received the cocktail vaccine including CL1, CL2, and LAP were significantly protected (78%) against metacercarial challenge, but vaccination with LAP alone elicited the highest level of protection (89%). All vaccine preparations induced high immunoglobulin G titers which were boosted after the challenge infection, but no correlations between antibody titers and worm burdens were found. However, the sera of those animals vaccinated with LAP contained LAP-neutralizing antibodies. Reduced liver damage, as assessed by the level of the liver enzyme gamma-glutamyl transferase, was observed in the groups vaccinated with CL1, CL2, and LAP or with LAP alone.  (+info)

Acidic pH as a physiological regulator of human cathepsin L activity. (4/644)

Human cysteine protease cathepsin L was inactivated at acid pH by a first-order process. The inactivation rate decreased with increasing concentrations of a small synthetic substrate, suggesting that substrates stabilize the active conformation. The substrate-independent inactivation rate constant increased with organic solvent content of the buffer, consistent with internal hydrophobic interactions, disrupted by the organic solvent, also stabilizing the enzyme. Circular dichroism showed that the inactivation is accompanied by large structural changes, a decrease in alpha-helix content being especially pronounced. The high activation energy of the reaction at pH 3.0 (200 kJ.mol-1) supported such a major conformational change occurring. The acid inactivation of cathepsin L was irreversible, consistent with the propeptide being needed for proper folding of the enzyme. Aspartic protease cathepsin D was shown to cleave denatured, but not active cathepsin L, suggesting a potential mechanism for in-vivo regulation and turnover of cathepsin L inside lysosomes.  (+info)

A novel egg-derived tyrosine phosphatase, EDTP, that participates in the embryogenesis of Sarcophaga peregrina (flesh fly). (5/644)

We have previously reported that cathepsin L mRNA is present in unfertilized eggs of Sarcophaga peregrina (flesh fly) as a maternal mRNA, which suggests that cathepsin L is required for embryogenesis. Now we have identified an egg protein, with a molecular mass of 100 kDa, that is extremely susceptible to cathepsin L digestion and which disappears rapidly as the embryos develop. We purified this protein to homogeneity, cloned its cDNA, and found that it contained a consensus sequence for the active site of tyrosine phosphatase. In fact this protein showed tyrosine phosphatase activity, indicating that it is a novel tyrosine phosphatase. The expression and subsequent disappearance of this protein, which we have named egg-derived tyrosine phosphatase (EDTP), may be indispensable for embryogenesis of Sarcophaga.  (+info)

Collagenase, cathepsin B and cathepsin L gene expression in the synovial membrane of patients with early inflammatory arthritis. (6/644)

OBJECTIVE: To examine the expression of the matrix metalloproteinase, MMP-1, and the cysteine proteases, cathepsin B (CB) and cathepsin L (CL), in the synovial membrane (SM) of patients with early inflammatory arthritis. METHODS: Samples of SM were obtained by blind needle biopsy or needle arthroscopy from inflamed knees of 28 patients with early inflammatory arthritis (mean disease duration 10.2 months, range 2 weeks-18 months). Sixteen patients had rheumatoid arthritis (RA), nine psoriatic arthritis and there was one each with ankylosing spondylitis, gout and an undifferentiated arthritis. Comparison was made with tissue from two patients with established erosive RA and three normal synovial tissue samples. In situ hybridization was performed using digoxigenin-labelled RNA probes. RESULTS: MMP-1, CB and CL were expressed in all patients with early arthritis and in established erosive RA, whereas normal synovium showed only scanty expression. The three proteases were prominent in perivascular infiltrates and endothelial cells of early arthritis tissue. MMP-1 was observed primarily in the lining layer, but was also evident in the sublining area. CB and CL were expressed to a lesser extent in the lining layer, and were present mainly in the subintima. The three proteases were not found in lymphoid aggregrates. No differences were observed between the disease categories. CONCLUSIONS: The detection of MMP-1, CB and CL in the synovium shortly after symptom onset implies that the potential for joint destruction exists at a very early stage in the disease. In addition, the perivascular and endothelial cell expression suggests a role for these proteases in mononuclear cell influx to the inflamed synovium and in angiogenesis.  (+info)

Short report: Diagnosis of human fascioliasis: detection of anti-cathepsin L antibodies in blood samples collected on filter paper. (7/644)

We have developed an ELISA for the diagnosis of human fascioliasis based on the detection of IgG4 antibodies to Fasciola hepatica cathepsin LI cysteine protease. Use of this assay in the Bolivian Altiplano, a region with a high prevalence of the disease, was hampered by the reluctance of the indigenous population to provide blood. To overcome this problem, we have investigated the method of collecting small quantities of blood from the finger onto filter paper, followed by the elution of antibodies for use in the diagnostic assay. Serum samples and blood samples collected onto filter paper were obtained from 57 individuals living in the village of Cutusuma in 1987 and from 11 individuals in Chijipata in 1996. Analysis of the IgG4-ELISA results revealed that there is highly significant linear relationship (P < 0.001) between the two methods of sampling. Most importantly, a reliable diagnosis was made with the blood-filter samples from Cutusuma, which had been stored for 10 years at 40 degrees C. While some deterioration of the blood-filter samples from Cutusuma had occurred over the 10-year storage period, no deterioration occurred with the Chijipata samples, which were stored for one year. Therefore, the method of collecting blood onto filter paper should prove useful for large-scale epidemiologic studies on human fascioliasis in the Bolivian Altiplano and in other regions where this disease is prevalent.  (+info)

Short report: Immunodiagnosis of human fascioliasis using recombinant Fasciola hepatica cathepsin L1 cysteine proteinase. (8/644)

Our laboratory recently developed a diagnostic test (ELISA) for human fascioliasis based on the detection of serum IgG4 antibodies reactive with Fasciola hepatica cathepsin L1 (CL1). In the present study, we have used recombinant CL1, generated by functional expression of the cDNA in Saccharomyces cerevisiae, in this immunodiagnostic test and compared its performance with native CL1. Sera obtained from 64 individuals living in Cutusuma village in the northern Altiplano of Bolivia, a region with a high prevalence of human fascioliasis, were analyzed by the IgG4-ELISA. A highly statistically significant correlation (r2 = 0.751, P < 0.001) was demonstrated between the absorbances obtained using the recombinant and native proteins. These assays showed that 38 (59%) of the individuals tested were seropositive for fascioliasis, whereas only 26 of them were coprologically positive for F. hepatica eggs. All seronegative patients were also coprologically negative. Serum from individuals infected with schistosomiasis mansoni, cysticercosis, hydatidosis, and Chagas disease did not contain antibodies reactive with the recombinant or native CL1. Therefore, recombinant CL1 shows excellent potential for the development of the first standardized assay for the sensitive and specific diagnosis of human fascioliasis. Finally, our data supports earlier reports on the high prevalence of human fascioliasis in the Bolivian Altiplano, which collectively suggest that the disease has been endemic there for more than a decade.  (+info)

Taenia solium metacestode, a larval pork tapeworm, is a causative agent of neurocysticercosis, one of the most common parasitic diseases in the human central nervous system. In this study, we identified a cDNA encoding for a cathepsin L-like cysteine protease from the T solium metacestode (TsCL-1) and characterized the biochemical properties of the recombinant enzyme. The cloned cDNA of 1216 bp encoded 339 amino acids with an approximate molecular weight of 37.6 kDa which containing a typical signal peptide sequence (17 amino acids), a pro-domain (106 amino acids), and a mature domain (216 amino acids). Sequence alignments of TsCL-1 showed low sequence similarity of 27.3-44.6 to cathepsin L-like cysteine proteases from other helminth parasites, but the similarity was increased to 35.9-55.0 when compared to mature domains. The bacterially expressed recombinant protein (rTsCL-1) did not show enzyme activity; however, the rTsCL-1 expressed in Pichia pastoris showed typical biochemical ...
SID 26681509 is a reversible and potent human cathepsin L inhibitor. SID 26681509 displays no inhibitory activity of cathepsin G.
CTSL3P (ENST00000354530.2) at chr9:87772915-87786884 - Homo sapiens cathepsin L family member 3, pseudogene (CTSL3P), non-coding RNA. (from RefSeq NR_027917) CTSL (ENST00000343150.10) at chr9:87726119-87731469 - Homo sapiens cathepsin L (CTSL), transcript variant 1, mRNA. (from RefSeq NM_001912) CTSL (ENST00000495822.1) at chr9:87726134-87731393 - cathepsin L (from HGNC CTSL) CTSL (ENST00000482054.1) at chr9:87726140-87729680 - cathepsin L (from HGNC CTSL) CTSL3P (ENST00000412179.5) at chr9:87772453-87774299 - cathepsin L family member 3, pseudogene (from HGNC CTSL3P) CTSL (ENST00000375894.9) at chr9:87726114-87731073 - cathepsin L (from HGNC CTSL) CTSL (ENST00000342020.5) at chr9:87726140-87728997 - Belongs to the peptidase C1 family. (from UniProt Q5T8F0) CTSL (ENST00000340342.10) at chr9:87726109-87731386 - Homo sapiens cathepsin L (CTSL), transcript variant 2, mRNA. (from RefSeq NM_145918) CTDSPL2 (ENST00000558966.5) at chr15:44427793-44524543 - Probable phosphatase (By similarity). (from ...
