Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.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 L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.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).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 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.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.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.Cathepsin G: A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.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.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.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.Benzoylarginine-2-Naphthylamide: An enzyme substrate which permits the measurement of peptide hydrolase activity, e.g. trypsin and thrombin. The enzymes liberate 2-naphthylamine, which is measured by colorimetric procedures.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.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.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.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 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.2,2'-Dipyridyl: A reagent used for the determination of iron.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).Ribonuclease H, Human Immunodeficiency Virus: A ribonuclease activity that is a component of the HIV REVERSE TRANSCRIPTASE. It removes the RNA strand of the RNA-DNA heteroduplex produced by reverse transcription. Once the RNA moiety is removed a double stranded DNA copy of the HIV RNA can be synthesized.BoliviaRibonuclease H: A ribonuclease that specifically cleaves the RNA moiety of RNA:DNA hybrids. It has been isolated from a wide variety of prokaryotic and eukaryotic organisms as well as RETROVIRUSES.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.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.Lysosomal Storage Diseases: Inborn errors of metabolism characterized by defects in specific lysosomal hydrolases and resulting in intracellular accumulation of unmetabolized substrates.Blood Proteins: Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.Carboxypeptidases: Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.Microchemistry: The development and use of techniques and equipment to study or perform chemical reactions, with small quantities of materials, frequently less than a milligram or a milliliter.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.BooksPublishing: "The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.MEDLINE: The premier bibliographic database of the NATIONAL LIBRARY OF MEDICINE. MEDLINE® (MEDLARS Online) is the primary subset of PUBMED and can be searched on NLM's Web site in PubMed or the NLM Gateway. MEDLINE references are indexed with MEDICAL SUBJECT HEADINGS (MeSH).Serial Publications: Publications in any medium issued in successive parts bearing numerical or chronological designations and intended to be continued indefinitely. (ALA Glossary of Library and Information Science, 1983, p203)Biological Science Disciplines: All of the divisions of the natural sciences dealing with the various aspects of the phenomena of life and vital processes. The concept includes anatomy and physiology, biochemistry and biophysics, and the biology of animals, plants, and microorganisms. It should be differentiated from BIOLOGY, one of its subdivisions, concerned specifically with the origin and life processes of living organisms.Impulse Control Disorders: Disorders whose essential features are the failure to resist an impulse, drive, or temptation to perform an act that is harmful to the individual or to others. Individuals experience an increased sense of tension prior to the act and pleasure, gratification or release of tension at the time of committing the act.East Timor: A country in Southeastern Asia, northwest of Australia in the Lesser Sunda Islands at the eastern end of the Indonesian archipelago. It includes the eastern half of the island of Timor, the Oecussi (Ambeno) region on the northwest portion of the island of Timor, and the islands of Pulau Atauro and Pulau Jaco. On May 20, 2002, East Timor was internationally recognized as an independent state. This followed its declared independence from Portugal on November 20, 1975 and a period of armed conflict with Indonesia.Human Rights Abuses: Deliberate maltreatment of groups of humans beings including violations of generally-accepted fundamental rights as stated by the Universal Declaration of Human Rights, adopted and proclaimed by the United Nations General Assembly resolution 217 A (III) of 10 December 1948.Anger: A strong emotional feeling of displeasure aroused by being interfered with, injured or threatened.Aggression: Behavior which may be manifested by destructive and attacking action which is verbal or physical, by covert attitudes of hostility or by obstructionism.Explosive Agents: Substances that are energetically unstable and can produce a sudden expansion of the material, called an explosion, which is accompanied by heat, pressure and noise. Other things which have been described as explosive that are not included here are explosive action of laser heating, human performance, sudden epidemiological outbreaks, or fast cell growth.Guanfacine: A centrally acting antihypertensive agent with specificity towards ADRENERGIC ALPHA-2 RECEPTORS.Thyroid Neoplasms: Tumors or cancer of the THYROID GLAND.Saudi ArabiaCarcinoma, Papillary: A malignant neoplasm characterized by the formation of numerous, irregular, finger-like projections of fibrous stroma that is covered with a surface layer of neoplastic epithelial cells. (Stedman, 25th ed)Carcinoma, Papillary, Follicular: A thyroid neoplasm of mixed papillary and follicular arrangement. Its biological behavior and prognosis is the same as that of a papillary adenocarcinoma of the thyroid. (From DeVita Jr et al., Cancer: Principles & Practice of Oncology, 3d ed, p1271)Thyroid Gland: A highly vascularized endocrine gland consisting of two lobes joined by a thin band of tissue with one lobe on each side of the TRACHEA. It secretes THYROID HORMONES from the follicular cells and CALCITONIN from the parafollicular cells thereby regulating METABOLISM and CALCIUM level in blood, respectively.Adenocarcinoma, Follicular: An adenocarcinoma of the thyroid gland, in which the cells are arranged in the form of follicles. (From Dorland, 27th ed)Carcinoma: A malignant neoplasm made up of epithelial cells tending to infiltrate the surrounding tissues and give rise to metastases. It is a histological type of neoplasm but is often wrongly used as a synonym for "cancer." (From Dorland, 27th ed)

The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C. (1/90)

Recent studies have shown that the bovine cysteine proteinase inhibitor, cystatin C, is synthesized as a preprotein containing a 118-residue mature protein. However, the forms of the inhibitor isolated previously from bovine tissues had shorter N-terminal regions than expected from these results, and also lower affinity for proteinases than human cystatin C. In this work, we report the properties of recombinant, full-length bovine cystatin C having a complete N-terminal region. The general characteristics of this form of the inhibitor, as reflected by the isoelectric point, the far-ultraviolet circular dichroism spectrum, the thermal stability and the changes of tryptophan fluorescence on interaction with papain, resembled those of human cystatin C. The affinity and kinetics of inhibition of papain and cathepsins B, H and L by the bovine inhibitor were also comparable with those of the human inhibitor, although certain differences were apparent. Notably, the affinity of bovine cystatin C for cathepsin H was somewhat weaker than that of human cystatin C, and bovine cystatin C bound to cathepsin L with about a four-fold higher association rate constant than the human inhibitor. This rate constant is comparable with the highest values reported previously for cystatin-cysteine proteinase reactions. The full-length, recombinant bovine cystatin C bound appreciably more tightly to proteinases than the shorter form characterized previously. Digestion of the recombinant inhibitor with neutrophil elastase resulted in forms with truncated N-terminal regions and appreciably decreased affinity for papain, consistent with the forms of bovine cystatin C isolated previously having arisen by proteolytic cleavage of a mature, full-length inhibitor.  (+info)

Cysteine proteinase cathepsin H in tumours and sera of lung cancer patients: relation to prognosis and cigarette smoking. (2/90)

