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C8511
Cathepsin C from bovine spleen
Type X, lyophilized powder, ≥5 units/mg protein
Sinónimos:
Dipeptidyl aminopeptidase, Dipeptidyl peptidase I
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origen biológico
bovine spleen
Nivel de calidad
tpo
Type X
Ensayo
>25% protein (biuret)
Formulario
lyophilized powder
actividad específica
≥5 units/mg protein
composición
Protein, ≥25% biuret
fabricante / nombre comercial
Sigma-Aldrich
condiciones de almacenamiento
OK to freeze (Unstable. Keep frozen)
concentración
≥5 unit/mg protein
Categorías relacionadas
Descripción general
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.[1] 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.[2]
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.[1]
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.[1] 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.[2]
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.[1]
Aplicación
Cathepsin C from bovine spleen has been used for the in vitro enzyme activity assays.[3] It has also been used as a digestion enzyme for in vitro myelin oligodendrocyte glycoprotein (MOG) digestion.[4]
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.[5]
Acciones bioquímicas o fisiológicas
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.[1]
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).[2]
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).[2]
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.[6] The endopeptidase activity requires the presence of halide ions and sulfydryl activators.[7]
Precaución
Unstable. Keep frozen.
Definición de unidad
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.
Forma física
Lyophilized from a 1 M sodium chloride solution.
sustrato
Referencia del producto
Descripción
Precios
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
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