The aim of the work was to identify and characterize the cysteine proteinases of bone tissue, as these enzymes appear necessary for bone resorption. Three cysteine-dependent proteolytic activities were separated from a homogenate of mouse calvaria by a fractionation procedure involving (NH4)2SO4 precipitation, gel filtration and ion-exchange chromatography. The first two are typical cathepsins B and L with respect to (1) their reactivity with anti-(cathepsin B) and anti-(cathepsin L) antibodies respectively, (2) their relative rate constants for inhibition by benzyloxycarbonyl-Phe-Phe-CHN2 and L-3-carboxy-trans-2,3-epoxypropionyl-L-leucylamido-(4-guanid ino)butane and (3) their enzymic properties, such as the higher activities of cathepsin L against collagen and gelatin as compared with cathepsin B, and the fact that benzyloxycarbonyl-Arg-Arg 4-methoxy-2-naphthylamide is hydrolysed only by cathepsin B. Cathepsin L was mainly recovered in its precursor form, as indicated by its apparent 40 kDa ...
There are no specific protocols for Recombinant human Cathepsin L protein (ab81780). Please download our general protocols booklet
Purpose : We have previously demonstrated that an accumulation of advanced glycation end-products (AGEs) in the Bruchs membrane (BrM) can alter retinal pigment epithelium (RPE) lysosomal activity by changing expression of key effectors and inhibitors. Altered activity of lysosomal cysteine proteases, the cathepsins, can in turn impact signalling via the NF-kB pathway. The aim of this study therefore was to analyse the effects of AGEs on specific lysosomal cathepsins, and the endogenous levels of effectors of the NF-kB signalling pathway in RPE. Methods : ARPE-19 cells were cultured on AGE-containing BrM mimics in vitro for 7-14 days. Intracellular processing of the cysteine proteases cathepsins B, L and S were assessed by qPCR and immunoblotting, while their intracellular activity was assessed using fluorescence-based cleavage assays. Expression of NF-kB (p65) and its main regulatory protein, IκBα, was assessed by qPCR and immunoblotting. Statistical analysis was performed using the ...
Cathepsin L antibody [2H7] (cathepsin L1) for ELISA, WB. Anti-Cathepsin L mAb (GTX50040) is tested in Human samples. 100% Ab-Assurance.
19 products from 13 suppliers. Compare and order Cathepsin L2 ELISA Kits. View citations, images, detection ranges, sensitivity, prices and more. Recommended products for the most popular species. Our scientists will help you find the right ELISA kit for your needs.
Certain cysteine proteases, such as cathepsin L (Ctsl), have been involved in yolk processing mechanisms in oocytes and embryos of lower vertebrates. In zebrafish (Danio rerio), three different ctsl genes, ctsla, ctslb and ctslc, have been found in the genome, but their pattern of expression, as well as information on which the encoded enzymes are potentially involved in yolk absorption during embryogenesis, is unknown. Here, phylogenetic and gene structure analysis revealed that zebrafish ctsla and ctslb genes are similar, showing a highly conserved structure in comparison with human ctsl, while ctslc presents different exon organization together with an earlier evolution. Thus, ctslc appears to be evolved from a common ancestral ctsl-like gene, possibly through an early duplication event, whereas ctsla and ctslb may be originated from a second duplication mechanism. Zebrafish ctsla, ctslb and ctslc also showed different patterns of mRNA expression during embryogenesis and in adult tissues. ...
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Rabbit polyclonal Cathepsin L/MEP antibody. Validated in WB and tested in Mouse, Human. Independently reviewed in 1 review(s). Immunogen corresponding to full length protein.
2014 (English)In: Scandinavian Journal of Rheumatology, ISSN 0300-9742, E-ISSN 1502-7732, Vol. 43, no S127, 53-53 p.Article in journal, Meeting abstract (Other academic) Published ...
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Remodeling of cellular metabolism is a genuine feature of rapidly growing cells. Herein we report that mouse embryonic fibroblasts, lacking the Cathepsin L (Cts L) gene, proliferate faster than wild-types and display a noticeable glycolytic shift to satisfy their ever-growing metabolic needs. Mass spectrometry analyses identified LDHA as an essential metabolic junction in these cells, and downstream biochemical studies suggested that Cts L regulates LDHA expression and function. Together, these data uncover an unprecedented role for Cathepsin L in cell metabolism. ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
|p|E-64-c, which is also known as Ep-475, is an analog of E-64 and inhibitor of cysteine proteinases. [1]|br /|The cysteine proteinases, of which Cathepsins B and H and cathepsin L exist in mammals, contain an essential highly reactive thiol group, and th
Ischaemia-reperfusion (IR) injury contributes to the cardiac damage following myocardial infarction and paradoxically reduces the benefits of reperfusion therapy. In patients with ischaemic heart disease, cathepsin-L is elevated in the serum and correlates with disease severity. Our data demonstrate that cathepsin-L released from ex vivo rat hearts after ischaemia, and the cathepsin-L inhibitor CAA0225 improves cardiac function during ischaemia-reperfusion ex vivo. However, the effects of the CAA0225 in in vivo hearts during ischaemia-reperfusion are unknown. We hypothesised that using CAA0225 in an in vivo mouse model of ischaemia-reperfusion would identify the role cathepsin-L plays during ischaemia-reperfusion. Ischaemia-reperfusion injury was induced by 45 min temporary coronary artery ligation and CAA0225 was given by intra-venous injection during ischaemia before reperfusion. Double-dye staining demonstrated no difference in area at risk between groups whereas CAA0225 significantly reduced ...
Efficacy of Sandwich and Dot-ELISA in Diagnosis of Fascioliasis using a Pair of Polyclonal Antibodies Against Cathepsin L Antigen in Naturally Infected Sheep ...
Increased human cathepsin L activity is linked to invasive and metastatic cancers where it promotes degradation of the extracellular matrix. This major cysteine protease found in cell lysosomes and secreted from tissues ...
Nanomaterials are being incorporated into many biological applications for use as therapeutics sensors or labels. silver nanoparticles due to the increased use of these materials in biological applications. This manuscript depicts how both of these types of nanomaterials affect cathepsin activity which could impact the hosts immune system and its ability to respond to pathogens. Cathepsin B activity decreases in a dose-dependent manner with all nanoparticles tested. Alternatively the impact of nanoparticles on cathepsin L activity depends greatly on the type and size of the material. ≤ 0.05 was used as the level for significance. A-867744 Results Ag-NP Biocompatibility in Vero cells After a 24-h exposure a 25% decline in cell viability was observed in Vero cells exposed to 50 μg/ml of 10-nm uncoated Ag-NPs Mouse monoclonal to MAP2. MAP2 is the major microtubule associated protein of brain tissue. There are three forms of MAP2; two are similarily sized with apparent molecular weights of 280 ...
Cathepsin S, Human, Recombinant, E. coli, is prepared without a tag or fusion protein. A major lysosomal cysteine proteinase with high specific activity. - Find MSDS or SDS, a COA, data sheets and more information.
Sigma-Aldrich offers abstracts and full-text articles by [Tomasz Gogiel, Małgorzata Wolańska, Zofia Galewska, Piotr Kinalski, Krzysztof Sobolewski, Lech Romanowicz].
The protein therapeutic and CD95L inhibitor asunercept is currently under clinical investigation for the treatment of glioblastoma and myelodysplastic syndrome. The purpose of this study was to predict the asunercept pharmacokinetics in children and to give dose recommendations for its first use in pediatric glioblastoma patients. A physiologically-based pharmacokinetic (PBPK) model of asunercept in healthy and diseased adults was successfully developed using the available clinical Phase I and Phase II study data. This model was then extrapolated to different pediatric populations, to predict the asunercept exposure in children and to find equivalent starting doses. Simulation of the asunercept serum concentration-time curves in children between 1–18 years of age shows that a dosing regimen based on body weight results in a similar asunercept steady-state exposure in all patients (pediatric or adult) above 12 years of age. For children between 1–12 years, higher doses per kg body weight are
Savalas, L. R., Gasnier, B., Damme, M., Lübke, T., Wrocklage, C., Debacker, C., Jezeqou, A., Reinheckel, T., Hasilik, A., Saftig, P., et al. (2011). Disrupted in renal carcinoma 2 (DIRC2), a novel transporter of the lysosomal membrane, is proteolytically processed by cathepsin L. Biochemical Journal 436, 113-121 ...
|p|EPZ5676 is a potent inhibitor of DOT1L histone methyltransferase, according to X-ray crystallographic analysis, that occupies the S-adenosyl methionine (SAM) binding pocket of DOT1L and induces conformational changes in DOT1L resulting in the opening o
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Cathepsin F is a protein that in humans is encoded by the CTSF gene. Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. In general, cathepsins contain a signal sequence, followed by a propeptide and then a catalytically active mature region. The very long (251-amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily. This cystatin-like domain contains some of the elements known to be important for inhibitory activity. CTSF encodes a predicted protein of 484 amino acids that contains a 19-residue signal ...
Looking for online definition of Cathepsin S in the Medical Dictionary? Cathepsin S explanation free. What is Cathepsin S? Meaning of Cathepsin S medical term. What does Cathepsin S mean?