In order to evaluate the role of cysteine peptidase cathepsin H (Cath H) in human lung cancer its protein levels were determined in 148 pairs of lung tumour tissue and adjacent non-tumourous lung parenchyma using the enzyme-linked immunosorbent assay technique. Additionally, Cath H levels were determined in sera of 171 patients with malignant tumours, 34 patients with benign lung diseases and 47 healthy controls. The median level of Cath H in tumour tissue was 0.64 times that in the corresponding lung parenchyma. Relating tumour levels with histological type we found higher Cath H levels in small-cell and adenocarcinomas and lower levels in squamous cell carcinoma, large-cell carcinoma and secondary tumours. A significant difference in Cath H level between lung tumour tissue and non-tumourous lung parenchyma was associated with the group of cigarette smokers (156 vs 263 ng mg(-1) protein, P < 0.001). For this group of patients Cath H tumour levels correlated with the survival rate, while for the entire patient population this was not the case. Smokers with high tumour levels of Cath H experienced poor survival. Cath H was significantly higher in sera of patients with malignant and benign lung diseases than in control sera (P < 0.001). The increase was significant for all histological types, being the highest in small-cell and squamous cell carcinomas. Our study reveals that in lung tumours there is different behaviour of Cath H compared with other cysteine peptidases, e.g. cathepsin B and cathepsin L. Variations between tissue and serum levels of Cath H indicate either reduced expression or enhanced secretion of this enzyme in lung tumours.  (+info)

Alterations in cathepsin H activity and protein patterns in human colorectal carcinomas. (3/90)

Our analyses of cathepsin H activity levels and protein forms in human colorectal cancers compared to matched control mucosa support the concept that altered proteinase expression patterns may reflect both cancer stage and site. Cathepsin H-specific activity was significantly increased in colorectal cancers compared to control mucosa (P = 0.003; n = 77). Highest specific activities and cancer/normal ratios (C/N) for activity were measured in Dukes' B and C stage carcinomas, cancers involved in local spread and invasion to lymph nodes. In contrast, cathepsin B and L activities analysed in the same paired extracts had been shown to be most frequently elevated in earlier stage carcinomas (Dukes' A and B), confirming that cathepsin H demonstrates a distinct pattern of expression during colorectal cancer progression. Although cathepsin H activities were most commonly elevated in Dukes' C cancers at all colon sites, both specific activity and C/N ratios were significantly higher for cancers of the left colon compared to other colon locations. A subset of 43 paired extracts analysed on Western blots also revealed consistent changes in cathepsin H protein forms in cancers. Normal mucosa typically showed a strong protein doublet at 31 and 29 kDa while cancers demonstrated decreased expression or total loss of the 31 kDa protein (90% of cases), equal or increased expression of the 29-kDa protein (67% of cases) and the new appearance or up-regulation of a cathepsin H band at 22 kDa (78% of cases). C/N ratios for cathepsin H enzyme activity correlated significantly with C/N ratios for the 29 kDa mature single-chain protein form (P < 0.001), with increased activity most commonly associated with elevated expression of 29-kDa cathepsin H but also with up-regulation of the 22-kDa band, suggesting a shift to more fully processed, mature active cathepsin H protein forms in cancers. Changes in cathepsin H expression were also detected by immunohistochemistry as elevated cathepsin H staining in tumour epithelial cells.  (+info)

Differential expression patterns of cathepsins B, H, K, L and S in the mouse ovary. (4/90)

Cathepsins B, H, K, L and S belong to a family of lysosomal cysteine proteinases which participate in a variety of proteolytic processes, including degradation of extracellular matrix. Although the presence of cathepsin mRNAs in the ovary has been reported earlier, very little information is available on their temporospatial expression. In the present study, Northern analysis revealed cyclic changes in the mRNA levels for cathepsins B, H, K, L and S during the 4-day oestrous cycle in the mouse ovary. Immunohistochemical localization revealed distinct expression patterns suggesting different functions for the cathepsins studied. Cathepsin B was predominantly seen in the germinal epithelium throughout the oestrous cycle. Upon follicular maturation, an increasing number of granulosa cells became positive for all cathepsins. Strong cathepsin H staining was sharply defined in theca externa which also stained for cathepsins K and S. Corpus luteum was the predominant location of cathepsin L. The distribution of cathepsin S resembled that of cathepsin L. The developing oocyte stained positive for all cathepsins. In-situ hybridization confirmed the differential production of cathepsin mRNAs by granulosa, thecal and luteal cells. These complex temporal and spatial expression patterns at different stages of the oestrous cycle and follicular development suggest divergent functions for specific cathepsins in follicular development, growth and rupture.  (+info)

Expression patterns of cathepsins B, H, K, L and S in the human endometrium. (5/90)

Cathepsins B, H, K, L and S belong to the family of lysosomal cysteine proteinases and participate in a variety of proteolytic processes, including degradation of the extracellular matrix (ECM). In the present study, we used Northern hybridization to demonstrate the presence of mRNAs for cathepsins B, H, K, L and S in human endometrium during both the proliferative and secretory phases of menstrual cycle. The mRNA levels for cathepsins H and K were significantly lower in secretory phase endometrium in comparison with proliferative phase endometrium. Immunohistochemical localization of the different cathepsins revealed widespread distribution of all cathepsins in both stroma and epithelial cells. The immunoreactivity for cathepsins B, H and K exhibited changes related to endometrial location and/or to the phase of the cycle. The strongest immunoreactivity for cathepsins B, H, L and S was observed in the surface epithelium of the endometrium. The staining for cathepsins was predominantly intracellular, but immunoreactivity was also detected on the surface of small lymphoid cells in the stroma. The findings of the present study suggest that cysteine cathepsins are needed for normal development and function of human endometrium during both the proliferative and secretory phases.  (+info)

Analysis of a truncated form of cathepsin H in human prostate tumor cells. (6/90)

Increased expression of proteases has been correlated with the malignant progression of a variety of tumors. We found a significant increase in cathepsin H expression in high-grade prostatic intraepithelial neoplasia and carcinoma of the prostate. Two forms of cathepsin H, the full-length form (CTSH) and a truncated form with a 12-amino acid deletion in its signal peptide region (CTSHDelta10-21), were identified by cDNA sequence analysis. This deletion occurred not at the genomic level but likely at the RNA processing level. Both forms are expressed in prostate tissues as well as LNCaP, PC-3, and DU-145 prostate cancer cell lines. The deletion within the signal peptide region affected the trafficking of cathepsin H. Fluorescence microscopy, subcellular fractionation, and activity data indicated that the truncated form was perinuclear and secreted and had a reduced lysosomal association as compared with the full-length cathepsin H. Furthermore, the truncated cathepsin H was enzymatically active. Therefore, an increase in overall cathepsin H expression, particularly in the truncated form with a high secretion propensity, may affect cell biological behaviors such as those associated with tumor progression.  (+info)

