C8511
Cathepsin C from bovine spleen
Type X, lyophilized powder, ≥5 units/mg protein
Synonyme(s) :
Dipeptidyl aminopeptidase, Dipeptidyl peptidase I
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About This Item
Produits recommandés
Source biologique
bovine spleen
Niveau de qualité
Type
Type X
Pureté
>25% protein (biuret)
Forme
lyophilized powder
Activité spécifique
≥5 units/mg protein
Composition
Protein, ≥25% biuret
Fabricant/nom de marque
Sigma-Aldrich
Conditions de stockage
OK to freeze (Unstable. Keep frozen)
Concentration
≥5 unit/mg protein
Technique(s)
activity assay: suitable
Adéquation
suitable for molecular biology
Application(s)
life science and biopharma
Conditions d'expédition
dry ice
Température de stockage
−20°C
Informations sur le gène
cow ... CTSC(352958)
Catégories apparentées
Description générale
Research Area: Cell Signaling
Dipeptidyl peptidase I (DPPI), also known as cathepsin C, is an abundant lysosomal cysteine protease from the papain superfamily with a molecular weight of approximately 200 kDa. It is widely expressed in a variety of mammalian tissues, with the highest levels found in the lungs, kidneys, liver, and spleen, and relatively lower levels in the brain.
DPPI is the only member of its family that is functional as a tetramer, consisting of four identical subunits, each composed of an N-terminal fragment, a heavy chain, and a light chain. It is identified as one of the multifaceted protease-processing machines, having been shown to function beyond its role as a non-specific lysosomal protease.
Dipeptidyl peptidase I (DPPI), also known as cathepsin C, is an abundant lysosomal cysteine protease from the papain superfamily with a molecular weight of approximately 200 kDa. It is widely expressed in a variety of mammalian tissues, with the highest levels found in the lungs, kidneys, liver, and spleen, and relatively lower levels in the brain.
DPPI is the only member of its family that is functional as a tetramer, consisting of four identical subunits, each composed of an N-terminal fragment, a heavy chain, and a light chain. It is identified as one of the multifaceted protease-processing machines, having been shown to function beyond its role as a non-specific lysosomal protease.
Application
Cathepsin C from bovine spleen has been used for the in vitro enzyme activity assays. It has also been used as a digestion enzyme for in vitro myelin oligodendrocyte glycoprotein (MOG) digestion.
Cathepsin C has been used in a study that demonstrated the potential of a proteomics approach to identify novel proteins expressed by extravillous trophoblast and to uncover the mechanisms leading to disease states in pregnancy. Cathepsin C has also been used in a study to evaluate biodegradable thermogels.
The enzyme from Sigma has been used in the activation of granzyme k (Gzmk) precursor from E. coli. Granzymes are granule-stored lymphocyte serine proteases that are implicated in T- and natural killer cell-mediated cytotoxic defense reactions.
Actions biochimiques/physiologiques
Cathepsin C (Cat C) serves as the physiological activator of groups of serine proteases within immune and inflammatory cells, playing a crucial role in the defense mechanisms of an organism. It may play a role in chronic airway diseases such as asthma. Cat C also acts as a protease link between inflammation and thrombosis.
Cat C participates in neutrophil recruitment and production of chemokines and cytokines in many inflammatory diseases. Cathepsin C plays a crucial role as an essential enzyme in activating granule serine proteases in cytotoxic T lymphocytes, natural killer cells (granzymes A and B), mast cells (chymase and tryptase), and neutrophils (cathepsin G, proteinase 3, and elastase).
Cat C participates in neutrophil recruitment and production of chemokines and cytokines in many inflammatory diseases. Cathepsin C plays a crucial role as an essential enzyme in activating granule serine proteases in cytotoxic T lymphocytes, natural killer cells (granzymes A and B), mast cells (chymase and tryptase), and neutrophils (cathepsin G, proteinase 3, and elastase).
Cathespin C is a dipeptidyl aminopeptidase that can sequentially remove dipeptides from a peptide chain with an unsubstituted N-terminus. The enzyme exhibits a preference for glycine and proline as N-terminal aminoacids. Substrates that have an N-terminal lysyl or arginyl residue, or a penultimate proryl residue are not targeted by this enzyme. The endopeptidase activity requires the presence of halide ions and sulfydryl activators.
Attention
Unstable. Keep frozen.
Définition de l'unité
One unit will produce 1 μmole of Gly-Phe-NHOH from Gly-Phe-NH2 and hydroxylamine per min at pH 6.8 at 37 °C using DL-phenylalanine hydroxamic acid as the standard. In addition to its hydrolytic properties, cathepsin C catalyzes the polymerization of dipeptide amides.
Forme physique
Lyophilized from a 1 M sodium chloride solution.
Substrat
Réf. du produit
Description
Tarif
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
Purification and properties of dipeptidyl transferase (Cathepsin C).
R M Metroione et al.
Biochemistry, 5(5), 1597-1604 (1966-05-01)
M Kuribayashi et al.
Journal of biochemistry, 113(4), 441-449 (1993-04-01)
By employing various synthetic substrates, as well as soluble denatured protein substrate (TAP-lysozyme) and its derivatives, endopeptidase activity of cathepsin C, dipeptidyl aminopeptidase I [EC 3.4.14.1], from bovine spleen was investigated. Cathepsin C efficiently degraded Z-Phe-Arg-MCA, Pro-Phe-Arg-MCA, and Suc-Leu-Leu-Val-Tyr-MCA. This
Christian D Sadik et al.
Clinical oral investigations, 16(2), 591-597 (2011-03-08)
Papillon-Lefèvre syndrome (PLS) is characterised by aggressively progressive periodontitis combined with palmo-plantar hyperkeratosis. It is caused by "loss of function" mutations in the cathepsin C gene. The hypothesis behind this study is that PLS patients' polymorphonuclear leukocytes (PMNs) produce more
Ellen Melaleuca Menkhorst et al.
PloS one, 7(2), e31418-e31418 (2012-02-24)
Inadequate or inappropriate implantation and placentation during the establishment of human pregnancy is thought to lead to first trimester miscarriage, placental insufficiency and other obstetric complications. To create the placental blood supply, specialized cells, the 'extravillous trophoblast' (EVT) invade through
Min Hee Park et al.
Accounts of chemical research, 45(3), 424-433 (2011-10-14)
All living creatures respond to external stimuli. Similarly, some polymers undergo conformational changes in response to changes in temperature, pH, magnetic field, electrical field, or the wavelength of light. In one type of stimuli-responsive polymer, thermogel polymers, the polymer aqueous
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