Complexes of gold( I) have long been used to treat rheumatoid arthritis although the precise biological targets of gold are not well understood. One intriguing therapeutic target of Au( I) is the cathepsin family of lysosomal cysteine proteases. Here, we present the inhibition of cathepsin B by a known Au( I)-based drug and a series of derivatives. The complexes investigated were reversible, competitive inhibitors with IC50 values ranging from 0.3 to 250 mu M, depending on the substituents around the Au( I). ...
Cathepsin B, H, L and D activities in liver lysosomes were compared between species. Although cathepsin B and D were detected in bovine, pig, chicken and rat liver, striking species differences were evident for cathepsin H and L. Cathepsin L activity was particularly high in chicken lysosomal extracts, but could not be detected in bovine and pig extracts. Whereas there was no significant cathepsin H activity in bovine extracts, rat liver lysosomal extracts contained large amounts of cathepsin H activity. ...
Vectors based on different serotypes of adeno-associated virus hold great promise for human gene therapy, based on their unique tissue tropisms and distinct immunological profiles. A particularly interesting candidate is AAV8, which can efficiently and rapidly transduce a wide range of tissues in vivo. To further unravel the mechanisms behind AAV8 transduction, we used yeast two-hybrid analyses to screen a mouse liver complementary DNA library for cellular proteins capable of interacting with the viral capsid proteins. In total, we recovered approximately 700 clones, comprising over 300 independent genes. Sequence analyses revealed multiple hits for over 100 genes, including two encoding the endosomal cysteine proteases cathepsins B and L. Notably, these two proteases also physically interacted with the corresponding portion of the AAV2 capsid in yeast, but not with AAV5. We demonstrate that cathepsins B and L are essential for efficient AAV2- and AAV8-mediated transduction of mammalian cells, and
The parasitic protozoon Leishmania mexicana possesses an abundance of developmentally regulated cathepsin L-like cysteine proteinases expressed at highest levels in amastigotes. We recently characterised lmcpa, a single-copy gene encoding one such proteinase, LmCPa, which differs from other homologues by possessing a 3-amino-acid insertion at the amino terminal of the predicted mature proteinase. To investigate the role of LmCPa in L. mexicana, we used gene-targeting of promastigotes with hygromycin- and phleomycin-resistance markers to generate null mutants by disrupting sequentially both alleles of lmcpa. The promastigote null mutants did not differ significantly from wild-type L. mexicana in growth rate or morphology and could differentiate to metacyclics and the amastigote-like form, both of which could infect the J774G8 macrophage-like cell line. The null mutant amastigote-like form obtained from the J774G8 cells could also establish rump lesions in CBA mice. By these criteria, therefore, ...
1CPJ: CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN
Alopecia X occurs in several arctic breeds with plush undercoat such as the Keeshond, Pomeranian, Samojede, Chow-Chow, and Alaskan Malamute. It is characterized by hair loss and dark coloration of the affected skin areas. The disease typically starts at 1-5 years of age and predominantly affects the rump of the animals. Alopecia X has also been termed growth hormone-responsive alopecia and black skin disease. Although many experts believe in a genetic cause for alopecia X, the exact mode of inheritance is still under discussion. The primary aim of this study is to collect a suitable sample collection for genetic analyses. During the project DNA samples from healthy and affected Keeshonden and Pomeranians will be collected. Pedigree analysis of these dogs will allow the determination of the mode of inheritance. The second aim of this study concerns the investigation of the cathepsin L gene (CTSL) in the acquired samples. Mutations in this gene cause hair loss in the so-called furless mouse mutant and
Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. In humans, it is coded by the CTSB gene. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene.
Cathepsin B (CtsB) is a lysosomal cysteine proteinase that is specifically translocated to the extracellular milieu during cancer progression. The development of a lipidated CtsB inhibitor incorporated into the envelope of a liposomal nanocarrier (LNC-NS-629) is described. Ex vivo and in vivo studies confirmed selective targeting and internalization of LNC-NS-629 by tumor and stromal cells, thus validating CtsB targeting as a highly promising approach to cancer diagnosis and treatment ...
We synthesized one series of fluorogenic substrates for cathepsin B derived from the peptide Bz-F-R-MCA (Bz = benzoyl, MCA = 7-methyl-coumarin amide) substituting Phe at the P(2) position by non-natural basic amino acids that combine a positively charged group with aromatic or aliphatic radicals at the same side chain, namely, 4-aminomethyl-phenylalanine, 4-guanidine-phenylalanine. 4-aminomethyl-N-isopropyl-phenylalanine. 3-pyridyl-alanine, 4-piperidinyl-alanine, 4-amino-methyl-cyclohexyl-alanine. 4-aminocyclohexyl-alanine, and N(im)-dimethyl-histidine. Bz-F-R-MCA was the best substrate for cathepsin B but also hydrolyzed Bz-R-R-MCA with lower efficiency, since the protease accepts Arg at St due to the presence of Glu(245) at the bottom of this subsite. the presence of the basic non-natural amino acids at the Pt position of the substrate partially restored the catalytic efficiency of cathepsin B. All the kinetic parameters for hydrolysis of the peptides described in this paper are in accordance ...
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When the researchers combined the two cathepsins and allowed them to attack samples of elastin, they expected to see increased degradation of the protein. What they saw, however, was not much more damage than cathepsin K did by itself. Platt at first believed the experiment was flawed, and asked Barry - an undergraduate student in his lab who specializes in modeling - to examine what possible conditions could account for the experimental result. Barrys modeling suggested that effects observed could occur if cathepsin S were degrading cathepsin K instead of attacking the elastin - a protein essential in arteries and the cardiovascular system.. That theoretical result led to additional experiments in which the researchers measured a direct correlation between an increase in the amount of cathepsin S added to the experiment and a reduction in the degradation of collagen. By increasing the amount of cathepsin S ten-fold over the amount used in the original experiment, Platt and Barry were able to ...
Cathepsin D小鼠单克隆抗体[CTD-19](ab6313)可与小鼠, 人样本反应并经WB, IP, ELISA, IHC, ICC/IF实验严格验证,被13篇文献引用并得到14个独立的用户反馈。
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Polyclonal antibody for Cathepsin B/CTSB detection. Host: Rabbit.Size: 100μg/vial. Tested applications: WB. Reactive species: Human. Cathepsin B/CTSB information: Molecular Weight: 37822 MW; Subcellular Localization: Lysosome. Melanosome. Secreted, extrac
Heparanase, also known as HPSE, is an enzyme that acts both at the cell-surface and within the extracellular matrix to degrade polymeric heparan sulfate molecules into shorter chain length oligosaccharides. The protein is originally synthesised in an inactive 65 kDa proheparanase form in the golgi apparatus and transferred to late endosomes/lysosomes for transport to the cell-surface. In the lysosome it is proteolytically processed into its active form. Proteolytic processing results in the production of three products, a linker peptide an 8 kDa proheparanase fragment and a 50 kDa proheparanase fragment The 8 kDa and 50 kDa fragments form a heterodimer and it is this heterodimer that constitutes the active heparanase molecule. The linker protein is so called because prior to its excision it physically links the 8 kDa and 50 kDa proheparanase fragments. Complete excision of the linker peptide appears to be a prerequisite to the complete activation of the heparanase enzyme. Crystal structures of ...
Exerts, in vitro, a potent antimicrobial activity. Probably due to an impairment of the function of the respiratory chain and of energy-dependent activities in the inner membrane of susceptible microorganisms (By similarity).
Immunoelectron microscopy identifying avidin (8-nm gold) and cathepsin L (15-nm gold) immunoreactivity in organelles from late endosome, lysosome, and hybrid
Impaired T cell priming and cytokine production in OX40L-deficient mice and MGP34-treated mice. (A) OX40L-deficient mice have impaired recall proliferative resp
Principal Investigator:KATUNUMA Nobuhiko, Project Period (FY):1989 - 1990, Research Category:Grant-in-Aid for Developmental Scientific Research (B)., Research Field:Pathological medical chemistry
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Inflammatory breast cancer (IBC) is an aggressive, metastatic and highly angiogenic form of locally advanced breast cancer with a relatively poor three-year survival rate. Breast cancer invasion has been linked to proteolytic activity at the tumor cell surface. Here we explored a role for active cathepsin B on the cell surface in the invasiveness of IBC. We examined expression of the cysteine protease cathepsin B and the serine protease urokinase plasminogen activator (uPA), its receptor uPAR and caveolin-1 in two IBC cell lines: SUM149 and SUM190. We utilized a live cell proteolysis assay to localize in real time the degradation of type IV collagen by IBC cells. IBC patient biopsies were examined for expression of cathepsin B and caveolin-1. Both cell lines expressed comparable levels of cathepsin B and uPA. In contrast, levels of caveolin-1 and uPAR were greater in SUM149 cells. We observed that uPA, uPAR and enzymatically active cathepsin B were colocalized in caveolae fractions isolated from SUM149
Electrospray mass spectrometric techniques were used to demonstrate that mature (single-chain) recombinant rat cathepsin B is capable of sequentially removing the three dipeptides which comprise the C-terminal extension of the proenzyme. A pepsin-cleaved form of a non-active mutant recombinant rat procathepsin B (Cys-29-Ser) was used as a substrate to study C-terminal processing by mature cathepsin B. The results indicate that the first two residues (Arg-Phe) are removed efficiently, while the remaining four (Gln-Tyr-Trp-Gly), particularly the final two, are much more resistant to proteolysis. These cleavages were pronounced at pH 5.0 compared with pH 6.0, in agreement with the lower pH optimum for cathepsin B exopeptidase activity reported previously. From this example of the peptidyldipeptidase activity of cathepsin B we conclude that removal of the C-terminal extension may occur in any intracellular compartment where active cathepsin B is found. ...