Expression of cathepsins B, H, K, L, and S during human fetal lung development. (7/90)

Cathepsins are involved in lysosomal protein degradation, proenzyme activation, antigen processing, and hormone maturation. They are secreted by tumor cells and macrophages and catalyze the remodeling of extracellular matrix proteins. To gain insight into the expression pattern of cathepsins during fetal lung development, the expression of cathepsins B, H, K, L, and S at protein and mRNA levels were evaluated by using immunohistochemistry and in situ hybridization. Early expression of cathepsins B, H, and K was found in epithelial cells of the branching presumptive bronchi (<12th week of gestation). The most intense cathepsin K-specific immunoreactivity was found in developing airways with a lumen. Cathepsin K was found in epithelial cells only, whereas in contrast, cathepsins B and H were detected both in epithelial and interstitial cells. During fetal maturation, interstitial cells displayed cathepsin L immunoreactivity and, in the saccular phase (>26th week of gestation), both cathepsin L and S immunoreactivities. A continuous decline in the proportion of cathepsin H-positive interstitial CD68-positive cells was observed. These discrete temporal and spatial variations in cathepsin expression during organogenesis of the human lung indicate different physiological roles for the individual enzymes in different cell types and developmental stages.  (+info)

Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis. (8/90)

OBJECTIVE: Modification with proteases and cholesterylesterase transforms LDL to a moiety that resembles lipoproteins isolated from atherosclerotic lesions and possesses atherogenic properties. To identify changes in monocyte-derived foam cells laden with enzymatically modified LDL (E-LDL), we compared patterns of the most abundant transcripts in these cells after incubation with LDL or E-LDL. METHODS AND RESULTS: Serial analyses of gene expression (SAGE) libraries were constructed from human monocytes after treatment with LDL or E-LDL. Several tags were differentially expressed in LDL-treated versus E-LDL-treated cells, whereby marked selective induction by E-LDL of cathepsin H was conspicuous. We show that cathepsin H is expressed in atherosclerotic lesions in colocalization with E-LDL. Furthermore, we demonstrate that LDL modified with cathepsin H and cholesterylesterase can confer onto LDL the capacity to induce macrophage foam cell formation and to induce cathepsin H. CONCLUSIONS: Cathepsin H could contribute to the transformation of LDL to an atherogenic moiety; the process might involve a self-sustaining amplifying circle.  (+info)

*Osteoclast

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 ...

*Histone

... 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 ...

*Batten disease

Cathepsin D is involved in CLN10.[9]. *DNA analysis can be used to help confirm the diagnosis of Batten disease. When the ...

*Retinoic acid syndrome

Mediation by cathepsin G has been suggested. The treatment of RAS usually involves administering dexamethasone IV, with the ...

*Chromatin

... , Histones & Cathepsin; PMAP The Proteolysis Map-animation [ Recent chromatin publications and news] Protocol for in ...

*Polysulfated glycosaminoglycan

... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...

*Carboxypeptidase C

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, ...

*Amentoflavone

It is also an inhibitor of human cathepsin B. Amentoflavone has a variety of in vitro activities including antimalarial ... "Amentoflavone and its derivatives as novel natural inhibitors of human Cathepsin B". Bioorg. Med. Chem. 13 (20): 5819-5825. doi ...

*Keratinocyte

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. ...

*Histolysain

Lushbaugh, W.B.; Hofbauer, A.F.; Pittman, F.E. (1985). "Entamoeba histolytica: purification of cathepsin B". Exp. Parasitol. 59 ...

*Protease inhibitor (biology)

... these include cathepsin L, papain, and procaricain. It forms an alpha-helical domain that runs through the substrate-binding ...

*Dipeptidyl-peptidase I

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 ...

*Katepsin-D - Википедија, слободна енциклопедија

Katepsin-D (EC 3.4.23.5, Cathepsin D) je enzim.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju ... Takahashi, T. & Tang, J. (1981). „Cathepsin D from porcine and bovine spleen". Methods Enzymol. 80: 565-581. PMID 7341918.. ... Barrett, A.J. (1977). „Cathepsin D and other carboxyl proteinases". Ур.: Barrett, A.J. Proteinases in Mammalian Cells and ... Barrett, A.J. (1977). „Cathepsin D and other carboxyl proteinases". Ур.: Barrett, A.J. Proteinases in Mammalian Cells and ...

*Cystatin B

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 ...

*Neuroproteomics

These cysteine proteases include calpain, caspase, and cathepsin. These three proteins are examples of detectable signs of ...

*Odanacatib

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 ...

*Phytepsin

A plant aspartic proteinase resembling mammalian cathepsin D". Eur. J. Biochem. 202 (3): 1021-1027. doi:10.1111/j.1432- ...

*Endostatin

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 ...

*GLB1

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. ...

*Mary Ellen Jones (chemist)

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. ( ...

*MEP1A

1982). "Action of rat liver cathepsin L on glucagon". Acta Biol. Med. Ger. 40 (9): 1139-43. PMID 7340337. Kaushal GP, Walker PD ...

*Gabriel-Colman rearrangement

... 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 ...

*Collagen, type XVIII, alpha 1

2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ...

*Pycnodysostosis

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. ...