Cathepsins are intracellular proteinases that hydrolyze the peptide bonds of proteins. These enzyme have been implicated in the tenderization of aging beef, with the deterioration of radiation-stabilized meats on storage, and in the spoilage of fish prior to processing. Hence, the cathepsins of edible muscles are of concern to the food scientist. The purpose of the research reported herein was to develop procedures for the purification of the cathepsin from salmon muscle. The availability of a purified preparation of salmon muscle cathepsins should stimulate interest and research in the characterization of these enzymes and lead to better means for the control of catheptic activity in fish muscle. Results from these investigations indicate that salmon muscle cathepsins exhibit pH optima at 3.7, 6.9, and 8.5 when Folins reagent was used to determine the products of protein hydrolysis; whereas, pH optima at 3.7 and 7.3 were obtained when the products of protein hydrolysis were determined by ...
Cathepsin B is a lysosomal cysteine protease, which is involved in the degradation of the extracellular matrix in tumor growth. It has been investigated in various carcinomas of the gastrointestinal tract, lung, breast, and others. Correlations with clinico-pathological variables and a worse prognosis associated with a strong expression of cathepsin B have been observed in some studies. However, in gastric cancer, previous results were contradictory. In the present immunohistochemical study, gastric adenocarcinomas from 115 patients were included. All patients were treated by gastrectomy with D2 lymphadenectomy. 49 patients were women (42.6 %) and 66 (57.4 %) were men. The mean age was 64.4 years (range: 33 - 85). All carcinomas were classified according to the UICC, WHO, Laur n, Goseki and Ming classification. Formalin-fixed and paraffin-embedded specimens were immunohistochemically stained according to a standard ABC peroxidase method. The extent of immunoreactivity was scored ...
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Purpose: : To evaluate the utility of Cathepsin S (CATS) as a biomarker for diagnosing Sjögrens Syndrome (SjS), CATS levels in the tears of patients with SjS were compared to CATS levels in patients with other forms of autoimmune diseases and keratoconjuctivitis sicca (KCS). Current markers utilized for diagnosis of SjS include SSA/SBB autoantigens; however, these markers lack sensitivity and specificity in unequivocally diagnosing SjS. Methods: : 111 patients were recruited. Schirmers tests were administered to 41 patients diagnosed with primary or secondary SjS, 23 patients with Rheumatoid Arthritis (RA) without secondary SjS, 17 patients with Systemic Lupus Erythematosus (SLE) without secondary SjS, 20 patients with other autoimmune diseases without secondary SjS, and 10 patients with KCS. Schirmers strips were placed on ice after tear collection. Tear proteins were subsequently eluted and analyzed within 4 hours for CATS activity using the BioVision Cathepsin S Activity Assay Kits with ...
Compounds of the formula (I), wherein R.sub.1 is aryl or biaryl; R.sub.2 is aryl-lower alkyl, biaryl-lower alkyl, benzo-fused cycloalkyl, cycloalkyl-lower alkyl, bicycloalkyl-lower alkyl, aryloxy-lower alkyl, or aryl-C.sub.2 -C.sub.7 -alkyl in which C.sub.2 -C.sub.7 -alkyl is interrupted by Y; Y is O, S, SO, SO.sub.2, CO or NR.sub.6 ; R.sub.3 is hydrogen or lower alkyl; or R.sub.2 and R.sub.3 combined are C.sub.2 -C.sub.7 -alkylene or C.sub.2 -C.sub.7 -alkylene interrupted by Y; R.sub.4 is hydrogen or lower alkyl; R.sub.5 is hydrogen, optionally substituted lower alkyl, aryl-lower alkyl, biaryl-lower alkyl, cycloalkyl-lower alkyl, bicycloalkyl-lower alkyl, aryloxy-lower alkyl, or aryl-C.sub.2 -C.sub.7 -alkyl in which C.sub.2 -C.sub.7 -alkyl is interrupted by Y; R.sub.6 is hydrogen, lower alkyl or aryl-lower alkyl; and pharmaceutically acceptable salts thereof, which are useful as cysteine cathepsin inhibitors ##STR1##
Introduction: The Cathepsins are a group of lysosomal thiol proteinases or endopeptidases found in extracts of various tissues.Cathepsins, with the…
1CPJ: Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design.
The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors.
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A cDNA library was established from human kidney RNA and screened with an extended oligonucleotide probe derived from the amino-acid sequence of human cathepsin H. A recombinant clone, pRF15, was isolated and characterized. DNA sequence analysis of its 1106-nucleotide-long insert revealed that pRF15 …
Cathepsin G binds to human lymphocytes.: Cathepsin G is a serine protease located in the azurophil granules of neutrophils. We have shown previously that cathep
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This unit describes an assay for the direct and selective detection of the four cathepsins B, H, K, and L in adherently growing cells
Mouse Polyclonal Anti-Cathepsin A/Lysosomal Carboxypeptidase A Antibody. Validated: WB. Tested Reactivity: Human. 100% Guaranteed.
J:162893 Baston-Buest DM, Schanz A, Buest S, Fischer JC, Kruessel JS, Hess AP, The embryos cystatin C and F expression functions as a protective mechanism against the maternal proteinase cathepsin S in mice. Reproduction. 2010 Apr;139(4):741-8 ...
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Human CTSB full-length ORF (NP_001899.1, 1 a.a. - 339 a.a.) recombinant protein with GST-tag at N-terminal. (H00001508-P02) - Products - Abnova
Livestock infection by the parasitic fluke Fasciola hepatica causes major economic losses worldwide. The excretory-secretory (ES) products produced by F. hepatica are key players in understanding the host-parasite interaction and offer targets for chemo- and immunotherapy. For the first time, subproteomics has been used to compare ES products produced by adult F. hepatica in vivo, within ovine host bile, with classical ex host in vitro ES methods. Only cathepsin L proteases from F. hepatica were identified in our ovine host bile preparations. Several host proteins were also identified including albumin and enolase with host trypsin inhibitor complex identified as a potential biomarker for F. hepatica infection. Time course in vitro analysis confirmed cathepsin L proteases as the major constituents of the in vitro ES proteome. In addition, detoxification proteins (glutathione transferase and fatty acid-binding protein), actin, and the glycolytic enzymes enolase and glyceraldehyde-3-phosphate ...
TY - JOUR. T1 - Co-distribution of cysteine cathepsins and matrix metalloproteases in human dentin. AU - Scaffa, Polliana Mendes Candia. AU - Breschi, Lorenzo. AU - Mazzoni, Annalisa. AU - Vidal, Cristina de Mattos Pimenta. AU - Curci, Rosa. AU - Apolonio, Fabianni. AU - Gobbi, Pietro. AU - Pashley, David. AU - Tjäderhane, Leo. AU - Tersariol, Ivarne Luis dos Santos. AU - Nascimento, Fábio Dupart. AU - Carrilho, Marcela Rocha. PY - 2017/2/1. Y1 - 2017/2/1. N2 - It has been hypothesized that cysteine cathepsins (CTs) along with matrix metalloproteases (MMPs) may work in conjunction in the proteolysis of mature dentin matrix. The aim of this study was to verify simultaneously the distribution and presence of cathepsins B (CT-B) and K (CT-K) in partially demineralized dentin; and further to evaluate the activity of CTs and MMPs in the same tissue. The distribution of CT-B and CT-K in sound human dentin was assessed by immunohistochemistry. A double-immunolabeling technique was used to identify, ...
Podosomes mediate cell migration and invasion by coordinating the reorganization of actin cytoskeleton and focal matrix degradation. MMP and serine proteases have been found to function at podosomes. The lysosomal cysteine cathepsins, a third major class of matrix-degrading enzymes involved in tumor invasion and tissue remodeling, have yet to be linked to podosomes with the exception of cathepsin K in osteoclasts. Using inhibitors and shRNA-mediated depletion, we show that cathepsin B participates in podosomes-mediated focal matrix degradation and invasion in v-Src-transformed fibroblasts. We observed that lysosomal marker LAMP-1 localized at the center of podosome rosettes protruding into extracellular matrix using confocal microscopy. Time-lapse live-cell imaging revealed that lysosomal vesicles moved to and fused with podosomes. Disruption of lysosomal pH gradient with Bafilomycin A1, chloroquine, or ammonium chloride greatly enhanced the formation of podosomes and increased the matrix degradation.
Cathepsins in general are of interest to parasitologists, as there is considerable evidence that they play a key role in the biology of parasites [29]. In this study, a CB of C. sinensis was cloned and overexpressed in E. coli. It was classified as CB due to its sequence homology to cathepsin B protein and structure. The putative amino acid sequence shared 63%, 52% and 50% identities with cathepsin B from S. japonicum, H. sapiens and F. hepatica, respectively. Sequence analysis showed that Cs CB has typical catalytic residue of cysteine, histidine and asparagine, as well an occluding loop that is the signature of cathepsin Bs [30]. A haemoglobinase motif which is shared by helminth blood-feeders could be found in this deduced sequence [31]. Since C. sinensis generally feed on bile and epithelial cells rather than blood, however, it is thought that this motif may be an important tool for identifying potential hemoglobinases and contribute to haemoglobin degradation [32]. The occluding loop is a ...
l-Asparaginase is a key therapeutic agent for treatment of childhood acute lymphoblastic leukemia (ALL). There is wide individual variation in pharmacokinetics, and little is known about its metabolism. The mechanisms of therapeutic failure with l-asparaginase remain speculative. Here, we now report that 2 lysosomal cysteine proteases present in lymphoblasts are able to degrade l-asparaginase. Cathepsin B (CTSB), which is produced constitutively by normal and leukemic cells, degraded asparaginase produced by Escherichia coli (ASNase) and Erwinia chrysanthemi. Asparaginyl endopeptidase (AEP), which is overexpressed predominantly in high-risk subsets of ALL, specifically degraded ASNase. AEP thereby destroys ASNase activity and may also potentiate antigen processing, leading to allergic reactions. Using AEP-mediated cleavage sequences, we modeled the effects of the protease on ASNase and created a number of recombinant ASNase products. The N24 residue on the flexible active loop was identified as ...
The intracellular domains of the membrane-anchoring regions of some precursors of epidermal growth factor (EGF) family members have intrinsic biologic activities. We have determined the role of the human proEGF cytoplasmic domain (proEGFcyt) as part of the proEGF transmembrane-anchored region (proEGFctF) in the regulation of motility and elastinolytic invasion in human thyroid cancer cells. We found proEGFctF to act as a negative regulator of motility and elastin matrix penetration and the presence of proEGFcyt or proEGF22.23 resulted in a similar reduction in motility and elastinolytic migration. This activity was counteracted by EGF-induced activation of EGF receptor signaling. Decreased elastinolytic migratory activity in the presence of proEGFctF and proEGFcyt/proEGF22.23 coincided with decreased secretion of elastinolytic procathepsin L. The presence of proEGFctF and proEGFcyt/proEGF22.23 coincided with the specific transcriptional up-regulation of t-SNARE member SNAP25. Treatment with ...
Buy cathepsin H Inhibitors from Santa Cruz. These inhibit cathepsin H and may affect a variety of other cellular metabolism and protein degradation related proteins.
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase activity. It can also act as a carboxydipeptidase, like cathepsin B, but has been shown to preferentially cleave substrates through a monopeptidyl carboxypeptidase pathway. The propeptide region of cathepsin X, the shortest among papain-like peptidases, is covalently attached to the active site cysteine in the inactive form of the enzyme. Little is known about the biological function of cathepsin X. Some studies point to a role in early tumorigenesis. A more recent study indicates that cathepsin X expression is restricted to immune cells suggesting a role in phagocytosis and the regulation of the immune response. ...
Mouse monoclonal Cathepsin K antibody (Clone 3F9) validated for WB, IHC and ELISA, specific for Human Cathepsin K, produced in vitro, azide-free.
On the basis of these findings, we pursued the hypothesis that VSV particles containing GP118K are an intermediate in the CatB-dependent entry pathway. This hypothesis predicts that the GP118K-containing particles should bypass a block to infection of cells in which presumptive GP1 cleavage by cellular CatB and/or CatL is inhibited. Accordingly, we treated cells with inhibitor to reduce CatB activity to ∼10% and CatL activity to undetectable levels, and we then challenged those cells with CatL-treated VSV particles containing increasing amounts of GP118K (Fig. 2D). Infection of these cells was enhanced in a GP118K-dependent manner, indicating that GP1 cleavage is an essential step in entry. In contrast, we observed little or no GP118K-dependent enhancement of infection in cells with ∼100% CatL or ∼100% CatB, indicating that the required intracellular cleavage of GP1 that is mimicked by in vitro GP1→GP118K cleavage is mediated by CatL and/or CatB.. VSV particles containing GP118K remain ...
CTSB - CTSB (GFP-tagged) - Human cathepsin B (CTSB), transcript variant 5 available for purchase from OriGene - Your Gene Company.
Todays study seeks to research the role of cathepsin L in glutamate receptor-induced transcription factor nuclear factor-kappa B (NF-B) activation and excitotoxicity in rats striatal neurons. degradation and phosphorylation, adjustments in the degrees of IKK, p-IKK, TP53, caspase-3, beclin1, p62, and LC3II/LC3I. The results show that QA-induced lack of striatal neurons were inhibited by Z-FF-FMK […]. Read More ». ...
Todays study seeks to research the role of cathepsin L in glutamate receptor-induced transcription factor nuclear factor-kappa B (NF-B) activation and excitotoxicity in rats striatal neurons. degradation and phosphorylation, adjustments in the degrees of IKK, p-IKK, TP53, caspase-3, beclin1, p62, and LC3II/LC3I. The results show that QA-induced lack of striatal neurons were inhibited by Z-FF-FMK […]. Read More ». ...
Machleidt, W.; Assfalg-Machleidt, Irmgard; Billing, A.; Fröhlich, D.; Jochum, Marianne; Joka, T. und Nast-Kolb, Dieter (1993): The role of lysosomal cysteine proteinases as markers of macrophage activation and as non-specific mediators of inflammation. In: Faist, E.; Meakins, J. und Schildberg, F. W. (Hrsg.): Host Defence Dysfunction in Trauma, Shock and Sepsis. Berlin, Heidelberg: Springer. S. 459-463 [PDF, 1MB] ...
Buy anti-CTSC antibody, Rabbit anti-Bovine Cathepsin C Polyclonal Antibody-AAQ08887.1 (MBS573038) product datasheet at MyBioSource, Primary Antibodies. Application: Immunoprecipitation (IP)
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Their ebook Opposing to require nucleic longitudinal acids, receptor and helix of Single sequences and protein scientists is internal to recombinant sites. The internal ebook to select different true constructs over the longitudinal baculoviral cells makes penalized non-profit conceptual cathepsin acids. Their ebook to contact complete time-to-event requirements, model and leptin of future changes and increment mHost-XS cleaves important to 6th data.
TY - JOUR. T1 - Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis. AU - Farges, M C AU - Balcerzak, Denis Pierre. AU - Fisher, B D AU - Attaix, D AU - Bechet, D AU - Ferrara, M AU - Baracos, V E PY - 2002/2. Y1 - 2002/2. N2 - Rat gastrocnemius showed increased protein degradation (+75-115%) at 48 h after traumatic injury. Injured muscle showed increased cathepsin B activity (+327%) and mRNA encoding cathepsin B (+670%), cathepsin L (+298%), cathepsin H (+159%), and cathepsin C (+268%). In in situ hybridization, cathepsin B mRNA localized to the mononuclear cell infiltrate in injured muscle, and only background levels of hybridization were observed either over muscle cells in injured tissue or in uninjured muscle. Immunogold/electron microscopy showed specific staining for cathepsin B only in lysosome-like structures in cells of the mononuclear cell infiltrate in injured muscle. Muscle cells were uniformly negative in the ...
AbstractCardiovascular disease is responsible for the majority of deaths in the developed world. Particularly in patients with chronic kidney disease (CKD), the imbalance of calcium and phosphate may accelerate both vascular and valve inflammation and calcification. One in two patients with CKD are reported as dying from cardiovascular causes due to the resulting acceleration in the development of atherosclerosis plaques. In addition, CKD patients on hemodialysis are prone to aortic valve calcification and often need valve replacement before they undergo kidney transplantation. The lysosomal proteases, cathepsins, are composed of 11 cysteine members (cathepsin B, C, F, H, K, L, O, S, V, W, and Z), as well as serine proteases cathepsin A and G, which cleave peptide bonds with serine as the amino acid, and aspartyl proteases D and E, which use an activated water molecule bound to aspartate to break peptide substrate. Cysteine proteases, also known as thiol proteases, degrade protein via the deprotonation
The first part of this thesis addresses the design and synthesis of amine building blocks accomplished by applying two different synthetic procedures, both of which were developed using solid-phase chemistry. Chapter 1 presents the first of these methods, entailing a practical solid-phase parallel synthesis route to N-monoalkylated aminopiperidines and aminopyrrolidines achieved by selective reductive alkylation of primary and/or secondary amines. Solid-phase NMR spectroscopy was used to monitor the reactions for which a new pulse sequence was developed. The second method, reported in Chapter 2, involves a novel approach to the synthesis of secondary amines starting from reactive alkyl halides and azides. The convenient solid-phase protocol that was devised made use of the Staudinger reaction in order to accomplish highly efficient alkylations of N-alkyl phosphimines or N-aryl phosphimines with reactive alkyl halides.. The second part of the thesis describes the design and synthesis of three ...
Apoptosis was inhibited in rat cardiomyocytes pretreated with the aspartic protease inhibitor pepstatin A and subsequently exposed to naphthazarin (5,8-dihydroxy-1,4-naphthoquinone). Cathepsin D was released from lysosomes to the cytosol upon exposure to naphthazarin, and the enzyme activity decreased simultaneously. Later, cathepsin D reappeared in granules of increased size, and enzyme activity was restored. Activation of caspase-3- like proteases was detected, and the number of cells showing apoptotic morphology increased with time. Pepstatin A pretreatment did not prevent release of cathepsin D from lysosomes but did significantly inhibit subsequent naphthazarin-induced caspase activation and apoptotic morphology. This suggests that cathepsin D exerts its apoptosis-stimulating effect upstream of caspase-3-like activation. (C) 2000 Academic Press.. ...