*Endothelin 3

1990). "Generation of human endothelin by cathepsin E". FEBS Lett. 273 (1-2): 99-102. doi:10.1016/0014-5793(90)81060-2. PMID ...
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 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. ...
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 …
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Abcam provides specific protocols for Cathepsin H overexpression 293T lysate (whole cell) (ab94088) : Transfected Lysate Preparation Notes
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.
Cathepsin H antibody (cathepsin H) for IHC-P, WB. Anti-Cathepsin H pAb (GTX33065) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
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We investigated whether p21 cooperates with a p53 mutant. R273H is a naturally occurring mutation that abolishes the DNA binding and thus the trans‐activating activity of p53 [3]. Therefore, in contrast to p53wt expression, p53R273H expression in H1299 cells failed to induce p21 and Mdm2 (Fig 4D, left). Slug protein levels and cellular invasiveness were not markedly altered after expressing p53R273H, but decreased when p53R273H and p21 were co‐expressed. Consistent with this, p53R273H and p21 co‐expression elevated Slug ubiquitination to considerably higher levels than p53R273H expression alone did (Fig 4D, right). These results provide support for the ability of p53R273H to cooperate with p21 in promoting Slug ubiquitination/degradation and thus suppressing cell invasion. Our data also suggest that p53 can contribute to tumor suppression even after the loss of its trans‐activating activity. However, our results are in contrast with a previous report that shRNA‐mediated knockdown of ...
Kevin Benedict is an opinionated futurist, Principal Analyst at the Center for Digital Intelligence™, C4DIGI.com, emerging technologies analyst, and digital transformation and business strategy consultant. In the past 8 years he has taught workshops for large enterprises and government agencies in 18 different countries, and is a keynote speaker at conferences worldwide. He spent nearly 5 years working as a Senior Analyst at Cognizant (CTSH), and 2 years serving in Cognizants Center for the Future of Work where he wrote many reports, hundreds of articles, interviewed technology experts, and produced videos on the future of digital technologies and their impact on industries. He has written articles published in The Guardian, wrote the Forward to SAP Press book titled "Mobilizing Your Enterprise with SAP", published over 3,000 articles and was featured as thought leader and digital strategist in the Department of Defenses IQT intelligence journal. Kevin lectures and leads workshops, teaches ...
2007 12 06.392177 08 17 24.39 -05 44 03.6 23.4V 15BY518 645 C~2scb 2007 12 06.393006 08 17 24.40 -05 44 03.5 15BY518 645 C~2scb 2007 12 06.395494 08 17 24.39 -05 44 03.7 15BY518 645 C~2scb 2008 01 01.313332 08 15 42.86 -05 47 43.1 22.6V 15BY518 645 C~2scb 2008 01 01.314161 08 15 42.87 -05 47 43.1 15BY518 645 C~2scb 2008 01 01.316649 08 15 42.85 -05 47 43.2 15BY518 645 C~2scc 2014 01 04.54955 08 54 52.487 -06 24 34.13 21.8G 15BY518 F51 C~2qbh 2014 04 05.25388 08 48 39.785 -05 39 14.33 22.2G 15BY518 F51 C~2qbh 2014 12 16.59004 09 02 47.110 -06 28 17.89 22.0G 15BY518 F51 C~2qbh 2014 12 30.50769 09 01 58.726 -06 29 59.22 21.7G 15BY518 F51 C~2qbh 2015 01 19.47348 09 00 29.231 -06 27 57.56 22.3w 15BY518 F51 C~1vYC 2015 01 19.48481 09 00 29.183 -06 27 57.36 22.5w 15BY518 F51 C~1vYC 2015 01 19.49615 09 00 29.119 -06 27 57.43 22.3w 15BY518 F51 C~1vYC 2015 01 19.50762 09 00 29.069 -06 27 57.02 22.1w 15BY518 F51 C~1vYC 2015 01 21.49804 09 00 19.278 -06 27 27.74 22.0w 15BY518 F51 C~1vYC 2015 01 21.51155 09 ...
PubMed 24936061. T. Fløyel, C. Brorsson, L.B. Nielsen, M. Miani, C.H. Bang-Berthelsen, M. Friedrichsen, A.J. Overgaard, L.A. Berchtold, A. Wiberg, P. Poulsen, L. Hansen, S. Rosinger, B.O. Boehm, R. Ram, Q. Nguyen, M. Mehta, G. Morahan, P. Concannon, R. Bergholdt, J.H. Nielsen, T. Reinheckel, M. von Herrath, A. Vaag, D.L. Eizirik, H.B. Mortensen, J. Størling, F. Pociot. CTSH regulates β-cell function and disease progression in newly diagnosed type 1 diabetes patients. Proc Natl Acad Sci U S A. 2014 Jul 15;111(28):10305-10. Epub 2014 Jun 30 ...
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Introduction: The Cathepsins are a group of lysosomal thiol proteinases or endopeptidases found in extracts of various tissues.Cathepsins, with the…
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] ...
Tyroserleutide TFA, isolated from the degradation products of porcine spleen, is a small molecular tripeptide which inhibits tumor growth both in vitro and in vivo. - Mechanism of Action & Protocol.
Protein expression of CDK1 and p-CDK1 in rat spleens.(A) Western blot determination of CDK1 and p-CDK1 protein expression in control and aniline-treated rats. (
Dr. Pimple Popper just posted a video to Instagram that shows her popping a spitting cyst on a mans cheek. The mans pimple was actually inflamed, and the sac had to be removed entirely.
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 ...
1CPJ: CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN
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 ...
Porcine spleen cells induced with Newcastle disease virus F strain could produce an antiviral substance. The substance was sensitive to trypsin and did not penetrate the dialyser. These indicated that it was characteristic of an Interferon. The antiviral activity of crude porcine spleen cell interferon(PSIFN)was 1.3×10~5u/ml on porket kidney cells. PSIFN production was significantly enhanced by pretreating cells with porcine IFN. The crude PSIFN was less stable to low pH treatment, to 56℃ and to 0.1% SDS. I...
The ICOS-B7h costimulatory receptor-ligand pair is required for germinal center formation, the production of isotype-switched antibodies, and antibody affinity maturation in response to T cell-dependent antigens. However, the potentially distinct roles of regulated B7h expression on B cells and dendritic cells in T cell-dependent antibody responses have not been defined. We generated transgenic mice with lineage-restricted B7h expression to assess the cell-type specific roles of B7h expression on B cells and dendritic cells in regulating T cell-dependent antibody responses. Our results show that endogenous B7h expression is reduced on B cells after activation in vitro and is also reduced in vivo on antibody-secreting plasma B cells in comparison to both naïve and germinal center B cells from which they are derived. Increasing the level of B7h expression on activated and plasma B cells in B-B7hTg mice led to an increase in the number of antibody-secreting plasma cells generated after immunization and a
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 ...
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 ...
Preferential solvation of di-2-pyridylketonebenzoyl hydrazone was investigated in aqueous-ethanol binary mixtures . The kinetics and mechanism of the hydrolysis of a series of substituted furfurylidenefuroyl hydrazones (X-FFH) in 25% (v/v) ethanol-buffer mixtures have been studied by ultraviolet visible spectrophotometry at different temperatures in the range 22-500C. The hydrolysis reactions were found to follow first-order kinetics. The effect of pH, molecular structure and temperature on the rate of hydrolysis have been discussed. A mechanism for the hydrolysis is postulated in which the attack of water on the protonated substrate is subject to general acid-base catalysis using HCl-sodium acetate buffer solution. The hydrolysis of 5-Chlorothiophenylidene salicoyl hydrazone (CTSH) was found to obey specific acid catalysis using HCl-KCl buffer solutions. The observed rate constants and the catalytic rate constants with respect to H+, HC2O4- and H2C2O4 were calculated. Activation energy and ...
1CPJ: Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design.
This unit describes an assay for the direct and selective detection of the four cathepsins B, H, K, and L in adherently growing cells
rat Cathepsin D/CTSD gene cDNA, cloning vector & expression plasmid, mutiple tags. Optimized for high expression in mammalian cells. Save up to 60%.
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 ...
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 ...
article{b6a0ecd9-da63-4a19-b309-0a87b322a637, abstract = {A polymorphism in the coding region of the human cystatin D gene has been detected by direct sequencing of amplified DNA from different individuals. The variation, resulting from a T/C transition in exon 1 of the gene, causes an amino acid variation, Cys/Arg, at the protein level. An allele-specific oligonucleotide hybridization assay was developed and used to demonstrate this polymorphism in the population. The deduced frequencies were 0.55 and 0.45 for the Cys and Arg variant-encoding alleles, respectively.}, author = {Balbin, Milagros and Freije, José P and Abrahamson, Magnus and Velasco, Gloria and Grubb, Anders and Lopez-Otin, Carlos}, issn = {1432-1203}, language = {eng}, number = {6}, pages = {668--669}, publisher = {Springer}, series = {Human Genetics}, title = {A sequence variation in the human cystatin D gene resulting in an amino acid (Cys/Arg) polymorphism at the protein level}, url = {http://dx.doi.org/10.1007/BF00202491}, ...
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 ...
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. ...
By using a monoclonal antibody we have identified a new polypeptide doublet (C4h and C4l) of Mr approximately 21 kD and pI 8 and 7, respectively, that is associated with and (at the immunofluorescence level) uniformly distributed on actin filament bundles in rat, mouse, and other vertebrate species. C4 is absent in neurones, erythrocytes, and skeletal muscle but the epitope is evolutionarily conserved as it is present in invertebrates such as molluscs and crustaceans. C4h is not found in cells such as lymphocytes and oncogenically transformed mesenchymal cells where actin stress fiber bundles are reduced in number or absent. C4l, on the other hand, is always present. C4h expression can also be blocked by switching normal nontransformed mesenchymal cells from adherent to suspension culture. Reexpression of C4h occurs 24 h after these cells are returned to normal adherent culture conditions, but can be blocked by either actinomycin D or cycloheximide, suggesting that the expression of this epitope ...
In the nervous system, FA2H is specifically expressed in myelinating cells, and the postnatal upregulation of FA2H expression follows a similar time course as described for oligodendrocyte-specific genes involved in the synthesis of the myelin sheath, e.g., CGT and PLP (Eckhardt et al., 2005; Alderson et al., 2006). Furthermore, upregulation of the FA2H gene expression correlates with the increase in HFA during postnatal brain development (Alderson et al., 2006). FA2H−/− mice lack HFA-GalC and HFA-sulfatide in the brain and peripheral nerves, confirming the hypothesis that FA2H is responsible for HFA-sphingolipid synthesis in the nervous system. Oligodendrocytes lacking HFA-sphingolipids, however, differentiated normally in vivo, as shown by a normal time course of myelin gene expression during postnatal development and normal numbers of oligodendrocyte precursor cells and mature oligodendrocytes in the brain. Moreover, we found no structural abnormalities of myelin at the ultrastructural ...
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Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. It is a member of the cysteine cathepsin protease family, which has 11 members. As one of the 11 cathepsins, cathepsin Z contains distinctive features from others. Cathepsin Z has been reported involved in cancer malignancy and inflammation. The CTSZ gene is located at 20q13.32 on chromosome 20, consisting of 6 exons. At least two transcript variants of this gene have been found, but the full-length nature of only one of them has been determined. Cathepsin Z is characterized by an unusual and unique 3-amino acid insertion in the highly conserved region between the glutamine of the putative oxynion hole and the active site cysteine. The pro-region of cathepsin Z shares no significant similarity with other cathepsin family sequences. It contains only 41 amino acid residues without the conserved motif of ERFNIN or GNFD found in other cysteine proteinases. Besides, the proregion sequence ...
From NCBI Gene:. The protein encoded by this gene is a lysosomal cysteine proteinase involved in bone remodeling and resorption. This protein, which is a member of the peptidase C1 protein family, is predominantly expressed in osteoclasts. However, the encoded protein is also expressed in a significant fraction of human breast cancers, where it could contribute to tumor invasiveness. Mutations in this gene are the cause of pycnodysostosis, an autosomal recessive disease characterized by osteosclerosis and short stature. [provided by RefSeq, Apr 2013]. From UniProt: ...
|p||strong|CA-074|/strong|, a specific cathepsin B inhibitor, also abolished the neurotoxic effects caused by Abeta42-activated BV2 cell [1]. Co-treatment of cultures with the cathepsin B inhibitors CA-074 or Z-FA-FMK suppressed the cytostatic effects of
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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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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. ...
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?
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 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.
The present invention relates to isolated polypeptides having aminopeptidase activity and isolated nucleic acid sequences encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as methods for producing and using the polypeptides.
Novel Aspartic Proteinase of the PepSIN Family (Napsin A, or NAPSA) belongs to the peptidase A1 family and plays a role in pneumocyte surfactant processing. It is also known as aspartyl protease 4 (ASP4), KAP, Kdap, napsin-1, NAP1, NAPA, and SNAPA. Two closely related proteins are known, Napsin A and Napsin B. Napsin A is a single-chain, 38-kDa protein. It is expressed at high levels in human lung and kidney, and at lower levels in spleen. Napsin A expression has been detected in type II pneumocytes and in lung adenocarcinomas.. ...
Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-hurler polydystrophy) are caused by mutations in the GlcNAc-phosphotransferase alpha / beta -subunits precursor gene. Kudo M, Brem MS, Canfield WM Am J Hum Genet. 2006 Mar;78(3):451-63. For more information on Mucolipidosis II and mucolipidosis IIIA, please visit OMMBID Chapter 138. Thank you very much in advance […]. ...
Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase C1 family. In humans, it is encoded by the CTSC gene. Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Cathepsin C catalyses excision of dipeptides from the N-terminus of protein and peptide substrates, except if (i) the amino group of the N-terminus is blocked, (ii) the site of cleavage is on either side of a proline residue, (iii) the N-terminal residue is lysine or arginine, or (iv) the structure of the peptide or protein prevents further digestion from the N-terminus. The cDNAs encoding rat, human, murine, bovine, dog and two Schistosome cathepsin Cs have been cloned and sequenced and show that the enzyme is highly conserved. The human and rat cathepsin C cDNAs encode precursors (prepro-cathepsin C) comprising signal peptides of 24 residues, pro-regions of 205 (rat cathepsin C) or 206 (human ...
Bombyx cysteine proteinase inhibitor: Bombyx cysteine proteinase inhibitor (BCPI) from the hemolymph of Bombyx mori; alpha and beta are two forms differing only in three amino acid residues at N terminal; amino acid sequence in first source
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
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.
From NCBI Gene:. This gene encodes a member of the peptidase C1 family and lysosomal cysteine proteinase that appears to be a central coordinator for activation of many serine proteinases in cells of the immune system. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate heavy and light chains that form a disulfide-linked dimer. A portion of the propeptide acts as an intramolecular chaperone for the folding and stabilization of the mature enzyme. This enzyme requires chloride ions for activity and can degrade glucagon. Defects in the encoded protein have been shown to be a cause of Papillon-Lefevre syndrome, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. [provided by RefSeq, Nov 2015]. From UniProt: ...
Mouse monoclonal Cathepsin K antibody (Clone 3F9) validated for WB, IHC and ELISA, specific for Human Cathepsin K, produced in vitro, azide-free.
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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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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 ...
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 ...
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 recently reported that adeno-associated virus serotype 1 (AAV1) transduction of murine nigral dopaminergic (DA) neurons with constitutively active ras homolog enriched in brain with a mutation of serine to histidine at position 16 [Rheb(S16H)] induced the production of neurotrophic factors, resulting in neuroprotective effects on the nigrostriatal DA system in animal models of Parkinsons disease (PD). To further investigate whether AAV1-Rheb(S16H) transduction has neuroprotective potential against neurotoxic inflammation, which is known to be a potential event related to PD pathogenesis, we examined the effects of Rheb(S16H) expression in nigral DA neurons under a neurotoxic inflammatory environment induced by the endogenous microglial activator prothrombin kringle-2 (pKr-2 ...
|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
Cathepsin G ELISA Kits für viele Reaktivitäten. Human, Säugetier, Maus und weitere. Cathepsin G ELISA Kits vergleichen und bestellen.
References for Abcams Human Cystatin C ELISA Kit (ab119589). Please let us know if you have used this product in your publication
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 ...
The chemical formula for sodium salicylate is C7H5NaO3. All of the numbers in the chemical formula for sodium salicylate are subscript numbers in accordance with standard chemical formula...
Hi Tina, I always resuspend oligos at about 100 µM in TE (pH 8.0) then aliqout and store at -20°C. Tim Tina wrote: , I study the expression of TNFa in porcine spleen cells. There is only two , papers who gives the sequence of primers to use. I tested these 2 primers , set. I got a signal for first three PCR reactions, but after (e.g. other , PCR reactions with the same cDNA) the PCR signal (band intensity) decreased , until it disappears. , I diluted the primers in sterile water. The primers were used at 0.25uM, , dNTP at 5mM, TAQ (Perkin Elmer) 0.75 units and with Perkin Elmer buffer. , Total volume : 25 uL. The PCR reaction, RTases and electrophoresis on , agarose are good since our positive control (human) are good. , Can we dilute primers in some buffer instead of water. If yes, which buffer , ? , Is there a special task with porcine primers? , Does water have any effect on the primers? , Any suggestions ? , , Thanks a lot ! ...
Papain is a medicine available in a number of countries worldwide. A list of US medications equivalent to Papain is available on the Drugs.com website.