Mutants of Caenorhabditis elegans having about 10% of wild-type activity of the aspartyl protease cathepsin D have been isolated by screening. Mutant homozygotes have normal growth rates and no obvious morphological or developmental abnormalities. The mutant gene (cad-1) has been mapped to the right extremity of linkage group II. Heterozygous animals (cad-1/+) show intermediate enzyme levels and animals heterozygous for chromosomal deficiencies of the right extremity of linkage group II have 50% of wild-type activity. Cathepsin D purified from a mutant strain has a lower activity per unit mass of pure enzyme. These data suggest that cad-1 is a structural gene for cathepsin D. ...
NARANJO, D et al. COMPARATIVE PROTEIN STRUCTURE MODELLING OF CATHEPSIN B FROM Fasciola hepatica. Rev Salud Anim. [online]. 2007, vol.29, n.1, pp.58-64. ISSN 0253-570X.. Cathepsin B was selected as a possible new therapeutic target of Fasciola hepatica. This is a cystein excretion protease present in the early phases of the parasite. First, we propose a three-dimensional model by homology of the cathepsin B of F.hepatica, by using as templates cathepsins B of human and rat (1PBH, 2PBH and 3PBH, 1MIR) from PDB (protein data bank). Its quality was checked by WHAT IF and a total final energy was -6750.96 KJ/mol as measure by GROMOS96. The active site (Cys 104, His 275, Asn 295) and amino acids involved in its stabilization by hydrogen bonds (Val 107, Phe 250, Gly 302), were identified. Also its secondary structure was predicted. The three-dimensional model could be employed in order to perform virtual screening by means of docking programs and data bases of virtual chemical compounds of the type ...
Authors: Therese Featherston, Reginald Marsh, Bede van Schaijik, Helen D. Brasch, Swee T. Tan and Tinte Itinteang. Frontiers in Medicine. July 2017. Volume 4, Article 100 doi: 10.3389/fmed.2017.00100. http://journal.frontiersin.org/article/10.3389/fmed.2017.00100/full. The GMRI has previously demonstrated the putative presence of two cancer stem cell (CSC) subpopulations within moderately differentiated oral tongue squamous cell carcinoma (MDOTSCC), which express components of the renin-angiotensin system (RAS).. In this study we investigated the expression and localisation of the proteases cathepsins B, D, and G in relation to these CSC subpopulations within MDOTSCC.. We identified the presence of cathepsins B and D in the CSCs and cathepsin G on what are phenotypically mast cells. The identification of these suggests the presence of bypass loops for the RAS. Consistent with our other findings with respect to the control of the RAS, this represents an additional area of regulation as part of a ...
Lysosomal cysteine cathepsins belong to a family of 11 human proteolytic enzymes. Some of them correlate with progression in a variety of cancers and therefore are considered as potential therapeutic targets. Until recently, the contribution of individual cathepsins to tumorigenesis and tumor progression remained unknown. By crossing various types of mouse cancer models with mice where specific cathepsins have been ablated, we contributed to this gap of knowledge and will summarize the results in this report. The employed models are the Rip1-Tag2 model for pancreatic neuroendocrine tumors, the K14-HPV16 model for squamous skin and cervical cancers, and the MMTV-PyMT model for metastasizing breast cancer, the KPC model for pancreatic ductal adenocarcinoma, and the APC(min) mice developing early stages of intestinal neoplasia. All models harbor mutations in relevant tumor suppressors and/or cell-type specific expression of potent oncogenes, which initiate de novo carcinogenesis in the targeted ...
These methods were optimized as previously. described with some modification [27]. For both methods, each mass spectrum was obtained from the sum of 10 scans of 150 laser shots each and using 512 K data points. Typically, the target plate offset was 100 V with the deflector plate set at 180 V. The ion funnels operated at 100 V and 6.0 V, respectively, with the skimmers at 15 and 5 V. The analyzer entrance was maintained at −7 V, and side kick technology was used to further optimize peak shape and signal intensity. The two acquisition settings differentiate for the trapping potentials (LM, 0.6 and 0.55 V; Alpelisib datasheet HM, 0.95 and 0.80 V), the required excitation power (LM, 25%; HM, 28%) and pulse time (LM, 10 μs; HM, 20 μs), the time of flight to the ICR cell (LM, 1.350 ms; HM, 2.700 ms) and the quadrupole filter mass (LM, m/z 1300; HM, m/z 2500). For each spotted sample, two duplicate spots were measured using the LM and the other two using the HM. Approximately 4.5 h were needed to ...
The catalytic activation of some caspases and cathepsins in human and mouse monocytes undergoing M-CSF-driven differentiation generates 2 NPM1 fragments that contribute to the differentiated phenotype by decreasing the migration, motility, and bacteria phagocytosis capabilities of the resting cells. As soon as the macrophage is activated by LPS, the proteolytic process is stopped, and the native NPM1 negatively regulates cytokine and chemokine gene expression and their secretion; that is, the full-length NPM1 is a transcriptional corepressor that maintains the right amount of cytokine gene expression.. Proteolysis of cellular components by cysteine proteases, including various combinations of caspases and cathepsins, has been associated with specific pathways of cell differentiation.23,24 Caspases and cathepsins are activated along M-CSF-driven differentiation of human peripheral blood monocytes.2,3,25 One of the protease targets in this differentiation context is NPM1,5 the proteolysis of which ...
African animal trypanosomiasis is a major threat to African agriculture causing a loss estimated to 4.5 billion US$ per annum. Trypanosoma congolense is the major causative agent in African animal trypanosomiasis and is transmitted by tsetse flies of the Glossina spp. Congopain, a major cathepsin L-like cysteine peptidase in T. congolense is associated with trypanotolerance in NDama cattle and is a target for an anti-disease vaccine. It is suggested that trypanotolerant cattle control the disease by antibody mediated neutralisation of congopain, and that immunisation of cattle against congopain can mimic trypanotolerance resulting in minimised disease pathology. Susceptible cattle immunised with recombinant catalytic domain of congopain, C2, produced high levels of anti-congopain IgG specific antibodies against congopain, maintained weight and exhibited less severe anaemia. However, there was no effect on the establishment of T. congolense infection and acute anaemia development in ...
TY - JOUR. T1 - Effects of insulin on protein degradation and lysosomal cathepsin D in perfused skeletal muscle. AU - Li, J. B.. AU - Rannels, S. R.. AU - Burkart, M. E.. AU - Jefferson, L. S.. PY - 1975/1/1. Y1 - 1975/1/1. UR - http://www.scopus.com/inward/record.url?scp=0016610685&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0016610685&partnerID=8YFLogxK. M3 - Article. AN - SCOPUS:0016610685. VL - 34. SP - No.654. JO - Federation Proceedings. JF - Federation Proceedings. SN - 0014-9446. IS - 3. ER - ...
We infused microgram quantities of active or inactive PMN elastase and cathepsin G into the renal arteries of rats. Both active and inactive elastase localized to the glomerular capillary wall equally, and in amounts that could be achieved physiologically in GN. However, elastase-perfused rats developed marked proteinuria (196 +/- 32 mg/24 h) compared with control rats receiving inactive elastase (19 +/- 2 mg/24 h, p less than 0.005). Similar results were seen with active and inactive cathepsin G. Neither elastase nor cathepsin G infusion was associated with histologic evidence of glomerular injury. We conclude that the PMN neutral serine proteinases elastase and cathepsin G can mediate marked changes in glomerular permeability in vivo due to their proteolytic activity, and thus, may contribute to the proteinuria observed in PMN-dependent models of GN. ...
The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and kininogens. This gene encodes a stefin that functions as an intracellular thiol protease inhibitor. The protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. The protein is thought to play a role in protecting against the proteases leaking from lysosomes. Evidence indicates that mutations in this gene are responsible for the primary defects in patients with progressive myoclonic epilepsy (EPM1). One type of mutation responsible for EPM1 is the expansion in the promoter region of this gene of a CCCCGCCCCGCG repeat from 2-3 copies to 30-78 copies. [provided by RefSeq, Jul 2016 ...
Of these hydrolytic enzymes, cathepsin K is of most importance. Cathepsin K and other cathepsins[edit]. Cathepsin K is a ... Several other cathepsins are expressed in osteoclasts including cathepsins B, C, D, E, G, and L. The function of these cysteine ... characterised by a lack of functional cathepsin K expression. Knockout studies of cathepsin K in mice lead to an osteopetrotic ... Studies on cathepsin L knockout mice have been mixed, with a report of reduced trabecular bone in homozygous and heterozygous ...
... , Histones & Cathepsin; PMAP The Proteolysis Map-animation [ Recent chromatin publications and news] Protocol for in ...
... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...
Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... Miller, J.J.; Changaris, D.G.; Levy, R.S. (1992). "Purification, subunit structure and inhibitor profile of cathepsin-A". J. ... Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ...
Cathepsin E. TALE homeodomain transcription factors. Hydrocortisone. Since keratinocyte differentiation inhibits keratinocyte ... "The role of cathepsin E in terminal differentiation of keratinocytes". Biological Chemistry. 392 (6): 571-85. doi:10.1515/BC. ...
Cathepsin D is involved in CLN10. DNA analysis can be used to help confirm the diagnosis of Batten disease. When the mutation ...
... s were discovered in 1884 by Albrecht Kossel.[17] The word "histone" dates from the late 19th century and is derived from the German word "Histon", a word itself of uncertain origin - perhaps from the Greek histanai or histos. In the early 1960s, before the types of histones were known and before histones were known to be highly conserved across taxonomically diverse organisms, James F. Bonner and his collaborators began a study of these proteins that were known to be tightly associated with the DNA in the nucleus of higher organisms.[18] Bonner and his postdoctoral fellow Ru Chih C. Huang showed that isolated chromatin would not support RNA transcription in the test tube, but if the histones were extracted from the chromatin, RNA could be transcribed from the remaining DNA.[19] Their paper became a citation classic.[20] Paul T'so and James Bonner had called together a World Congress on Histone Chemistry and Biology in 1964, in which it became clear that there was no consensus on the ...
Lushbaugh, W.B.; Hofbauer, A.F.; Pittman, F.E. (1985). "Entamoeba histolytica: purification of cathepsin B". Exp. Parasitol. 59 ...
Mediation by cathepsin G has been suggested. The treatment of RAS usually involves administering dexamethasone IV, with the ...
... these include cathepsin L, papain, and procaricain. It forms an alpha-helical domain that runs through the substrate-binding ...
McDonald, J.K.; Zeitman, B.B.; Reilly, T.J.; Ellis, S. (1969). "New observations on the substrate specificity of cathepsin C ( ... Planta, R.J.; Gorter, J.; Gruber, M. (1964). "The catalytic properties of cathepsin C". Biochim. Biophys. Acta. 89: 511-519. ... Metrione, R.M.; Neves, A.G.; Fruton, J.S. (1966). "Purification and properties of dipeptidyl transferase (cathepsin C)". ... Dipeptidyl peptidase I (EC 3.4.14.1, cathepsin C, dipeptidyl aminopeptidase I, dipeptidyl transferase, dipeptide arylamidase I ...
The protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. The protein ... 1994). "Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status ... 1988). "Cathepsin D inactivates cysteine proteinase inhibitors, cystatins". Biochem. Biophys. Res. Commun. 154 (2): 765-72. doi ... Cystatin B has been shown to interact with Cathepsin B. GRCh38: Ensembl release 89: ENSG00000160213 - Ensembl, May 2017 GRCm38 ...
These cysteine proteases include calpain, caspase, and cathepsin. These three proteins are examples of detectable signs of ...
It is an inhibitor of cathepsin K, an enzyme involved in bone resorption. It is being developed by Merck & Co. The phase III ... Le Gall, C. L.; Bonnelye, E.; Clézardin, P. (2008). "Cathepsin K inhibitors as treatment of bone metastasis". Current Opinion ... February 2008). "The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K". Bioorg. Med. Chem. Lett. 18 (3 ...
A plant aspartic proteinase resembling mammalian cathepsin D". Eur. J. Biochem. 202 (3): 1021-1027. doi:10.1111/j.1432- ...
2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ... 2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ... by proteases such as cathepsins. Collagen is a component of epithelial and endothelial basement membranes. Endostatin, as a ...
Cathepsin A is also required for normal elastin biosynthesis. GRCh38: Ensembl release 89: ENSG00000170266 - Ensembl, May 2017 ... The elastin receptor complex includes S-Gal, neuraminidase and Cathepsin A. When elastin-derived peptides bind to the S-Gal ... cathepsin) A is required for proper elastic fiber formation and inactivation of endothelin-1". Circulation. 117 (15): 1973-81. ...
add NAE ref]. She pursued these interests by studying androsterone and monopalmitin at Armour, and cathepsin C at Yale. Jones ... Under the direction of Joseph S. Fruton, Jones' dissertation research involved the catalytic properties of cathepsin C, a type ... Her doctorate was entitled: Transamidation reactions catalyzed by cathepsin C. Jones completed her studies in three years ... Transamidation Reactions Catalyzed by Cathepsin C. Yale University, 1952. Kresge, Nicole; Simoni, Robert D.; Hill, Robert L. ( ...
1982). "Action of rat liver cathepsin L on glucagon". Acta Biol. Med. Ger. 40 (9): 1139-43. PMID 7340337. Kaushal GP, Walker PD ...
... cathepsin G and proteinase 3" Bioorg. Med. Chem. 1995, 3, 187-193. ([5]) Schapira, C. B.; Perillo, I. A.; Lamdan, S. "3-Oxo-1,2 ... cathepsin G and proteinase 3. Phthalimide derivatives were seen to be inactive, while saccharin derivatives were seen to be ...
2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ...
Deficiency of Cathepsin K, a cysteine protease in osteoclasts, is known to cause this condition. Cathepsin K became a much ... Motyckova, G; Fisher, DE (2002). "Pycnodysostosis: role and regulation of cathepsin K deficiency in osteoclast function and ... is a lysosomal storage disease of the bone caused by a mutation in the gene that codes the enzyme cathepsin K. Pycnodysostosis ... a lysosomal storage disease caused by cathepsin K deficiency". Science. 273 (5279): 1236-1238. doi:10.1126/science.273.5279. ...
1990). "Generation of human endothelin by cathepsin E". FEBS Lett. 273 (1-2): 99-102. doi:10.1016/0014-5793(90)81060-2. PMID ...
Several other cathepsins are expressed in osteoclasts including cathepsins B, C, D, E, G, and L. The function of these cysteine ... Of these hydrolytic enzymes, cathepsin K is of most importance. Cathepsin K is a collagenolytic, papain-like, cysteine protease ... characterised by a lack of functional cathepsin K expression. Knockout studies of cathepsin K in mice lead to an osteopetrotic ... Cathepsin K has an optimal enzymatic activity in acidic conditions. It is synthesized as a proenzyme with a molecular weight of ...
Cathepsin B and L play a crucial role in arthritic cartilage degeneration. The inhibitor of cathepsin isolated from this fungus ... The fungal metabolite, aurantiamide acetate, has been isolated from Aspergillus penicillioides, as a cathepsin inhibitor. ... a Selective Cathepsin Inhibitor, Produced by Aspergillus penicillioides". Bioscience, Biotechnology, and Biochemistry. 65 (5): ...
... cathepsin G". Blood. 93 (6): 2089-97. PMID 10068683. Tan J, Prakash MD, Kaiserman D, Bird PI (July 2013). "Absence of SERPINB6A ... antitrypsin to inhibit cathepsin proteases". Biochemistry. 41 (15): 4998-5004. doi:10.1021/bi0159985. PMID 11939796. Schick C, ... "Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chymotrypsin-like proteinases cathepsin G and mast cell ... "DNA accelerates the inhibition of human cathepsin V by serpins". The Journal of Biological Chemistry. 282 (51): 36980-6. doi: ...
"Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... 2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal ... Cathepsin W is a protein that in humans is encoded by the CTSW gene.[5][6][7] ...
PLS is caused by mutations in the cathepsin C (CTSC) gene. Dipeptidyl-peptidase I encoded by the CTSC gene removes dipeptides ... Mutation analysis of the cathepsin C gene in Indian families with Papillon-Lefèvre syndrome ... Mutation analysis of the cathepsin C gene in Indian families with Papillon-Lefèvre syndrome. In: BMC Medical Genetics, 4 (5). ...
A functional role for cathepsin B was confirmed by the ability of CA074, a cell impermeable and highly selective cathepsin B ... Here we explored a role for active cathepsin B on the cell surface in the invasiveness of IBC. We examined expression of the ... Our study is the first to show that the proteolytic activity of cathepsin B and its co-expression with caveolin-1 contributes ... A statistically significant co-expression of cathepsin B and caveolin-1 was found in IBC patient biopsies, thus validating our ...
First, we propose a three-dimensional model by homology of the cathepsin B of F.hepatica, by using as templates cathepsins B of ... NARANJO, D et al. COMPARATIVE PROTEIN STRUCTURE MODELLING OF CATHEPSIN B FROM Fasciola hepatica. Rev Salud Anim. [online]. 2007 ... Cathepsin B was selected as a possible new therapeutic target of Fasciola hepatica. This is a cystein excretion protease ... Palabras clave : Fasciola hepatica; cathepsin B proteases; comparative protein structure modelling; protein data bank. ...
Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode.pdf(1186KB). --. -- ... In this study, we identified a cDNA encoding for a cathepsin L-like cysteine protease from the T solium metacestode (TsCL-1) ... In this study, we identified a cDNA encoding for a cathepsin L-like cysteine protease from the T solium metacestode (TsCL-1) ... Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode.pdf ...
Legumain, cathepsin B and L were analyzed in cell lysates by immunoblotting and their enzymatic activities were analyzed by ... In contrast, cathepsin B activity was not affected. Furthermore, invasion was suppressed in cystatin E/M over-expressing ... High activity of cysteine proteases such as legumain and the cathepsins have been shown to facilitate growth and invasion of a ... cathepsin B and L were expressed and active in most of the cell lines, although at low levels in the melanomas expressing ...
Only cathepsin L proteases from F. hepatica were identified in our ovine host bile preparations. Several host proteins were ... Western blotting of in vitro and in vivo ES proteins showed only cathepsin L proteases were recognized by serum pooled from F. ... Time course in vitro analysis confirmed cathepsin L proteases as the major constituents of the in vitro ES proteome. In ... and further confirms the potential of the cathepsin L proteases as therapy candidates. ...