Human CTSZ ELISA Kit | biobool.comHuman CTSZ ELISA Kit | biobool.com

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 ...
more infohttps://www.biobool.com/elisa_kit/7091.html

Cathepsins (CTS) Gene Family | HUGO Gene Nomenclature CommitteeCathepsins (CTS) Gene Family | HUGO Gene Nomenclature Committee

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 ...
more infohttps://www.genenames.org/cgi-bin/genefamilies/set/470

Cathepsin W - WikipediaCathepsin W - Wikipedia

"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] ...
more infohttps://en.wikipedia.org/wiki/Cathepsin_W

Cathepsin D - WikipediaCathepsin D - Wikipedia

"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 ...
more infohttps://en.wikipedia.org/wiki/Cathepsin_D

Cathepsin K (O35186) | InterPro | EMBL-EBICathepsin K (O35186) | InterPro | EMBL-EBI

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.
more infohttp://www.ebi.ac.uk/interpro/protein/O35186

CathePsin L family (O45734) | InterPro | EMBL-EBICathePsin L family (O45734) | InterPro | EMBL-EBI

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.
more infohttps://www.ebi.ac.uk/interpro/protein/O45734

RCSB PDB - Gene View 









 - CTSK - cathepsin KRCSB PDB - Gene View - CTSK - cathepsin K

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.
more infohttps://www.rcsb.org/pdb/gene/CTSK

Cathepsin Protease Inhibition Reduces Endometriosis Lesion Establishment.  - PubMed - NCBICathepsin Protease Inhibition Reduces Endometriosis Lesion Establishment. - PubMed - NCBI

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, ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/26482207

CTSV cathepsin V [Homo sapiens (human)] - Gene - NCBICTSV cathepsin V [Homo sapiens (human)] - Gene - NCBI

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 ...
more infohttps://www.ncbi.nlm.nih.gov/gene/1515

Enzymes Attack One Another In Cathepsin CannibalismEnzymes Attack One Another In 'Cathepsin Cannibalism'

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 ...
more infohttp://www.innovations-report.com/html/reports/life-sciences/enzymes-attack-quot-cathepsin-cannibalism-quot-200491.html

Cathepsin K Antibody
		        
	Cathepsin K Antibody

Cathepsin K Polyclonal Antibody from Invitrogen for Western Blot, Immunohistochemistry (Paraffin) and Flow Cytometry ... Protein Aliases: Cathepsin K; Cathepsin O; cathepsin O1; Cathepsin O2; Cathepsin X; CTSK; CTSO; CTSO2 ... Cite Cathepsin K Polyclonal Antibody. The following antibody was used in this experiment: Cathepsin K Polyclonal Antibody from ...
more infohttps://www.thermofisher.com/antibody/product/CTSK-Antibody-Polyclonal/PA5-14270

Anti-Cathepsin G antibody (ab231149) | AbcamAnti-Cathepsin G antibody (ab231149) | Abcam

Rabbit polyclonal Cathepsin G antibody. Validated in WB, IHC and tested in Rat, Human. Immunogen corresponding to recombinant ... Anti-Cathepsin G antibody (ab231149) at 3 µg/ml + Recombinant rat Cathepsin G protein. Secondary. HRP-Linked Guinea pig anti- ... This product Rabbit Anti-Cathepsin G antibody (ab231149) WB, IHC-P Goat Anti-Rabbit IgG H&L (HRP) (ab205718) IHC-P, WB, ELISA, ... All lanes : Anti-Cathepsin G antibody (ab231149) at 3 µg/ml. Lane 1 : Rat serum. Lane 2 : Rat heart lysate. Lane 3 : MCF7 ( ...
more infohttps://www.abcam.com/cathepsin-g-antibody-ab231149.html

Anti-Cathepsin D antibody (ab19555) | AbcamAnti-Cathepsin D antibody (ab19555) | Abcam

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) ...
more infohttp://www.abcam.com/cathepsin-d-antibody-ab19555.html

Cathepsin A (CTSA) AntikörperCathepsin A (CTSA) Antikörper

Am meisten referenzierte anti-Cathepsin A Antikörper. Show all anti-Cathepsin A (CTSA) Antikörper with Pubmed References. * ... Weitere Antikörper gegen Cathepsin A Interaktionspartner. Arabidopsis thaliana Cathepsin A (CTSA) Interaktionspartner ... Zusätzlich bieten wir Ihnen Cathepsin A Proteine (28) und Cathepsin A Kits (27) und viele weitere Produktgruppen zu diesem ... The Cathepsin C releases the glycosidases from complexes formed with cathepsin A, and reinstates their activity. ...
more infohttps://www.antikoerper-online.de/abstract/Cathepsin+A+

Cathepsin Detection Kits - MP BiomedicalsCathepsin Detection Kits - MP Biomedicals

MAGIC RED® CATHEPSIN B KIT. A fluorogenic test kit for Cathepsin B. (Patent# 6,235,493-May 22, 2001). Ref.: 1. Van Noorden, C.J ... MAGIC RED® CATHEPSIN K KIT. A fluorogenic test kit for Cathepsin K. (Patent# 6,235,493-May 22, 2001). Ref.: 1. Van Noorden, C.J ... MAGIC RED® CATHEPSIN L KIT. A fluorogenic test kit for Cathepsin L. (Patent# 6,235,493-May 22, 2001). Ref.: 1. Van Noorden, C.J ...
more infohttp://www.mpbio.com/index.php?cPath=2873_2_1999_2005_2031_2091_2235&country=223

WikiGenes - Ctsl - cathepsin LWikiGenes - Ctsl - cathepsin L

... cathepsin B), Arg-AMC (cathepsin H), and N-benzyloxycarbonyl-Phe-Arg-AMC (cathepsin L), were determined in rat lung throughout ... cathepsin-B and cathepsin-L activities [26].. *Furthermore, cathepsin L may play an important role in the degradation of the ... cathepsin B and cathepsin D. Thus, Ras utilizes different effectors to mediate transformation and to deregulate cathepsin L ... Cathepsin B-like and cathepsin L-like activities fell below control values initially, but from week 8 of the immunosuppressive ...
more infohttps://www.wikigenes.org/e/gene/e/25697.html

WikiGenes - CTSC - cathepsin CWikiGenes - CTSC - cathepsin C

Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic ... The results suggest that cathepsin L could be an important activator of DPPI in vivo and that cathepsin D and possibly the ... The enzymes, except cathepsin C, are endopeptidases (reviewed in Kirschke et al., 1995), although cathepsin B was found also to ... Mutations of the cathepsin C gene are responsible for Papillon-Lefèvre syndrome. Hart, T.C., Hart, P.S., Bowden, D.W., Michalec ...
more infohttps://www.wikigenes.org/e/gene/e/1075.html

Role of Cathepsin S in Periodontal Inflammation and InfectionRole of Cathepsin S in Periodontal Inflammation and Infection

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, ...
more infohttps://www.hindawi.com/journals/mi/2017/4786170/

Cathepsin Assay KitsCathepsin Assay Kits

BioVision develops and offers a wide variety of products including assay kits, antibodies, recombinant proteins & enzymes, and other innovative research tools for studying Apoptosis, Metabolism, Cell Proliferation, Cellular Stress, Cell Damage and Repair, Diabetes, Obesity and Metabolic Syndrome, Stem Cell Biology, Gene Regulation, Signal Transduction, etc. BioVisions products are currently being sold in more than 60 countries worldwide.
more infohttps://www.biovision.com/products/cancer-research/apoptosis-related-products/non-caspase-proteases/cathepsin/cathepsin-assay-kits.html

CTSB - Cathepsin B - Homo sapiens (Human) - CTSB gene & proteinCTSB - Cathepsin B - Homo sapiens (Human) - CTSB gene & protein

Cathepsin B. Cathepsin B, EC 3.4.22.1 (APP secretase, APPS) (Cathepsin B1) [Cleaved into: Cathepsin B light chain; Cathepsin B ... Cathepsin BImported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p>,a href="/ ... tr,E9PL32,E9PL32_HUMAN Cathepsin B (Fragment) OS=Homo sapiens OX=9606 GN=CTSB PE=1 SV=2 ...
more infohttps://www.uniprot.org/uniprot/E9PL32

Ctsg - Cathepsin G - Rattus norvegicus (Rat) - Ctsg gene & proteinCtsg - Cathepsin G - Rattus norvegicus (Rat) - Ctsg gene & protein

Cathepsin GAdd BLAST. ›26. Proteomic databases. PaxDb, a database of protein abundance averages across all three domains of ... sp,P17977,CATG_RAT Cathepsin G (Fragment) OS=Rattus norvegicus GN=Ctsg PE=1 SV=1 IIGGREARPNSHPYMAFLLIQSPEGL ...
more infohttp://www.uniprot.org/uniprot/P17977

anti-Cathepsin D Primary Antibodiesanti-Cathepsin D Primary Antibodies

Ausgesuchte Qualitäts-Hersteller für Cathepsin D Antikörper. Hier bestellen. ... Monoklonale und polyklonale Cathepsin D Antikörper für viele Methoden. ... Bezeichner auf Proteinebene für anti-Cathepsin D (CTSD) Antikörper etID16901.18 , cathepsin D , aspartic protease , cathepsin d ... cathepsin D (lysosomal aspartyl peptidase) , cathepsin D (lysosomal aspartyl protease) , prepro-cathepsin D, prepro-CD ...
more infohttps://www.antikoerper-online.de/peptide-hormone-metabolism-pathway-41/cathepsin-d-antibody-2858/

Human Cathepsin Enzyme Products - MP BiomedicalsHuman Cathepsin Enzyme Products - MP Biomedicals

CATHEPSIN L-HUMAN LIVER. Cathepsin L is unstable at neutral pH, but is relatively stable in the range 4.5 to 5.5.. ...
more infohttps://www.mpbio.com/index.php?cPath=2_2009_2882_2923&country=223

Cathepsin - WikipediaCathepsin - Wikipedia

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 ...
more infohttps://en.wikipedia.org/wiki/Cathepsin

Cathepsin A
     Summary Report | CureHunterCathepsin A Summary Report | CureHunter