... hepatica cathepsin B and amoebapore proteins, as novel vaccine candidates against F. hepatica formulated in an adjuvant ... F. hepatica cathepsin B is mainly expressed in metacercariae and newly excysted juveniles whilst cathepsin L is mainly ... Cathepsin B proteases of flukes: the key to facilitating parasite control? Trends Parasitol. 2010;26(10):506-14.View Article ... F. hepatica cathepsin B and amoebapore-like proteins were selected as vaccine candidates in the present study. According to the ...
TY - JOUR. T1 - Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes. T2 - Dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells. AU - Thiele, Dwain L. AU - Lipsky, Peter E.. PY - 1990. Y1 - 1990. N2 - Exposure of murine or human lymphocytes to L-leucyl-L-leucine methyl ester (Leu-Leu-OMe) results in selective killing of cytotoxic lymphocytes, whereas helper T cells and B cells remain functionally intact. Cytolytic lymphocytes incubated in the presence of toxic concentrations of Leu-Leu-OMe were found to contain membranolytic metabolites of the structure (Leu-Leu)n-OMe, where n ≥ 3. The sensitivity of cytotoxic lymphocytes to Leu-Leu-OMe was found to be dependent upon production of these metabolites by a lysosomal thiol protease, dipeptidyl peptidase I, which is present at far higher levels in cytotoxic lymphocytes than in cells without cytolytic potential or not of bone marrow origin. Thus, this granule enzyme is ...
Human cathepsin B2 ELISA Kit;Human cathepsin IV ELISA Kit;Human cathepsin Y ELISA Kit;Human cathepsin Z1 ELISA Kit;Human ... Human cathepsin P ELISA Kit;Human cathepsin X ELISA Kit;Human CTSX ELISA Kit;Human cathepsin Z ELISA Kit;Human carboxypeptidase ... The concentration of Cathepsin Z (CTSZ) in the samples is then determined by comparing the O.D. of the samples to the standard ... The microtiter plate provided in this kit has been pre-coated with an antibody specific to Cathepsin Z (CTSZ). Standards or ...
Cathepsin: Cathepsins ( Ancient Greek kata- "down" and hepsein "boil"; abbreviated CTS ) are proteases ( enzymes that degrades ... Cathepsins have a vital role in mammalian cellular turnover, e.g. bone resorption. They degrade polypeptides and are ... There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone ...
"Entrez Gene: CTSD cathepsin D".. *^ Barrett AJ (April 1970). "Cathepsin D. Purification of isoenzymes from human and chicken ... Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes.[7] The main function of cathepsin D is ... The optimum pH for cathepsin D in vitro is 4.5-5.0.[13] Cathepsin-D is an aspartic protease that depends critically on ... Cathepsin D is a protein that in humans is encoded by the CTSD gene.[5][6] This gene encodes a lysosomal aspartyl protease ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Cathepsin A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) ... Cathepsin H (cysteine protease) Cathepsin K (cysteine protease) Cathepsin L1 (cysteine protease) Cathepsin L2 (or V) (cysteine ... Cathepsin S (cysteine protease) Cathepsin W (cysteine proteinase) Cathepsin Z (or X) (cysteine protease) Cathepsins have been ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...
Cathepsin Cathepsin T at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Cathepsin T (EC 3.4.22.24) is an enzyme. This enzyme catalyses the following chemical reaction Interconversion of the three ... Pitot, H.C.; Gohda, E. (1987). "Cathepsin T". Methods Enzymol. 142: 279-289. doi:10.1016/s0076-6879(87)42038-7. PMID 2885716. ...
Incubation with the cathepsin L specific inhibitor, Z-FY-DMK, blocked cathepsin L signals, confirming the cathepsin L bands in ... Z-FY-DMK cathepsin L inhibitor does not inhibit all cathepsin activity of murine endometriotic lesions. Incubation with Z-FY- ... DMK, a selective inhibitor of cathepsin L, inhibited many of the cathepsin active bands but did not block all active cathepsin ... E-64 blocks all cathepsin proteolytic activity in murine endometriotic lesions. Incubation with the broad cathepsin inhibitor, ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
cathepsin L2. Names. cathepsin L2, preproprotein. cathepsin U. NP_001188504.1. *EC 3.4.22.43 ... using cathepsin V and cathepsin L as model enzymes, a series of chimeras were generated to identify noncatalytic regions that ... functions of cathepsin V are controlled by N-glycosylation Title: Determination of cathepsin V activity and intracellular ... CTSV cathepsin V [Homo sapiens] CTSV cathepsin V [Homo sapiens]. Gene ID:1515 ...
V. Zavanik-Bergant, A. Sekirnik, R. Golouh, V. Turk, and J. Kos, "Immunochemical localisation of cathepsin S, cathepsin L and ... Both stimulants caused a significant cathepsin S upregulation. A significantly elevated cathepsin S expression in gingival ... Role of Cathepsin S in Periodontal Inflammation and Infection. S. Memmert,1,2 A. Damanaki,1 A. V. B. Nogueira,3 S. Eick,4 M. ... "Antimicrobial peptide LL-37 is both a substrate of cathepsins S and K and a selective inhibitor of cathepsin L," Biochemistry, ...
Cathepsin K degrades both collagen and elastin, and is one of the most powerful proteases. Cathepsin S degrades elastin, and ... "We saw that the cathepsin K was going away much faster when there was cathepsin S present than when it was by itself," said ... "We kept increasing the amount of cathepsin S until the collagen was not affected at all because all of the cathepsin K was ... Barrys modeling suggested that effects observed could occur if cathepsin S were degrading cathepsin K instead of attacking the ...
Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Graham Simmons, Dhaval N. Gosalia, ... Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Graham Simmons, Dhaval N. Gosalia, ... Cathepsin-L-specific inhibitor blocks infection. (A) MDL28170 inhibits CTSL activity with an IC50 of 2.5 nM. A 1,000-compound ... Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry Message Subject (Your Name) has sent you ...
A direct immunohistochemical method of high specificity is presented for the demonstration of sites of cathepsin B1. Antisera ... Snellman, O.: Cathepsin B, the lysosomal thiol proteinase of calf liver. Biochem. J. 114, 673-678 (1969)Google Scholar ... Otto, K.: Cathepsins B1 and B2. In: Tissue proteinases, ed. by A. J. Barrett and J. T. Dingle, p. 1-28. North-Holland ... V. Cathepsin B as a potential effector of LNA hydrolysis. Histochemie 12, 240-243 (1968)Google Scholar ...
Rabbit polyclonal Cathepsin E antibody. Validated in WB, IHC, ICC/IF and tested in Mouse, Rat, Human. Cited in 3 publication(s ... Anti-Cathepsin E antibody (ab36996) at 1/1000 dilution + Murine reticulocyte lysate at 10 µg. Predicted band size: 42 kDa. ... High Expression of Cathepsin E in Tissues but Not Blood of Patients with Barretts Esophagus and Adenocarcinoma.. Ann Surg ... Cathepsin E is expressed abundantly in the stomach, Clara cells and alveolar macrophages of the lung, brain microglia, spleen, ...
Rabbit polyclonal Cathepsin D antibody validated for WB, ELISA, IHC, ICC/IF and tested in Human. Referenced in 1 publication ... This antibody reacts with human liver cathepsin D, and does not react with cathepsins B, H and L. ... IHC image of Cathepsin D staining in Human Lung formalin fixed paraffin embedded tissue section, performed on a Leica Bond™ ... Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Cathepsin D antibody (ab19555) ...
Protease activity Apolipoprotein A-I Aortic valve stenosis Cathepsin S C. Gebhard and F. Maafi contributed equally to this work ... Hooshdaran B, Kolpakov MA, Guo X, Miller SA, Wang T, Tilley DG, Rafiq K, Sabri A (2017) Dual inhibition of cathepsin G and ... Lindstedt L, Lee M, Oorni K, Bromme D, Kovanen PT (2003) Cathepsins F and S block HDL3-induced cholesterol efflux from ... Targeting circulating cathepsin S may lead to new therapies for human aortic valve disease. ...
  • The microtiter plate provided in this kit has been pre-coated with an antibody specific to Cathepsin Z (CTSZ). (biobool.com)
  • Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody specific to Cathepsin Z (CTSZ). (biobool.com)
  • After TMB substrate solution is added, only those wells that contain Cathepsin Z (CTSZ), biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. (biobool.com)
  • We observed that uPA, uPAR and enzymatically active cathepsin B were colocalized in caveolae fractions isolated from SUM149 cells. (uwindsor.ca)
  • Our study is the first to show that the proteolytic activity of cathepsin B and its co-expression with caveolin-1 contributes to the aggressiveness of IBC. (uwindsor.ca)
  • A functional role for cathepsin B was confirmed by the ability of CA074, a cell impermeable and highly selective cathepsin B inhibitor, to significantly reduce pericellular proteolysis and invasion by SUM149 cells. (uwindsor.ca)
  • Legumain, cathepsin B and L were expressed and active in most of the cell lines, although at low levels in the melanomas expressing cystatin E/M. In the melanoma lines where cystatin E/M was secreted, cystatin C was generally absent or expressed at a very low level. (uio.no)
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