Cathepsin A: A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a ... Cathepsin A. Subscribe to New Research on Cathepsin A A carboxypeptidase that catalyzes the release of a C-terminal amino acid ... 09/01/1987 - "Study of cathepsin A, B and D activities in the skin wound edges. ". 01/01/1984 - "Study of cathepsin A and D ... 02/01/2000 - "Cathepsin A activity in primary and metastatic human melanocytic tumors.". 01/01/1999 - "Cathepsin A activity in ...
more infohttp://www.curehunter.com/public/keywordSummaryD043402.do
  • 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)
  • The ultimate form of mature cathepsin D is composed of 337 amino acid residues, 196 amino acid residues in the heavy chain and 141 in the light chain. (wikipedia.org)
  • Distribution of the activity and expression of mature cathepsin L within the umbilical cord probably results from distinctions in the proenzyme activation process. (sigmaaldrich.com)
  • Cathepsin L-deficient mice were shown to have less adipose tissue, lower serum glucose and insulin levels, more insulin receptor subunits, more glucose transporter (GLUT4) and more fibronectin than wild type controls. (wikipedia.org)
  • Weight loss reduces adipose tissue cathepsin S and its circulating levels in morbidly obese women," Journal of Clinical Endocrinology and Metabolism , vol. 91, no. 3, pp. 1042-1047, 2006. (hindawi.com)
  • To test this, we used an immunocompetent endometriosis mouse model and found that endometriotic lesions exhibited a greater than 5-fold increase in active cathepsins compared to tissue from peritoneal wall or eutopic endometrium, with cathepsins L and K specifically implicated. (nih.gov)
  • Human endometriosis lesions also exhibited greater cathepsin activity than adjacent peritoneum tissue, supporting the mouse results. (nih.gov)
  • Platt's long-term research has focused on cathepsins, including the development of sensitive tools and assays to quantify their activity in cells and tissue, as well as potential diagnostic applications for breast, lung and cervical cancer. (innovations-report.com)
  • IHC image of Cathepsin D staining in Human Lung formalin fixed paraffin embedded tissue section, performed on a Leica Bond™ system using the standard protocol F. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH6, epitope retrieval solution 1) for 20 mins. (abcam.com)
  • Although a lysosomal, cathepsin B-dependent (Ctsb-dependent) pathway of apoptosis has been described, the contribution of this pathway to tissue damage remains unclear. (jci.org)
  • Our results are consistent with a model in which SARS-CoV employs a unique three-step method for membrane fusion, involving receptor-binding and induced conformational changes in S glycoprotein followed by cathepsin L (CTSL) proteolysis and activation of membrane fusion within endosomes. (pnas.org)
  • Determination of cathepsin V activity and intracellular trafficking by N-glycosylation. (nih.gov)
  • Cathepsins are involved in disease processes as varied as cancer metastasis, atherosclerosis, cardiovascular disease, osteoporosis and arthritis. (innovations-report.com)
  • Cathepsin K is the most potent mammalian collagenase. (wikipedia.org)
  • Leukocyte cathepsin S is a potent regulator of both cell and matrix turnover in advanced atherosclerosis," Arteriosclerosis, Thrombosis, and Vascular Biology , vol. 29, no. 2, pp. 188-194, 2009. (hindawi.com)
  • Decreased cathepsin V expression due to Fli1 deficiency contributes to the development of dermal fibrosis and proliferative vasculopathy in systemic sclerosis. (nih.gov)
  • Cathepsin S deficiency results in abnormal accumulation of autophagosomes in macrophages and enhances Ang II-induced cardiac inflammation," PLoS ONE , vol. 7, no. 4, Article ID e35315, 2012. (hindawi.com)
  • Cathepsin B has also been implicated in the progression of various human tumors including ovarian cancer. (wikipedia.org)
  • Cathepsins V and S may serve as auxiliary diagnostic and/or prognostic markers in thymic epithelial tumors. (nih.gov)
  • Title: Expression of cathepsins V and S in thymic epithelial tumors. (nih.gov)
  • E-64 blocks all cathepsin proteolytic activity in murine endometriotic lesions. (nih.gov)
  • The expression of cathepsin K in cultured endothelial cells is regulated by shear stress. (wikipedia.org)
  • Expression of cathepsins K, S and V within keratinocytes is reduced in photoprotected skin of aged women. (nih.gov)
  • Title: Differential expression of cathepsins K, S and V between young and aged Caucasian women skin epidermis. (nih.gov)
  • A significantly elevated cathepsin S expression in gingival biopsies from rats with experimental periodontitis was found in vivo , as compared to that from control. (hindawi.com)
  • Gingival biopsies from periodontitis patients showed a significantly higher cathepsin S expression than those from healthy gingiva. (hindawi.com)
  • The cathepsin A activity in lysates of metastatic lesions of malignant melanoma is significantly higher than in primary focus lysates. (wikipedia.org)
  • The requirement for cathepsin L proteolysis identifies a previously uncharacterized class of inhibitor for SARS-CoV infection. (pnas.org)
  • Along with Asp-protonation, lower pH also leads to conformational switch in cathepsin-D : the N-terminal segment of the protease moves out of the active site as pH drops. (wikipedia.org)
  • Cathepsin D enzymatic activity induces hydrolytic modification of apolipoprotein B-100-containing lipoproteins, including LDL, which means it may be involved in atherosclerosis as well. (wikipedia.org)
  • The genetic knockout for cathepsin S and K in mice with atherosclerosis was shown to reduce the size of atherosclerotic lesions. (wikipedia.org)
  • Because cathepsins have harmful effects on critical proteins such as collagen and elastin, pharmaceutical companies have been developing drugs to inhibit activity of the enzymes, but so far these compounds have had too many side effects to be useful and have failed clinical trials. (innovations-report.com)
  • The work could affect not only the development of drugs to inhibit cathepsin activity, but could also lead to a better understanding of how the enzymes work together. (innovations-report.com)
  • If you are targeting this system pharmaceutically, you may not have the types or quantities of cathepsins that you expect, which could cause off-target binding and side effects that were not anticipated. (innovations-report.com)
  • Targeting cathepsin S induces tumor cell autophagy via the EGFR-ERK signaling pathway," Cancer Letters , vol. 317, no. 1, pp. 89-98, 2012. (hindawi.com)
  • Unlike some of the other cathepsins, cathepsin D has some protease activity at neutral pH. (wikipedia.org)
  • Finally, we tested the hypothesis that inhibiting cathepsin activity could block endometriosis lesion attachment and implantation in vivo. (nih.gov)
  • Mouse endometriotic lesions exhibit elevated cathepsin proteolytic activity. (nih.gov)
  • By increasing the amount of cathepsin S ten-fold over the amount used in the original experiment, Platt and Barry were able to completely block the activity of cathepsin K, preventing damage to the collagen sample. (innovations-report.com)
  • The selective demonstration of cathepsin B activity by means of the naphthylamide reaction. (springer.com)
  • We kept increasing the amount of cathepsin S until the collagen was not affected at all because all of the cathepsin K was eaten by the cathepsin S. (innovations-report.com)
  • Spinal cathepsin S and fractalkine contribute to chronic pain in the collagen-induced arthritis model," Arthritis and Rheumatism , vol. 64, no. 6, pp. 2038-2047, 2012. (hindawi.com)